(c) 1992-2000 Regents of the University of California, Santa Cruz
Sequence Alignment and Modeling Software System
http://www.soe.ucsc.edu/research/compbio/sam.html
Citations (SAM, SAM-T99, HMMs)
- R. Hughey, A. Krogh, Hidden Markov models for sequence analysis: Extension and analysis of the basic method, CABIOS 12:95-107, 1996.
- K. Karplus, C. Barrett, R. Hughey, Hidden Markov models for detecting remote protein homologies, Bioinformatics 14(10):846-856, 1998.
- A. Krogh et al., Hidden Markov models in computational biology: Applications to protein modeling, JMB 235:1501-1531, Feb 1994.
Sequence numbers correspond to the following labels:
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- T0346 PPI63, Homo sapiens, 172 res
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- gi|31615559|pdb|1M9E|B_3:164 Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex. [Taxonomy]
- gi|31615558|pdb|1M9E|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex [Taxonomy]
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- gi|2981764|pdb|1AWV|F_2:164 Chain F, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981763|pdb|1AWV|E Chain E, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981762|pdb|1AWV|D Chain D, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981761|pdb|1AWV|C Chain C, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981760|pdb|1AWV|B Chain B, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981759|pdb|1AWV|A Chain A, Cypa Complexed With Hvgpia [Taxonomy]
- gi|2981757|pdb|1AWU|A Chain A, Cypa Complexed With Hvgpia (Pseudo-Symmetric Monomer) [Taxonomy]
- gi|2981736|pdb|1AWR|F Chain F, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981735|pdb|1AWR|E Chain E, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981734|pdb|1AWR|D Chain D, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981733|pdb|1AWR|C Chain C, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981732|pdb|1AWR|B Chain B, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981731|pdb|1AWR|A Chain A, Cypa Complexed With Hagpia [Taxonomy]
- gi|2981729|pdb|1AWQ|A Chain A, Cypa Complexed With Hagpia (Pseudo-Symmetric Monomer) [Taxonomy]
- gi|1633054|pdb|5CYH|A Chain A, Cyclophilin A Complexed With Dipeptide Gly-Pro [Taxonomy]
- gi|1633056|pdb|4CYH|A Chain A, Cyclophilin A Complexed With Dipeptide His-Pro [Taxonomy]
- gi|1633058|pdb|3CYH|A Chain A, Cyclophilin A Complexed With Dipeptide Ser-Pro [Taxonomy]
- gi|1633063|pdb|2CYH|A Chain A, Cyclophilin A Complexed With Dipeptide Ala-Pro [Taxonomy]
- gi|1827593|pdb|1RMH|B Chain B, Recombinant Cyclophilin A From Human T Cell [Taxonomy]
- gi|1827592|pdb|1RMH|A Chain A, Recombinant Cyclophilin A From Human T Cell [Taxonomy]
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- gi|51895760|gb|AAU13906.1|_3:165 peptidylprolyl isomerase A (cyclophilin A) [Homo sapiens]
- gi|10863927|ref|NP_066953.1| peptidylprolyl isomerase A isoform 1 [Homo sapiens]
- gi|15530260|gb|AAH13915.1| Peptidylprolyl isomerase A, isoform 1 [Homo sapiens]
- gi|12653801|gb|AAH00689.1| Peptidylprolyl isomerase A, isoform 1 [Homo sapiens]
- gi|32425484|gb|AAH03026.2| Peptidylprolyl isomerase A, isoform 1 [Homo sapiens]
- gi|74136179|ref|NP_001027981.1| cyclophilin A [Macaca mulatta]
- gi|13529080|gb|AAH05320.1| Peptidylprolyl isomerase A, isoform 1 [Homo sapiens]
- gi|51702778|sp|P62941|PPIA_PAPAN Peptidyl-prolyl cis-trans isomerase A (PPIase A) (Rotamase A) (Cyclophilin A) (Cyclosporin A-binding protein) [Taxonomy]
- gi|51702777|sp|P62940|PPIA_MACMU Peptidyl-prolyl cis-trans isomerase A (PPIase A) (Rotamase A) (Cyclophilin A) (Cyclosporin A-binding protein) [Taxonomy]
- gi|51702775|sp|P62937|PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A (PPIase A) (Rotamase A) (Cyclophilin A) (Cyclosporin A-binding protein) [Taxonomy]
- gi|51702776|sp|P62938|PPIA_CERAE Peptidyl-prolyl cis-trans isomerase A (PPIase A) (Rotamase A) (Cyclophilin A) (Cyclosporin A-binding protein) [Taxonomy]
- gi|99031692|pdb|1ZKF|B Chain B, Cyrstal Structure Of Human Cyclophilin-A In Complex With Suc-Agpf-Pna [Taxonomy]
- gi|99031691|pdb|1ZKF|A Chain A, Cyrstal Structure Of Human Cyclophilin-A In Complex With Suc-Agpf-Pna [Taxonomy]
- gi|77415502|gb|AAI06031.1| Peptidylprolyl isomerase A, isoform 1 [Homo sapiens]
- gi|49522214|gb|AAH73992.1| PPIA protein [Homo sapiens]
- gi|2565303|gb|AAB81961.1| cyclophilin A [Macaca mulatta]
- gi|2565301|gb|AAB81960.1| cyclophilin A [Cercopithecus aethiops]
- gi|2565299|gb|AAB81959.1| cyclophilin A [Papio hamadryas]
- gi|62738675|pdb|1YND|B Chain B, Structure Of Human Cyclophilin A In Complex With The Novel Immunosuppressant Sanglifehrin A At 1.6a Resolution [Taxonomy]
- gi|62738674|pdb|1YND|A Chain A, Structure Of Human Cyclophilin A In Complex With The Novel Immunosuppressant Sanglifehrin A At 1.6a Resolution [Taxonomy]
- gi|3402110|pdb|1CWM|A Chain A, Human Cyclophilin A Complexed With 4 Meile Cyclosporin [Taxonomy]
- gi|30309|emb|CAA68264.1| unnamed protein product [Homo sapiens]
- gi|30168|emb|CAA37039.1| peptidylprolyl isomerase [Homo sapiens]
- gi|55670666|pdb|1W8V|A Chain A, Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes [Taxonomy]
- gi|55670664|pdb|1W8M|A Chain A, Enzymatic And Structural Characterisation Of Non Peptide Ligand Cyclophilin Complexes [Taxonomy]
- gi|55670663|pdb|1W8L|A Chain A, Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes [Taxonomy]
- gi|1431709|pdb|1MIK|A Chain A, The Role Of Water Molecules In The Structure-Based Design Of (5-Hydroxynorvaline)-2-Cyclosporin: Synthesis, Biological Activity, And Crystallographic Analysis With Cyclophilin A [Taxonomy]
- gi|29726709|pdb|1NMK|B Chain B, The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-Ray Crystal Structure And Binding Data [Taxonomy]
- gi|29726708|pdb|1NMK|A Chain A, The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-Ray Crystal Structure And Binding Data [Taxonomy]
- gi|31615580|pdb|1M9Y|F Chain F, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex. [Taxonomy]
- gi|31615579|pdb|1M9Y|E Chain E, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex. [Taxonomy]
- gi|31615576|pdb|1M9Y|B Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex. [Taxonomy]
- gi|31615575|pdb|1M9Y|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex. [Taxonomy]
- gi|31615572|pdb|1M9X|F Chain F, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex. [Taxonomy]
- gi|31615571|pdb|1M9X|E Chain E, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex. [Taxonomy]
- gi|31615568|pdb|1M9X|B Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex. [Taxonomy]
- gi|31615567|pdb|1M9X|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex. [Taxonomy]
- gi|31615563|pdb|1M9F|B Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex. [Taxonomy]
- gi|31615562|pdb|1M9F|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex. [Taxonomy]
- gi|31615555|pdb|1M9D|B Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) O-Type Chimera Complex. [Taxonomy]
- gi|31615554|pdb|1M9D|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) O-Type Chimera Complex. [Taxonomy]
- gi|31615551|pdb|1M9C|B Chain B, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex. [Taxonomy]
- gi|31615550|pdb|1M9C|A Chain A, X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex. [Taxonomy]
- gi|24987752|pdb|1MF8|C Chain C, Crystal Structure Of Human Calcineurin Complexed With Cyclosporin A And Human Cyclophilin [Taxonomy]
- gi|24158965|pdb|1M63|G Chain G, Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition Of Immunophilin-Drug Complexes [Taxonomy]
- gi|24158962|pdb|1M63|C Chain C, Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition Of Immunophilin-Drug Complexes [Taxonomy]
- gi|4389150|pdb|1VBT|B Chain B, Structure Of Cyclophilin Complexed With Sulfur-Substituted Tetrapeptide Aapf [Taxonomy]
- gi|4389149|pdb|1VBT|A Chain A, Structure Of Cyclophilin Complexed With Sulfur-Substituted Tetrapeptide Aapf [Taxonomy]
- gi|4389147|pdb|1VBS|A Chain A, Structure Of Cyclophilin Complexed With (D)ala Containing Tetrapeptide [Taxonomy]
- gi|2781284|pdb|1OCA| Human Cyclophilin A, Unligated, Nmr, 20 Structures [Taxonomy]
- gi|2098513|pdb|1FGL|A Chain A, Cyclophilin A Complexed With A Fragment Of Hiv-1 Gag Protein [Taxonomy]
- gi|3402109|pdb|1CWL|A Chain A, Human Cyclophilin A Complexed With 4 4-Hydroxy-Meleu Cyclosporin [Taxonomy]
- gi|3402108|pdb|1CWK|A Chain A, Human Cyclophilin A Complexed With 1-(6,7-Dihydro)mebmt 2-Val 3-D-(2-S-Methyl)sarcosine Cyclosporin [Taxonomy]
- gi|3660172|pdb|1CWJ|A Chain A, Human Cyclophilin A Complexed With 2-Val 3-S-Methyl-Sarcosine Cyclosporin [Taxonomy]
- gi|3660171|pdb|1CWI|A Chain A, Human Cyclophilin A Complexed With 2-Val 3-(N-Methyl)-D-Alanine Cyclosporin [Taxonomy]
- gi|3402107|pdb|1CWH|A Chain A, Human Cyclophilin A Complexed With 3-D-Ser Cyclosporin [Taxonomy]
- gi|3402106|pdb|1CWF|A Chain A, Human Cyclophilin A Complexed With 2-Val Cyclosporin [Taxonomy]
- gi|2624880|pdb|1AK4|B Chain B, Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid [Taxonomy]
- gi|2624879|pdb|1AK4|A Chain A, Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid [Taxonomy]
- gi|1000028|pdb|2RMB|S Chain S, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000027|pdb|2RMB|Q Chain Q, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000026|pdb|2RMB|O Chain O, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000025|pdb|2RMB|M Chain M, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000024|pdb|2RMB|K Chain K, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000023|pdb|2RMB|I Chain I, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000022|pdb|2RMB|G Chain G, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000021|pdb|2RMB|E Chain E, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000020|pdb|2RMB|C Chain C, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000019|pdb|2RMB|A Chain A, Cyclophilin A (E.C.5.2.1.8) Complexed With Dimethyl-Cyclosporin A [Taxonomy]
- gi|1000015|pdb|2RMA|S Chain S, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000014|pdb|2RMA|Q Chain Q, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000013|pdb|2RMA|O Chain O, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000012|pdb|2RMA|M Chain M, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000011|pdb|2RMA|K Chain K, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000010|pdb|2RMA|I Chain I, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000009|pdb|2RMA|G Chain G, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000008|pdb|2RMA|E Chain E, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000007|pdb|2RMA|C Chain C, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|1000006|pdb|2RMA|A Chain A, Cyclophilin A (E.C.5.2.1.8) Complexed With Cyclosporin A [Taxonomy]
- gi|443368|pdb|2CPL| Cyclophilin A [Taxonomy]
- gi|1310885|pdb|1CWC|A Chain A, Mol_id: 1; Molecule: Cyclophilin A; Chain: A; Engineered: Yes; Mol_id: 2; Molecule: [4,N-Dimethylnorleucine]4-Cyclosporin; Chain: C; Engineered: Yes [Taxonomy]
- gi|1310886|pdb|1CWB|A Chain A, Mol_id: 1; Molecule: Cyclophilin A; Chain: A; Engineered: Yes; Mol_id: 2; Molecule: [4-[(E)-2-Butenyl]-4,4,N-Trimethyl-L-Threonine]1- Cyclosporin; Chain: C; Engineered: Yes [Taxonomy]
- gi|1310887|pdb|1CWA|A Chain A, Mol_id: 1; Molecule: Cyclophilin A; Chain: A; Engineered: Yes; Mol_id: 2; Molecule: Cyclosporin A; Chain: C; Engineered: Yes [Taxonomy]
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- gi|3659980|pdb|1BCK|A_3:165 Chain A, Human Cyclophilin A Complexed With 2-Thr Cyclosporin [Taxonomy]
- gi|3660173|pdb|1CWO|A Chain A, Human Cyclophilin A Complexed With Thr2, Leu5, D-Hiv8, Leu10 Cyclosporin [Taxonomy]
- gi|1431788|pdb|3CYS|A Chain A, Cyclophilin A Complexed With Cyclosporin A (Nmr, 22 Structures) [Taxonomy]
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- gi|76626934|ref|XP_884582.1|_3:164 PREDICTED: similar to peptidylprolyl isomerase A isoform 1 isoform 3 [Bos taurus]
- gi|76626932|ref|XP_884549.1| PREDICTED: similar to peptidylprolyl isomerase A isoform 1 isoform 2 [Bos taurus]
- gi|76626930|ref|XP_872100.1| PREDICTED: similar to peptidylprolyl isomerase A isoform 1 isoform 1 [Bos taurus]
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- gi|55628504|ref|XP_519076.1|_56:218 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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- gi|55655642|ref|XP_531396.1|_43:205 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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- gi|55633521|ref|XP_507684.1|_34:196 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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- gi|76677439|ref|XP_586960.2|_7:178 PREDICTED: similar to peptidylprolyl isomerase G, partial [Bos taurus]
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- gi|50750469|ref|XP_422008.1|_7:178 PREDICTED: similar to peptidyl-prolyl isomerase G (cyclophilin G); Clk-associating RS-cyclophilin [Gallus gallus]
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- gi|94368329|ref|XP_997780.1|_7:178 PREDICTED: similar to peptidyl-prolyl isomerase G (cyclophilin G) [Mus musculus]
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- gi|1770526|emb|CAA68053.1|_7:178 SRcyp protein [Homo sapiens]
- gi|45477084|sp|Q13427|PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G (Peptidyl-prolyl isomerase G) (PPIase G) (Rotamase G) (Cyclophilin G) (Clk-associating RS-cyclophilin) (CARS-cyclophilin) (CARS-Cyp) (SR-cyclophilin) (SRcyp) (SR-cyp) (CASP10) [Taxonomy]
- gi|1117968|gb|AAB40347.1| CARS-Cyp [Taxonomy]
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- gi|55613873|ref|XP_515886.1|_7:178 PREDICTED: similar to peptidyl-prolyl isomerase G (cyclophilin G); Clk-associating RS-cyclophilin [Pan troglodytes]
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- gi|1345921|sp|P24525|CYPH_BRANA_3:171 Peptidyl-prolyl cis-trans isomerase (PPIase) (Rotamase) (Cyclophilin) (Cyclosporin A-binding protein) [Taxonomy]
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- gi|85075989|ref|XP_955863.1|_11:180 hypothetical protein ( (AJ292563) peptidyl-prolyl cis-trans isomerase [Neurospora crassa OR74A] ) [Taxonomy]
- gi|9558358|emb|CAC00484.1| peptidyl-prolyl cis-trans isomerase [Neurospora crassa]
- gi|46397046|sp|Q9P3X9|PPID_NEUCR 41 kDa peptidyl-prolyl cis-trans isomerase (PPIase) (Rotamase) (Cyclophilin-41) (CYP-41) [Taxonomy]
- gi|28916887|gb|EAA26627.1| hypothetical protein ( (AJ292563) peptidyl-prolyl cis-trans isomerase [Neurospora crassa] ) [Taxonomy]
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- gi|66534750|ref|XP_393381.2|_49:209 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase (PPIase) (Rotamase) (Cyclophilin) (Cyclosporin A-binding protein) [Apis mellifera]
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- gi|60594462|pdb|2BIU|X_3:165 Chain X, Crystal Structure Of Human Cyclophilin D At 1.7 A Resolution, Dmso Complex [Taxonomy]
- gi|60594461|pdb|2BIT|X Chain X, Crystal Structure Of Human Cyclophilin D At 1.7 A Resolution [Taxonomy]
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- gi|2190533|gb|AAC47543.1|_112:273 similar to Schistosoma japonicum cyclophylin, encoded by GenBank Accession Number M93420; Method: conceptual translation supplied by author [Taxonomy]
- gi|51701753|sp|Q26548|PPIE_SCHMA Peptidyl-prolyl cis-trans isomerase E (PPIase E) (Rotamase E) (Cyclophilin E) [Taxonomy]
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- gi|109089181|ref|XP_001090367.1|_45:207 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase, mitochondrial precursor (PPIase) (Rotamase) (Cyclophilin F) [Macaca mulatta]
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- gi|11514610|pdb|1QNG|A_3:170 Chain A, Plasmodium Falciparum Cyclophilin Complexed With Cyclosporin A [Taxonomy]
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- gi|94381275|ref|XP_918992.2|_75:236 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (SP18) [Mus musculus]
- gi|94381010|ref|XP_001002180.1| PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (SP18) [Mus musculus]
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- gi|76648210|ref|XP_884234.1|_6:177 PREDICTED: similar to natural killer-tumor recognition sequence isoform a isoform 8 [Bos taurus]
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- gi|76648204|ref|XP_884147.1|_6:177 PREDICTED: similar to natural killer-tumor recognition sequence isoform a isoform 5 [Bos taurus]
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- gi|76648214|ref|XP_884281.1|_6:177 PREDICTED: similar to natural killer-tumor recognition sequence isoform a isoform 9 [Bos taurus]
- gi|76648212|ref|XP_588972.2| PREDICTED: similar to natural killer-tumor recognition sequence isoform a isoform 1 [Bos taurus]
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- gi|8039799|sp|P30415|NKTR_MOUSE_6:177 NK-tumor recognition protein (Natural-killer cells cyclophilin-related protein) (NK-TR protein) [Taxonomy]
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- gi|74000478|ref|XP_535510.2|_2:163 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase B precursor (PPIase) (Rotamase) (Cyclophilin B) (S-cyclophilin) (SCYLP) (CYP-S1) isoform 1 [Canis familiaris]
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- gi|118090|sp|P23284|PPIB_HUMAN_35:198 Peptidyl-prolyl cis-trans isomerase B precursor (PPIase) (Rotamase) (Cyclophilin B) (S-cyclophilin) (SCYLP) (CYP-S1) [Taxonomy]
- gi|181335|gb|AAA52150.1| cyclophilin B [Taxonomy]
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- gi|1310882|pdb|1CYN|A_5:168 Chain A, Cyclophilin B Complexed With [d-(Cholinylester)ser8]-Cyclosporin [Taxonomy]
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-
- gi|11514613|pdb|1QNH|B_3:170 Chain B, Plasmodium Falciparum Cyclophilin (Double Mutant) Complexed With Cyclosporin A [Taxonomy]
- gi|11514612|pdb|1QNH|A Chain A, Plasmodium Falciparum Cyclophilin (Double Mutant) Complexed With Cyclosporin A [Taxonomy]
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-
- gi|76614948|ref|XP_868977.1|_3:164 PREDICTED: similar to peptidylprolyl isomerase A isoform 1 isoform 1 [Bos taurus]
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-
-
- gi|73976759|ref|XP_848739.1|_139:301 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase E (PPIase E) (Rotamase E) (Cyclophilin E) (Cyclophilin 33) isoform 2 [Canis familiaris]
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-
-
-
- gi|66361463|pdb|1ZCX|A_16:178 Chain A, Cyclophilin_abh_like Domain Of Peptidylprolyl Isomerase E Isoform 1 [homo Sapiens]
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-
-
-
-
- gi|76668068|ref|XP_586293.2|_88:250 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase E (PPIase E) (Rotamase E) (Cyclophilin E) (Cyclophilin 33) [Bos taurus]
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-
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-
-
-
- gi|50759473|ref|XP_417658.1|_10:177 PREDICTED: similar to peptidyl prolyl isomerase H; cyclophilin H; rotamase H [Gallus gallus]
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-
- gi|6730156|pdb|1C5F|O_6:177 Chain O, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730155|pdb|1C5F|M Chain M, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730154|pdb|1C5F|K Chain K, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730153|pdb|1C5F|I Chain I, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730152|pdb|1C5F|G Chain G, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730151|pdb|1C5F|E Chain E, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730150|pdb|1C5F|C Chain C, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|6730149|pdb|1C5F|A Chain A, Crystal Structure Of The Cyclophilin-Like Domain From Brugia Malayi Complexed With Cyclosporin A [Taxonomy]
- gi|3212364|pdb|1A58| Cyclophilin From Brugia Malayi [Taxonomy]
- gi|3402025|pdb|1A33| Peptidylprolyl Isomerase, Cyclophilin-Like Domain From Brugia Malayi [Taxonomy]
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-
- gi|8039801|sp|P48820|RBP2_BOVIN_924:1085 Ran-binding protein 2 (RanBP2) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (358 kDa nucleoporin) (P270) [Taxonomy]
- gi|1004090|gb|AAB00071.1| spliced variant with Ran-binding and cyclophilin domains [Taxonomy]
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-
- gi|73976761|ref|XP_856959.1|_126:288 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase E (PPIase E) (Rotamase E) (Cyclophilin E) (Cyclophilin 33) isoform 3 [Canis familiaris]
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-
- gi|72041630|ref|XP_797957.1|_16:179 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase B precursor (PPIase) (Rotamase) (Cyclophilin B) (S-cyclophilin) (SCYLP) (CYP-S1) [Strongylocentrotus purpuratus]
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-
- gi|55599754|ref|XP_515680.1|_19:180 PREDICTED: similar to Ran-binding protein 2 (RanBP2) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (358 kDa nucleoporin) (P270) [Pan troglodytes]
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-
- gi|6014889|sp|Q41651|CYPB_VICFA_81:245 Peptidyl-prolyl cis-trans isomerase, chloroplast precursor (PPIase) (Rotamase) (Cyclophilin) (Cyclosporin A-binding protein) (CYP B) [Taxonomy]
- gi|499693|gb|AAA64430.1| cyclophilin [Taxonomy]
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-
-
- gi|58177555|pdb|1XQ7|C_5:166 Chain C, Cyclophilin From Trypanosoma Cruzi Bound To Cyclosporin A [Taxonomy]
- gi|58177554|pdb|1XQ7|B Chain B, Cyclophilin From Trypanosoma Cruzi Bound To Cyclosporin A [Taxonomy]
- gi|58177553|pdb|1XQ7|A Chain A, Cyclophilin From Trypanosoma Cruzi Bound To Cyclosporin A [Taxonomy]
- gi|58177526|pdb|1XO7|D Chain D, Crystal Structure Of Cyclophilin From Trypanosoma Cruzi [Taxonomy]
- gi|58177525|pdb|1XO7|C Chain C, Crystal Structure Of Cyclophilin From Trypanosoma Cruzi [Taxonomy]
- gi|58177524|pdb|1XO7|B Chain B, Crystal Structure Of Cyclophilin From Trypanosoma Cruzi [Taxonomy]
- gi|58177523|pdb|1XO7|A Chain A, Crystal Structure Of Cyclophilin From Trypanosoma Cruzi [Taxonomy]
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-
-
- gi|76622682|ref|XP_615596.2|_191:354 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase C (PPIase) (Rotamase) (Cyclophilin C) [Bos taurus]
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-
- gi|109078374|ref|XP_001093271.1|_37:200 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase C (PPIase) (Rotamase) (Cyclophilin C) [Macaca mulatta]
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-
-
-
-
-
-
-
-
- gi|73970864|ref|XP_538601.2|_100:262 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase C (PPIase) (Rotamase) (Cyclophilin C) [Canis familiaris]
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- gi|73953719|ref|XP_853114.1|_8:152 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase, mitochondrial precursor (PPIase) (Rotamase) (Cyclophilin F) [Canis familiaris]
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-
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-
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-
-
- gi|55587036|ref|XP_524688.1|_10:193 PREDICTED: similar to peptidyl prolyl isomerase H; cyclophilin H; rotamase H [Pan troglodytes]
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-
-
-
-
- gi|55651470|ref|XP_525294.1|_14:175 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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-
-
-
-
- gi|55586874|ref|XP_513346.1|_139:282 PREDICTED: similar to peptidylprolyl isomerase E isoform 2; peptidyl-prolyl cis-trans isomerase E; cyclophilin 33; cyclophilin E; PPIase E; rotamase E [Pan troglodytes]
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-
-
- gi|62661794|ref|XP_341364.2|_3:165 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (P31) [Rattus norvegicus]
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-
- gi|73949630|ref|XP_535256.2|_486:645 PREDICTED: similar to peptidylprolyl isomerase domain and WD repeat containing 1 isoform 1 [Canis familiaris]
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-
- gi|88943444|ref|XP_933266.1|_3:164 PREDICTED: similar to peptidylprolyl isomerase A (cyclophilin A)-like 4 [Homo sapiens]
- gi|41116300|ref|XP_371302.1| PREDICTED: similar to peptidylprolyl isomerase A (cyclophilin A)-like 4 [Homo sapiens]
- gi|41107503|ref|XP_371304.1| PREDICTED: similar to peptidylprolyl isomerase A (cyclophilin A)-like 4 [Homo sapiens]
-
- gi|62642872|ref|XP_215474.3|_503:662 PREDICTED: similar to RIKEN cDNA 4632422M10 [Rattus norvegicus]
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-
-
- gi|55614513|ref|XP_516021.1|_68:229 PREDICTED: similar to peptidylprolyl isomerase-like protein 3 isoform PPIL3b; cyclophilin-like protein 3; peptidylprolyl cis-trans isomerase-like protein 3; PPIase-like protein 3 [Pan troglodytes]
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-
- gi|62738924|pdb|1Z81|A_59:229 Chain A, Crystal Structure Of Cyclophilin From Plasmodium Yoelii [Taxonomy]
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-
-
- gi|88943041|ref|XP_932799.1|_3:164 PREDICTED: similar to peptidylprolyl isomerase A (cyclophilin A)-like 4 [Homo sapiens]
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-
-
- gi|76629673|ref|XP_878562.1|_1:151 PREDICTED: similar to peptidyl prolyl isomerase H isoform 3 [Bos taurus]
-
- gi|109077400|ref|XP_001085845.1|_486:645 PREDICTED: similar to peptidylprolyl isomerase domain and WD repeat containing 1 [Macaca mulatta]
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-
-
- gi|71042631|pdb|2A2N|C_16:175 Chain C, Crystal Structure Of The Peptidylprolyl Isomerase Domain Of Human Ppwd1 [Taxonomy]
- gi|71042630|pdb|2A2N|B Chain B, Crystal Structure Of The Peptidylprolyl Isomerase Domain Of Human Ppwd1 [Taxonomy]
- gi|71042629|pdb|2A2N|A Chain A, Crystal Structure Of The Peptidylprolyl Isomerase Domain Of Human Ppwd1 [Taxonomy]
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-
- gi|75765773|pdb|1ZKC|B_12:175 Chain B, Crystal Structure Of The Cyclophiln_ring Domain Of Human Peptidylprolyl Isomerase (Cyclophilin)-Like 2 Isoform B [Taxonomy]
- gi|75765772|pdb|1ZKC|A Chain A, Crystal Structure Of The Cyclophiln_ring Domain Of Human Peptidylprolyl Isomerase (Cyclophilin)-Like 2 Isoform B [Taxonomy]
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-
-
- gi|82407487|pdb|1XWN|A_6:166 Chain A, Solution Structure Of Cyclophilin Like 1(Ppil1) And Insights Into Its Interaction With Skip [Taxonomy]
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- gi|85112648|ref|XP_964379.1|_12:180 hypothetical protein ( (X17692) cyclophilin (cytosolic form) [Neurospora crassa OR74A] ) [Taxonomy]
- gi|295927|emb|CAA35682.1| cyclophilin (cytosolic form) [Neurospora crassa]
- gi|28926159|gb|EAA35143.1| hypothetical protein ( (X17692) cyclophilin (cytosolic form) [Neurospora crassa] ) [Taxonomy]
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-
- gi|90108954|pdb|2C3B|B_8:172 Chain B, The Crystal Structure Of Aspergillus Fumigatus Cyclophilin Reveals 3d Domain Swapping Of A Central Element [Taxonomy]
- gi|90108953|pdb|2C3B|A Chain A, The Crystal Structure Of Aspergillus Fumigatus Cyclophilin Reveals 3d Domain Swapping Of A Central Element [Taxonomy]
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-
- gi|56554362|pdb|1W74|B_18:190 Chain B, X-Ray Structure Of Peptidyl-Prolyl Cis-Trans Isomerase A, Ppia, Rv0009, From Mycobacterium Tuberculosis. [Taxonomy]
- gi|56554361|pdb|1W74|A Chain A, X-Ray Structure Of Peptidyl-Prolyl Cis-Trans Isomerase A, Ppia, Rv0009, From Mycobacterium Tuberculosis [Taxonomy]
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-
-
- gi|66534975|ref|XP_624114.1|_1:161 PREDICTED: similar to Peptidylprolyl isomerase-like protein 3, isoform PPIL3b [Apis mellifera]
-
-
-
-
-
-
- gi|62652001|ref|XP_345811.2|_27:188 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (SP18) [Rattus norvegicus]
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-
- gi|94396360|ref|XP_986172.1|_7:168 PREDICTED: similar to serologically defined colon cancer antigen 10 (predicted) isoform 3 [Mus musculus]
- gi|82952494|ref|XP_924619.1| PREDICTED: similar to serologically defined colon cancer antigen 10 (predicted) isoform 5 [Mus musculus]
- gi|51767901|ref|XP_127535.3| PREDICTED: serologically defined colon cancer antigen 10 isoform 1 [Mus musculus]
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-
-
-
-
- gi|55624250|ref|XP_526904.1|_3:165 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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-
- gi|94389141|ref|XP_999860.1|_143:312 PREDICTED: similar to peptidylprolyl isomerase (cyclophilin)-like 6 isoform 2 [Mus musculus]
- gi|82932803|ref|XP_913438.1| PREDICTED: similar to peptidylprolyl isomerase (cyclophilin)-like 6 isoform 3 [Mus musculus]
- gi|82932250|ref|XP_896765.1| PREDICTED: peptidylprolyl isomerase (cyclophilin)-like 6 isoform 1 [Mus musculus]
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-
-
- gi|73949620|ref|XP_535254.2|_7:168 PREDICTED: similar to serologically defined colon cancer antigen 10 (predicted) isoform 1 [Canis familiaris]
-
-
- gi|76689443|ref|XP_875959.1|_6:162 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase-like 1 (PPIase) (Rotamase) [Bos taurus]
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-
-
- gi|76562485|gb|ABA45069.1|_279:466 Cof-like hydrolase/peptidyl-prolyl cis-trans isomerase domain protein [Streptococcus agalactiae A909]
- gi|22533338|gb|AAM99229.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae 2603V/R]
- gi|22536506|ref|NP_687357.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae 2603V/R]
- gi|76787428|ref|YP_329045.1| Cof-like hydrolase/peptidyl-prolyl cis-trans isomerase domain protein [Streptococcus agalactiae A909]
- gi|77410633|ref|ZP_00786993.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae CJB111]
- gi|77404987|ref|ZP_00782088.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae H36B]
- gi|77176426|gb|EAO79194.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae H36B]
- gi|77163348|gb|EAO74299.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae CJB111]
- gi|76797817|ref|ZP_00780082.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae 18RS21]
- gi|76586831|gb|EAO63324.1| hydrolase, haloacid dehalogenase family/peptidyl-prolyl cis-trans isomerase, cyclophilin type [Streptococcus agalactiae 18RS21]
-
-
-
- gi|62649835|ref|XP_575932.1|_16:151 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (SP18) [Rattus norvegicus]
-
- gi|118112|sp|P28517|CYPR_CALVI_25:189 Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme precursor (PPIase) (Rotamase) [Taxonomy]
-
-
-
- gi|76661399|ref|XP_596750.2|_105:241 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase A (PPIase) (Rotamase) (Cyclophilin A) (Cyclosporin A-binding protein) (P31) [Bos taurus]
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-
-
- gi|76614946|ref|XP_876629.1|_3:131 PREDICTED: similar to peptidylprolyl isomerase A isoform 1 isoform 2 [Bos taurus]
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-
-
-
-
-
-
- gi|90109652|pdb|2FU0|A_8:160 Chain A, Plasmodium Falciparum Cyclophilin Pfe0505w Putative Cyclosporin-Binding Domain [Taxonomy]
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-
- gi|109081476|ref|XP_001106524.1|_11:160 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase B precursor (PPIase) (Rotamase) (Cyclophilin B) (S-cyclophilin) (SCYLP) (CYP-S1) isoform 1 [Macaca mulatta]
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-
-
-
-
-
-
-
-
-
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-
-
-
- gi|91082943|ref|XP_973192.1|_13:177 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme precursor (PPIase) (Rotamase) [Tribolium castaneum]
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-
- gi|55644695|ref|XP_523512.1|_17:155 PREDICTED: similar to peptidylprolyl isomerase A isoform 1; cyclophilin A; peptidyl-prolyl cis-trans isomerase A; T cell cyclophilin; rotamase; cyclosporin A-binding protein [Pan troglodytes]
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-
- gi|46014891|pdb|1J2A|A_5:166 Chain A, Structure Of E. Coli Cyclophilin B K163t Mutant [Taxonomy]
- gi|55670419|pdb|1VAI|B Chain B, Structure Of E. Coli Cyclophilin B K163t Mutant Bound To N- Acetyl-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin [Taxonomy]
- gi|55670418|pdb|1VAI|A Chain A, Structure Of E. Coli Cyclophilin B K163t Mutant Bound To N- Acetyl-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin [Taxonomy]
- gi|55670414|pdb|1V9T|B Chain B, Structure Of E. Coli Cyclophilin B K163t Mutant Bound To Succinyl-Ala-Pro-Ala-P-Nitroanilide [Taxonomy]
- gi|55670413|pdb|1V9T|A Chain A, Structure Of E. Coli Cyclophilin B K163t Mutant Bound To Succinyl-Ala-Pro-Ala-P-Nitroanilide [Taxonomy]
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-
- gi|93140605|sp|Q4WVU5|PPIL2_ASPFU_307:472 Peptidyl-prolyl cis-trans isomerase-like 2 (PPIase) (Rotamase) (Cyclophilin-60) (Cyclophilin-like protein Cyp-60) [Taxonomy]
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- gi|76629679|ref|XP_878851.1|_2:147 PREDICTED: similar to peptidyl prolyl isomerase H isoform 5 [Bos taurus]
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- gi|76562748|gb|ABA45332.1|_68:262 peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae A909]
- gi|22534561|gb|AAN00397.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae 2603V/R]
- gi|22537673|ref|NP_688524.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae 2603V/R]
- gi|76787691|ref|YP_330159.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae A909]
- gi|24413167|emb|CAD47245.1| Unknown [Streptococcus agalactiae NEM316]
- gi|25011627|ref|NP_736022.1| hypothetical protein gbs1586 [Streptococcus agalactiae NEM316]
- gi|77412534|ref|ZP_00788830.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae CJB111]
- gi|77409242|ref|ZP_00785950.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae COH1]
- gi|77406842|ref|ZP_00783872.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae H36B]
- gi|77174554|gb|EAO77393.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae H36B]
- gi|77172155|gb|EAO75316.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae COH1]
- gi|77161419|gb|EAO72434.1| peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Streptococcus agalactiae CJB111]
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- gi|75855568|ref|ZP_00763215.1|_1:161 COG0652: Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Vibrio sp. Ex25]
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- gi|55634027|ref|XP_507866.1|_45:162 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase, mitochondrial precursor (PPIase) (Rotamase) (Cyclophilin F) [Pan troglodytes]
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- gi|76610205|ref|XP_872672.1|_1:130 PREDICTED: similar to peptidylprolyl isomerase-like protein 3 isoform PPIL3b, partial [Bos taurus]
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- gi|1942801|pdb|1LOP|A_1:164 Chain A, Cyclophilin A Complexed With Succinyl-Ala-Pro-Ala-P-Nitroanilide [Taxonomy]
- gi|145290|gb|AAA23453.1| peptidyl-prolyl cis-trans isomerase b [Taxonomy]
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- gi|109077392|ref|XP_001087046.1|_7:132 PREDICTED: similar to serologically defined colon cancer antigen 10, partial [Macaca mulatta]
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- gi|91078016|ref|XP_970035.1|_191:356 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase 7 (PPIase) (Rotamase) (Cyclophilin-7) [Tribolium castaneum]
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- gi|55624338|ref|XP_517773.1|_3:140 PREDICTED: similar to cyclophilin-LC; cyclophilin homolog overexpressed in liver cancer; chromosome 1 amplified sequence 2 [Pan troglodytes]
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- gi|55627558|ref|XP_527529.1|_262:422 PREDICTED: similar to peptidylprolyl isomerase-like 4; serologically defined breast cancer antigen NY-BR-18; PPIase; cyclophilin-type peptidyl-prolyl cis-trans isomerase [Pan troglodytes]
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- gi|76671199|ref|XP_878825.1|_3:163 PREDICTED: similar to peptidylprolyl isomerase-like 4 isoform 3 [Bos taurus]
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- gi|76671201|ref|XP_615786.2|_3:163 PREDICTED: similar to peptidylprolyl isomerase-like 4 isoform 1 [Bos taurus]
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- gi|76671197|ref|XP_878729.1|_3:163 PREDICTED: similar to peptidylprolyl isomerase-like 4 isoform 2 [Bos taurus]
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- gi|74000472|ref|XP_865596.1|_1:106 PREDICTED: similar to Peptidyl-prolyl cis-trans isomerase B precursor (PPIase) (Rotamase) (Cyclophilin B) (S-cyclophilin) (SCYLP) (CYP-S1) isoform 3 [Canis familiaris]
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- gi|62666037|ref|XP_215401.3|_2949:3065 PREDICTED: similar to Ran-binding protein 2 [Rattus norvegicus]
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- gi|75856128|ref|ZP_00763762.1|_14:181 COG0652: Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Vibrio sp. Ex25]
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