LOCUS 2500651 367 aa 01-NOV-1997 DEFINITION RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 2500651 PID g2500651 DBSOURCE SWISS-PROT: locus RTC1_YEAST, accession Q08096 class: standard. created: Nov 1, 1997. sequence updated: Nov 1, 1997. annotation updated: Nov 1, 1997. xrefs: gi: 1419778 xrefs (non-sequence databases): PROSITE PS01287 KEYWORDS LIGASE; NUCLEAR PROTEIN. SOURCE baker's yeast. ORGANISM Saccharomyces cerevisiae Eukaryotae; Fungi; Ascomycota; Hemiascomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. REFERENCE 1 (residues 1 to 367) AUTHORS HUGHES,B. and POHL,T.M. TITLE Direct Submission JOURNAL Submitted (??-JUL-1996) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A. REFERENCE 2 (residues 1 to 367) AUTHORS GENSCHIK,P., BILLY,E., SWIANIEWICZ,M. and FILIPOWICZ,W. JOURNAL Unpublished REMARK CHARACTERIZATION. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING. [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] NUCLEAR (POTENTIAL). FEATURES Location/Qualifiers source 1..367 /organism="Saccharomyces cerevisiae" /db_xref="taxon:4932" 1..367 Protein 1..367 /product="RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" ORIGIN 1 msssapkytt fqgsqnfrlr ivlatlsgkp ikiekirsgd lnpglkdyev sflrliesvt 61 ngsvieisyt gttviyrpgi ivggasthic psskpvgyfv epmlylapfs kkkfsilfkg 121 itashndagi eaikwglmpv mekfgvreca lhtlkrgspp lgggevhlvv dsliaqpitm 181 heidrpiiss itgvaystrv spslvnrmid gakkvlknlq cevnitadvw rgensgkspg 241 wgitlvaqsk qkgwsyfaed igdagsipee lgekvacqll eeisksaavg rnqlplaivy 301 mvigkedigr lrinkeqide rfiillrdik kifntevflk pvdeadnedm iatikgigft 361 ntskkia //
Other Formats: Links:
LOCUS 1351630 363 aa 01-NOV-1997 DEFINITION PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 1351630 PID g1351630 DBSOURCE SWISS-PROT: locus RTC1_SCHPO, accession Q09870 class: standard. created: Feb 1, 1996. sequence updated: Feb 1, 1996. annotation updated: Nov 1, 1997. xrefs: gi: 1052518 xrefs (non-sequence databases): PROSITE PS01287 KEYWORDS LIGASE; NUCLEAR PROTEIN. SOURCE fission yeast. ORGANISM Schizosaccharomyces pombe Eukaryotae; Fungi; Ascomycota; Archiascomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces. REFERENCE 1 (residues 1 to 363) AUTHORS DEVLIN,K., ODELL,C., CHURCHER,C.M., BARRELL,B.G., RAJANDREAM,M.A. and WALSH,S.V. TITLE Direct Submission JOURNAL Submitted (??-NOV-1995) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A. STRAIN=972 COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING (BY SIMILARITY). [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] NUCLEAR (POTENTIAL). [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. FEATURES Location/Qualifiers source 1..363 /organism="Schizosaccharomyces pombe" /db_xref="taxon:4896" 1..363 Protein 1..363 /product="PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" ORIGIN 1 mstgqlkrfk gceylthrlv latlsgtpir vegiypdead pgvkdyqvsf lrllekltng 61 svieisytgt sfiyrpgnii ggrvvhdcpt tkgigyflep ililclfakt ptsltltgvt 121 ssnedigvdv lrtsvlpslq krfqvgdele lrilkrgsap ggggevnflc pvikeslppi 181 rlsefgrvfr irgiasstrv spafanrlve sargvlnpfi pdvfiytdvr rgdecgnspg 241 ysitlvaetn kgcsyaaehc geagetpedv gsfcakklle viesggcvdp ytqpstltgm 301 llssedvnti vvgqlgitsq lvvflrdvka lfnceyrfke lesgqvemsc lgkgylnvnr 361 riq //
LOCUS 2500650 379 aa 01-NOV-1997 DEFINITION PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 2500650 PID g2500650 DBSOURCE SWISS-PROT: locus RTC1_CAEEL, accession Q23400 class: standard. created: Nov 1, 1997. sequence updated: Nov 1, 1997. annotation updated: Nov 1, 1997. xrefs: gi: 1330371, gi: 1330376 xrefs (non-sequence databases): WORMPEP ZK1127.5, PROSITE PS01287 KEYWORDS LIGASE; NUCLEAR PROTEIN. SOURCE Caenorhabditis elegans. ORGANISM Caenorhabditis elegans Eukaryotae; Metazoa; Nematoda; Secernentea; Rhabditia; Rhabditida; Rhabditina; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. REFERENCE 1 (residues 1 to 379) AUTHORS DU,Z. TITLE Direct Submission JOURNAL Submitted (??-MAY-1996) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A. STRAIN=BRISTOL N2 REFERENCE 2 (residues 1 to 379) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16 (10), 2955-2967 (1997) MEDLINE 97327572 REMARK CONCEPTUAL TRANSLATION. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING (BY SIMILARITY). [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] NUCLEAR (POTENTIAL). [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. FEATURES Location/Qualifiers source 1..379 /organism="Caenorhabditis elegans" /db_xref="taxon:6239" 1..379 Protein 1..379 /product="PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" ORIGIN 1 mssetlefsg cnffrirlay silsgrpiri inirknddrp girdfeskli gllekvtngt 61 kveisrtgtq vifrpgmitg gvvnldcgte rcisyflepl lllspfckvp mviklkgvtn 121 apgeisvdgm kaswlkvynk fvlndekldi kiqarglkpe gggvvvftap ivktlrpvkr 181 qqvgkvckir gqayvtkvtp slayrmidaa kkamhgyisd vyitvdqrkg daggaspgyg 241 lfltaetteg viyqaeaisr pkgesgvpil pedigieagh allqqiymgg aldssaqila 301 stfmtlcpkd vshflygplp mysvhalrhl kqffeiefkm edfkktlkee eadlktgsad 361 kamvtavgvg ysnlnktil //
LOCUS 2500652 338 aa 01-NOV-1997 DEFINITION PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 2500652 PID g2500652 DBSOURCE SWISS-PROT: locus RTCA_METJA, accession Q60335 class: standard. created: Nov 1, 1997. sequence updated: Nov 1, 1997. annotation updated: Nov 1, 1997. xrefs: gi: 1590827, gi: 1498784 xrefs (non-sequence databases): PROSITE PS01287, TIGR MJ0025 KEYWORDS LIGASE. SOURCE Methanococcus jannaschii. ORGANISM Methanococcus jannaschii Archaea; Euryarchaeota; Methanococcales; Methanococcaceae; Methanococcus. REFERENCE 1 (residues 1 to 338) AUTHORS BULT,C.J., WHITE,O., OLSEN,G.J., ZHOU,L., FLEISCHMANN,R.D., SUTTON,G.G., BLAKE,J.A., FITZGERALD,L.M., CLAYTON,R.A., GOCAYNE,J.D., KERLAVAGE,A.R., DOUGHERTY,B.A., TOMB,J.-F., ADAMS,M.D., REICH,C.I., OVERBEEK,R., KIRKNESS,E.F., WEINSTOCK,K.G., MERRICK,J.M., GLODEK,A., SCOTT,J.L., GEOGHAGEN,N.S.M., WEIDMAN,J.F., FUHRMANN,J.L., NGUYEN,D., UTTERBACK,T.R., KELLEY,J.M., PETERSON,J.D., SADOW,P.W., HANNA,M.C., COTTON,M.D., ROBERTS,K.M., HURST,M.A., KAINE,B.P., BORODOVSKY,M., KLENK,H.-P., FRASER,C.M., SMITH,H.O., WOESE,C.R. and VENTER,J.C. TITLE Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii JOURNAL Science 273 (5278), 1058-1073 (1996) MEDLINE 96337999 REMARK SEQUENCE FROM N.A. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING (BY SIMILARITY). [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. FEATURES Location/Qualifiers source 1..338 /organism="Methanococcus jannaschii" /db_xref="taxon:2190" 1..338 Protein 1..338 /product="PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" ORIGIN 1 mdfividgsy legggqiirt avslsaltqk pvkiinirkk rknkglapqh vsavkavkkl 61 cnaevfglnv gseeltfips klspkdftid igtagsislv iqtllplslg inkkftvkik 121 ggtdvkrapp idyvknvtlk ilrnfgvlte lkvlkrgfyp egggevifev kpskikkfdl 181 iehsksnlve gisyvqnlde siarrmrkka vdllnkekll pnikiecskg istgagivlw 241 ndtlggsclg ekglraeiva eravnellke resgmaldky mgdqiipfla fgkgivgvse 301 itnhtktnmw vvkhfldvdf eikeykennc ngftievv //
LOCUS 2500648 366 aa 01-FEB-1998 DEFINITION RNA 3'-TERMINAL PHOSPHATE CYCLASE 1 (RNA-3'-PHOSPHATE CYCLASE 1) (RNA CYCLASE 1). ACCESSION 2500648 PID g2500648 DBSOURCE SWISS-PROT: locus RTC1_HUMAN, accession O00442 class: standard. created: Nov 1, 1997. sequence updated: Nov 1, 1997. annotation updated: Feb 1, 1998. xrefs: gi: 2125811, gi: 2125809 xrefs (non-sequence databases): PROSITE PS01287 KEYWORDS LIGASE; NUCLEAR PROTEIN. SOURCE human. ORGANISM Homo sapiens Eukaryotae; Metazoa; Chordata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 366) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16 (10), 2955-2967 (1997) MEDLINE 97327572 REMARK SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. TISSUE=BLOOD REFERENCE 2 (residues 1 to 366) AUTHORS Filipowicz,W. and Vicente,O. TITLE RNA 3'-terminal phosphate cyclase from HeLa cells JOURNAL Meth. Enzymol. 181, 499-510 (1990) MEDLINE 90340098 REMARK CHARACTERIZATION. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING. [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBUNIT] MONOMER. [SUBCELLULAR LOCATION] NUCLEAR. [TISSUE SPECIFICITY] UBIQUITOUS. [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. FEATURES Location/Qualifiers source 1..366 /organism="Homo sapiens" /db_xref="taxon:9606" 1..366 Protein 1..366 /product="RNA 3'-TERMINAL PHOSPHATE CYCLASE 1" /EC_number="6.5.1.4" ORIGIN 1 magprvevdg simegggqil rvstalscll glplrvqkir agrstpglrp qhlsglemir 61 dlcdgqlega eigsteitft pekikggiht adtktagsvc llmqvsmpcv lfaaspselh 121 lkggtnaema pqidytvmvf kpivekfgfi fncdiktrgy ypkgggeviv rmspvkqlnp 181 inltergcvt kiygrafvag vlpfkvakdm aaaavrcirk eirdlyvniq pvqepkdqaf 241 gngngiiiia etstgclfag sslgkrgvna dkvgieaaem llanlrhggt vdeylqdqli 301 vfmalangvs riktgpvtlh tqtaihfaeq iakakfivkk sedeedaakd tyiiecqgig 361 mtnpnl //
LOCUS 2500649 235 aa 01-NOV-1997 DEFINITION PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 2500649 PID g2500649 DBSOURCE SWISS-PROT: locus RTC1_DROME, accession P56175 class: standard. created: Nov 1, 1997. sequence updated: Nov 1, 1997. annotation updated: Nov 1, 1997. xrefs: gi: 8844 xrefs (non-sequence databases): FLYBASE FBgn00?????, PROSITE PS01287 KEYWORDS LIGASE; NUCLEAR PROTEIN. SOURCE fruit fly. ORGANISM Drosophila melanogaster Eukaryotae; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; Pterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila. REFERENCE 1 (residues 1 to 235) AUTHORS Yan,Y.L., Kunert,C.J. and Postlethwait,J.H. TITLE Sequence homologies among the three yolk polypeptide (Yp) genes in Drosophila melanogaster JOURNAL Nucleic Acids Res. 15 (1), 67-85 (1987) MEDLINE 87146365 REMARK SEQUENCE FROM N.A. REFERENCE 2 (residues 1 to 235) AUTHORS Garabedian,M.J., Shirras,A.D., Bownes,M. and Wensink,P.C. TITLE The nucleotide sequence of the gene coding for Drosophila melanogaster yolk protein 3 JOURNAL Gene 55 (1), 1-8 (1987) MEDLINE 87305580 REMARK SEQUENCE FROM N.A. REFERENCE 3 (residues 1 to 235) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16 (10), 2955-2967 (1997) MEDLINE 97327572 REMARK IDENTIFICATION, AND CONCEPTUAL TRANSLATION. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING (BY SIMILARITY). [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] NUCLEAR (POTENTIAL). [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. [CAUTION] THIS IS A CONCEPTUAL TRANSLATION; TWO PUTATIVE INTRONS WERE REMOVED TO PRODUCES THIS ORF. FEATURES Location/Qualifiers source 1..235 /organism="Drosophila melanogaster" /db_xref="taxon:7227" 1..235 Protein <1..235 /product="PROBABLE RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" Region 16..19 /note="PLGG -> SAGR (IN REF. 2)." /region_name="Conflict" ORIGIN 1 vdeglelkvv rrgvaplggg eiifrcpvrk slraiqfqsq gmvkrirgtv yackvspama 61 nrtveaakgc mlkflpdvyi ytdqnkgkms gnspgfgicl iaettdgvcf aadccsntre 121 esedtpsipe nlgkevalrl ldeiyrggcv dssyqwlaal yialgqkhvs kfltgalsny 181 tvhflqhlrd ffsitfklen peaededeae nvrgaqkvlm acvgigytni nkrvi //
LOCUS 2507354 339 aa 01-NOV-1997 DEFINITION RNA 3'-TERMINAL PHOSPHATE CYCLASE (RNA-3'-PHOSPHATE CYCLASE) (RNA CYCLASE). ACCESSION 2507354 PID g2507354 DBSOURCE SWISS-PROT: locus RTCA_ECOLI, accession P46849 class: standard. extra accessions:P46848,Q47349,created: Nov 1, 1995. sequence updated: Nov 1, 1997. annotation updated: Nov 1, 1997. xrefs: gi: 606010, gi: 606355, gi: 2367222, gi: 1789826, gi: 146716, gi: 1128963 xrefs (non-sequence databases): ECOGENE EG12938, PROSITE PS01287 KEYWORDS LIGASE. SOURCE Escherichia coli. ORGANISM Escherichia coli Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 339) AUTHORS BLATTNER,F.R., PLUNKETT,G. III, MAYHEW,G.F., PERNA,N.T. and GLASNER,F.D. TITLE Direct Submission JOURNAL Submitted (??-JAN-1997) TO EMBL/GENBANK/DDBJ DATA BANKS REMARK SEQUENCE FROM N.A. STRAIN=K12 / MG1655 REFERENCE 2 (residues 1 to 339) AUTHORS Cole,S.T. and Raibaud,O. TITLE The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon JOURNAL Gene 42 (2), 201-208 (1986) MEDLINE 86275993 REMARK SEQUENCE OF 149-339 FROM N.A. STRAIN=K12 REFERENCE 3 (residues 1 to 339) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16 (10), 2955-2967 (1997) MEDLINE 97327572 REMARK REVISION, AND CHARACTERIZATION. COMMENT [FUNCTION] CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'-CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING. [CATALYTIC ACTIVITY] ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. [SUBCELLULAR LOCATION] CYTOPLASMIC (POTENTIAL). [SIMILARITY] BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. [CAUTION] REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A FRAMESHIFT IN POSITION 122 THAT PRODUCES TWO SEPARATE ORFS. FEATURES Location/Qualifiers source 1..339 /organism="Escherichia coli" /db_xref="taxon:562" 1..339 Protein 1..339 /product="RNA 3'-TERMINAL PHOSPHATE CYCLASE" /EC_number="6.5.1.4" ORIGIN 1 mmkrmialdg aqgegggqil rsalslsmit gqpftitsir agrakpgllr qhltavkaat 61 eicgatvega elgsqrllfr pgtvrggdyr faigsagsct lvlqtvlpal wfadgpsrve 121 vsggtdnpsa ppadfirrvl epllakigih qqttllrhgf ypagggvvat evspvasfnt 181 lqlgergniv qmrgevllag vprhvaerei atlagsfslh eqnihnlprd qgpgntvsle 241 veseniterf fvvgekrvsa evvaaqlvke vkrylastaa vgeyladqlv lpmalagage 301 ftvahpschl ltniavverf lpvrfsliet dgvtrvsie //
LOCUS 2125812 366 aa 27-MAY-1997 DEFINITION phosphate cyclase. ACCESSION 2125812 PID g2125812 DBSOURCE EMBL: locus HSPHOSCYC, accession Y11651 KEYWORDS . SOURCE human. ORGANISM Homo sapiens Eukaryotae; mitochondrial eukaryotes; Metazoa; Chordata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 366) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16, 2955-2967 (1997) REFERENCE 2 (residues 1 to 366) AUTHORS Filipowicz,W. TITLE Direct Submission JOURNAL Submitted (05-MAR-1997) W. Filipowicz, Friedrich Miescher Institut, PO Box 2543, 4002 Basel, SWITZERLAND FEATURES Location/Qualifiers source 1..366 /organism="Homo sapiens" /db_xref="taxon:9606" /cell_line="HeLa" /clone_lib="Lambda gt11" Protein 1..366 /product="phosphate cyclase" CDS 1..366 /coded_by="Y11651:171..1271" ORIGIN 1 magprvevdg simegggqil rvstalscll glplrvqkir agrstpglrp qhlsglemir 61 dlcdgqlega eigsteitft pekikggiht adtktagsvc llmqvsmpcv lfaaspselh 121 lkggtnaema pqidytvmvf kpivekfgfi fncdiktrgy ypkgggeviv rmspvkqlnp 181 inltergcvt kiygrafvag vlpfkvakdm aaaavrcirk eirdlyvniq pvqepkdqaf 241 gngngiiiia etstgclfag sslgkrgvna dkvgieaaem llanlrhggt vdeylqdqli 301 vfmalangvs riktgpvtlh tqtaihfaeq iakakfivkk sedeedaakd tyiiecqgig 361 mtnpnl //
LOCUS 2125810 48 aa 27-MAY-1997 DEFINITION phosphate cyclase. ACCESSION 2125810 PID g2125810 DBSOURCE EMBL: locus HSPHCYCEX, accession Y11652 KEYWORDS . SOURCE human. ORGANISM Homo sapiens Eukaryotae; mitochondrial eukaryotes; Metazoa; Chordata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 48) AUTHORS Genschik,P., Billy,E., Swianiewicz,M. and Filipowicz,W. TITLE The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea JOURNAL EMBO J. 16, 2955-2967 (1997) REFERENCE 2 (residues 1 to 48) AUTHORS Filipowicz,W. TITLE Direct Submission JOURNAL Submitted (05-MAR-1997) W. Filipowicz, Friedrich Miescher Institut, PO Box 2543, 4002 Basel, SWITZERLAND COMMENT Related sequence Z57130, partial CpG island clone 165a4. FEATURES Location/Qualifiers source 1..48 /organism="Homo sapiens" /db_xref="taxon:9606" /tissue_type="blood" /clone="165a4" /clone_lib="CGI-1" /dev_stage="adult" Protein 1..48 /product="phosphate cyclase" CDS 1..48 /partial /coded_by="join(Y11652:233..277,Y11652:381..>481)" ORIGIN 1 magprvevdg simegggqil rvstalscll glplrvqkir agrstpgl //
the above reports in Macintosh PC UNIX Text HTML MIME format
