SWISS-PROT: P46849

ID RTCA_ECOLI STANDARD; PRT; 339 AA. AC P46849; P46848; Q47349; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE RNA 3'-TERMINAL PHOSPHATE CYCLASE (EC 6.5.1.4) (RNA-3'-PHOSPHATE DE CYCLASE) (RNA CYCLASE). GN RTCA. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RA BLATTNER F.R., PLUNKETT G. III, MAYHEW G.F., PERNA N.T., GLASNER F.D.; RL SUBMITTED (JAN-1997) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE OF 149-339 FROM N.A. RC STRAIN=K12; RX MEDLINE; 86275993. [NCBI, Geneva, Japan] RA COLE S.T., RAIBAUD O.; RL GENE 42:201-208(1986). RN [3] RP REVISION, AND CHARACTERIZATION. RX MEDLINE; 97327572. [NCBI, Geneva, Japan] RA GENSCHIK P., BILLY E., SWIANIEWICZ M., FILIPOWICZ W.; RL EMBO J. 16:2955-2967(1997). CC -!- FUNCTION: CATALYZES THE CONVERSION OF 3'-PHOSPHATE TO A 2',3'- CC CYCLIC PHOSPHODIESTER AT THE END OF RNA. THE MECHANISM OF ACTION CC OF THE ENZYME OCCURS IN 3 STEPS: (A) ADENYLATION OF THE ENZYME BY CC ATP; (B) THE ENZYME ACTS ON RNA-N3'P TO PRODUCE RNA-N3'PP5'A; (C) CC A NON CATALYTIC NUCLEOPHILIC ATTACK BY THE ADJACENT 2'HYDROXYL ON CC THE PHOSPHORUS IN THE DIESTER LINKAGE TO PRODUCE THE CYCLIC END CC PRODUCT. THE BIOLOGICAL ROLE OF THIS ENZYME IS UNKNOWN BUT IT IS CC LIKELY TO FUNCTION IN SOME ASPECTS OF CELLULAR RNA PROCESSING. CC -!- CATALYTIC ACTIVITY: ATP + RNA 3'-TERMINAL-PHOSPHATE = AMP + CC DIPHOSPHATE + RNA TERMINAL-2',3'-CYCLIC-PHOSPHATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE RNA 3'-TERMINAL CYCLASE FAMILY. CC -!- CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 122 THAT PRODUCES TWO SEPARATE ORFS. DR EMBL; U18997; G606355; ALT_FRAME. [EMBL / GenBank / DDBJ] [CoDingSequence] DR EMBL; U18997; G606354; ALT_FRAME. [EMBL / GenBank / DDBJ] [CoDingSequence] DR EMBL; AE000418; G1789826; ALT_FRAME. [EMBL / GenBank / DDBJ] [CoDingSequence] DR EMBL; AE000418; G1789825; ALT_FRAME. [EMBL / GenBank / DDBJ] [CoDingSequence] DR EMBL; M13585; G1128963; -. [EMBL / GenBank / DDBJ] [CoDingSequence] DR ECOGENE; EG12938; RTCA. DR ECOCYC; EG12938; RTCA. DR PROSITE; PS01287; RTC; 1. DR PRODOM [Domain structure / List of seq. sharing at least 1 domain] DR PROTOMAP; P46849. DR SWISS-2DPAGE; GET REGION ON 2D PAGE. KW LIGASE. SQ SEQUENCE 339 AA; 36034 MW; DCE616E7 CRC32; MMKRMIALDG AQGEGGGQIL RSALSLSMIT GQPFTITSIR AGRAKPGLLR QHLTAVKAAT EICGATVEGA ELGSQRLLFR PGTVRGGDYR FAIGSAGSCT LVLQTVLPAL WFADGPSRVE VSGGTDNPSA PPADFIRRVL EPLLAKIGIH QQTTLLRHGF YPAGGGVVAT EVSPVASFNT LQLGERGNIV QMRGEVLLAG VPRHVAEREI ATLAGSFSLH EQNIHNLPRD QGPGNTVSLE VESENITERF FVVGEKRVSA EVVAAQLVKE VKRYLASTAA VGEYLADQLV LPMALAGAGE FTVAHPSCHL LTNIAVVERF LPVRFSLIET DGVTRVSIE //
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P46849 in FASTA format

ModelDirect submission to Swiss-Model

Direct WU-BLAST submission at EMBNet-CH (Lausanne, Switzerland)

Direct BLAST submission at NCBI (Bethesda, USA)

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Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass


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