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Database: UniProt
Entry: Q9HVJ9
LinkDB: Q9HVJ9
Original site: Q9HVJ9 
ID   RTCA_PSEAE              Reviewed;         341 AA.
AC   Q9HVJ9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   29-OCT-2014, entry version 86.
DE   RecName: Full=RNA 3'-terminal phosphate cyclase;
DE            Short=RNA cyclase;
DE            Short=RNA-3'-phosphate cyclase;
DE            EC=6.5.1.4;
GN   Name=rtcA; OrderedLocusNames=PA4585;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS   12228).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
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) transfer of adenylate to an RNA-N3'P to produce RNA-
CC       N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-
CC       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 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC       diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE004091; AAG07973.1; -; Genomic_DNA.
DR   PIR; E83072; E83072.
DR   RefSeq; NP_253275.1; NC_002516.2.
DR   ProteinModelPortal; Q9HVJ9; -.
DR   SMR; Q9HVJ9; 3-331.
DR   STRING; 208964.PA4585; -.
DR   EnsemblBacteria; AAG07973; AAG07973; PA4585.
DR   GeneID; 881010; -.
DR   KEGG; pae:PA4585; -.
DR   PATRIC; 19843915; VBIPseAer58763_4799.
DR   PseudoCAP; PA4585; -.
DR   eggNOG; COG0430; -.
DR   HOGENOM; HOG000015264; -.
DR   InParanoid; Q9HVJ9; -.
DR   KO; K01974; -.
DR   OMA; QNEGPGN; -.
DR   OrthoDB; EOG6RNQDX; -.
DR   PhylomeDB; Q9HVJ9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.30.360.20; -; 1.
DR   Gene3D; 3.65.10.20; -; 2.
DR   HAMAP; MF_00200; RTC; 1.
DR   InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR   InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR   InterPro; IPR000228; RNA3'_term_phos_cyc.
DR   InterPro; IPR017770; RNA3'_term_phos_cyc_type_1.
DR   InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   PANTHER; PTHR11096; PTHR11096; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 1.
DR   SUPFAM; SSF52913; SSF52913; 1.
DR   SUPFAM; SSF55205; SSF55205; 2.
DR   TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR   PROSITE; PS01287; RTC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    341       RNA 3'-terminal phosphate cyclase.
FT                                /FTId=PRO_0000156419.
FT   NP_BIND     283    287       ATP. {ECO:0000250}.
FT   ACT_SITE    308    308       Tele-AMP-histidine intermediate.
FT                                {ECO:0000250}.
FT   BINDING     102    102       ATP. {ECO:0000250}.
SQ   SEQUENCE   341 AA;  36637 MW;  E7277E130981D24F CRC64;
     MRKDLIELDG SEGGGQILRS ALSLSMTSGQ PLRIRNIRGR RSRPGLLRQH LTAVRAAAEI
     CAAEVEGAEL GSRELAFRPG AIRAGDYAFA IGSAGSCSLV LQTLLPALLA ANGESRVRIS
     GGTHNPLAPP ADFLRDSWLP LLQRMGAEVD LELLRHGFVP AGGGELLARV RPARWRPLQL
     EHPGAALRRQ ARALLAGIPG HVGERELERV RQRLGWSDEE RQLEFLAEDQ GPGNALLLRI
     DCEHICATFC AFGQAGVSAE RVAEQVATQA IGWMESGCAA DEHLADQLLL PMALAGAGSF
     TTPRLSAHLQ SNRRVIERFL PVRIGDQALD GGGHRIVITS A
//
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