RTCA_PYRAB
ID RTCA_PYRAB Reviewed; 342 AA.
AC Q9V0Z6; G8ZJA0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=PYRAB06330; ORFNames=PAB1943;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic
CC phosphodiester at the end of RNA. The mechanism of action of the enzyme
CC occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer
CC of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of
CC the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to
CC produce the cyclic end product. The biological role of this enzyme is
CC unknown but it is likely to function in some aspects of cellular RNA
CC processing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062,
CC ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ248284; CAB49555.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70027.1; -; Genomic_DNA.
DR PIR; D75184; D75184.
DR RefSeq; WP_010867757.1; NC_000868.1.
DR AlphaFoldDB; Q9V0Z6; -.
DR SMR; Q9V0Z6; -.
DR STRING; 272844.PAB1943; -.
DR EnsemblBacteria; CAB49555; CAB49555; PAB1943.
DR GeneID; 1495540; -.
DR KEGG; pab:PAB1943; -.
DR PATRIC; fig|272844.11.peg.673; -.
DR eggNOG; arCOG04125; Archaea.
DR HOGENOM; CLU_027882_0_0_2; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR PhylomeDB; Q9V0Z6; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 1.
DR HAMAP; MF_00200; RTC; 1.
DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR InterPro; IPR037136; RNA3'_phos_cyclase_dom_sf.
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 InterPro; IPR036553; RPTC_insert.
DR PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..342
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156430"
FT ACT_SITE 307
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 283..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 36928 MW; F9B55209F5C07849 CRC64;
MITIDGSYGE GGGQILRTSI ALSAITGEPV RIINIRANRP NPGLRPQHLH GILALKHLAN
ADVKGAHVGS RELVFIPKRL EAKKVEVNIG TAGSITLVLQ ALLPAMAFAK NRVEFKITGG
TDVPWSPPVD YLANVTLFAL EKLGIMAGIK IVRRGHYPKG GGIIEGYVEP WKERRELVAT
KYSSIAKVEG ISHATNLPAH VAERQAKAAK EELSKLEVPV KIKTEVSKSL GPGSGIVVWA
ETDCLRLGGD ALGKRGKPAE VVGKEAAQEL LEQLKPGYCV DKFLGDQLIP FLAFSGGEIW
VSEVTNHLKT NIWVVENFLG KVFDLDGEVG KPGKVKVVRR VE
