RTCA_PYRFU
ID RTCA_PYRFU Reviewed; 342 AA.
AC Q8U0N7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=RNA 3'-terminal phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE Short=RNA cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE Short=RNA-3'-phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE EC=6.5.1.5 {ECO:0000269|PubMed:22074260};
DE AltName: Full=GTP-dependent RNA 3'-terminal-phosphate cyclase {ECO:0000305};
GN Name=rtc {ECO:0000303|PubMed:22074260};
GN Synonyms=rtcA {ECO:0000255|HAMAP-Rule:MF_00200}; OrderedLocusNames=PF1549;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=22074260; DOI=10.1111/j.1365-2443.2011.01561.x;
RA Sato A., Soga T., Igarashi K., Takesue K., Tomita M., Kanai A.;
RT "GTP-dependent RNA 3'-terminal phosphate cyclase from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL Genes Cells 16:1190-1199(2011).
CC -!- FUNCTION: Catalyzes the GTP-dependent conversion of 3'-phosphate to a
CC 2',3'-cyclic phosphodiester at the end of RNA. The biological role of
CC this enzyme is unknown but it is likely to function in some aspects of
CC cellular RNA processing. {ECO:0000269|PubMed:22074260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + GTP = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + diphosphate + GMP;
CC Xref=Rhea:RHEA:13969, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:83062, ChEBI:CHEBI:83064; EC=6.5.1.5;
CC Evidence={ECO:0000269|PubMed:22074260};
CC -!- ACTIVITY REGULATION: Inhibited by GMP. {ECO:0000269|PubMed:22074260}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.
CC {ECO:0000269|PubMed:22074260};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00200}.
CC -!- MISCELLANEOUS: Generally, RNA 3'-terminal phosphate cyclases are ATP
CC dependent, but P.furiosus enzyme preferentially uses GTP rather than
CC ATP. {ECO:0000305|PubMed:22074260}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00200}.
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DR EMBL; AE009950; AAL81673.1; -; Genomic_DNA.
DR RefSeq; WP_011012696.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0N7; -.
DR SMR; Q8U0N7; -.
DR STRING; 186497.PF1549; -.
DR PRIDE; Q8U0N7; -.
DR EnsemblBacteria; AAL81673; AAL81673; PF1549.
DR GeneID; 41713370; -.
DR KEGG; pfu:PF1549; -.
DR PATRIC; fig|186497.12.peg.1615; -.
DR eggNOG; arCOG04125; Archaea.
DR HOGENOM; CLU_027882_0_0_2; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR PhylomeDB; Q8U0N7; -.
DR BRENDA; 6.5.1.5; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA 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; SSF52913; SSF52913; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW RNA-binding.
FT CHAIN 1..342
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156432"
SQ SEQUENCE 342 AA; 36804 MW; D4D2E5898CB3B4BE CRC64;
MIIIDGSYGE GGGQILRTSI ALSAITGEPV KIINIRANRP NPGLRPQHLN AILALKKLAN
AKVEGAEVGS REVTFIPGEL KGGEIRVDIG TAGSITLVLQ ALLPAMVFAK DTVEFKITGG
TDVSWSPPVD YLINVTMFAL RKIGIEGEIK LLRRGHYPKG GGIVAGYVKP WIERKELIAE
EFENIYKVSG ISHATNLPAH VAERQAKAAM EELKVLGVPI EIKKEVSHSL GPGSGIVVWA
ETECLRLGGD ALGKKGKPAE EVGREAAQEL LSQVKTKACV DKFLGDQIIP FLAISGGKIK
VAEITKHLIT NVWVVEQFFG KVFEVKGGVG EKGEVRVVRK AW
