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   27-MAR-2024, entry version 112.
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};
GN   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   PaxDb; 186497-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   OrthoDB; 7994at2157; -.
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   CDD; cd00874; RNA_Cyclase_Class_II; 1.
DR   Gene3D; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1.
DR   Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 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   NCBIfam; TIGR03399; RNA_3prim_cycl; 1.
DR   PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1.
DR   PANTHER; PTHR11096:SF0; RNA 3'-TERMINAL PHOSPHATE CYCLASE; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 1.
DR   PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 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
//