ID   RTCA_PYRNV              Reviewed;         347 AA.
AC   B1YDJ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=6.5.1.4 {ECO:0000255|HAMAP-Rule:MF_00200};
GN   Name=rtcA {ECO:0000255|HAMAP-Rule:MF_00200};
GN   OrderedLocusNames=Tneu_0917;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00200}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00200};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00200}.
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00200}.
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; CP001014; ACB39854.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YDJ1; -.
DR   SMR; B1YDJ1; -.
DR   STRING; 444157.Tneu_0917; -.
DR   KEGG; tne:Tneu_0917; -.
DR   eggNOG; arCOG04125; Archaea.
DR   HOGENOM; CLU_027882_0_0_2; -.
DR   OrthoDB; 7994at2157; -.
DR   Proteomes; UP000001694; 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   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; 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; 2.
DR   SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..347
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_1000099356"
FT   ACT_SITE        312
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT   BINDING         286..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ   SEQUENCE   347 AA;  36649 MW;  709FB0EB3424C673 CRC64;
     MAVRIDGSYG EGGGQILRTS IALSALLGKP VEIVNIRAKR ANPGLQPQHL TGVSAAALLT
     DAEVEGAAKG STRLFFKPKA LKCGTFNIDI GTAGSISLVV QTLAPILLYA PCPTKLVITG
     GTDVAWAPPI DYMRFVFARY LTRFGARIAI ELVKRGHYPR GGGKAVVQAE PAGRLRAVDS
     VEFGRPAKIA GVSHAVNLPP HVAERQARAA REALAKLGYA AEVEVEARND GLGPGSGVVL
     WAESDVGNVV GGDALGERGK PAEEVGREAA EKLAAVLKAG ASLDPHMADM VVLYMALAQG
     RSRLSTTEAT MHLQTNIYIV EQFLPVKFKL ERAGPRYIIE VEGVGYP
//