ID   RTCA_HALSA              Reviewed;         339 AA.
AC   Q9HRE8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 118.
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; Synonyms=tpc; OrderedLocusNames=VNG_0732G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAG19210.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG19210.1; ALT_INIT; Genomic_DNA.
DR   PIR; F84230; F84230.
DR   RefSeq; WP_012289214.1; NC_002607.1.
DR   AlphaFoldDB; Q9HRE8; -.
DR   SMR; Q9HRE8; -.
DR   STRING; 64091.VNG_0732G; -.
DR   PaxDb; Q9HRE8; -.
DR   EnsemblBacteria; AAG19210; AAG19210; VNG_0732G.
DR   GeneID; 5952667; -.
DR   GeneID; 62886333; -.
DR   KEGG; hal:VNG_0732G; -.
DR   PATRIC; fig|64091.14.peg.559; -.
DR   HOGENOM; CLU_027882_0_0_2; -.
DR   InParanoid; Q9HRE8; -.
DR   OrthoDB; 52581at2157; -.
DR   PhylomeDB; Q9HRE8; -.
DR   Proteomes; UP000000554; 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; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..339
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_0000156424"
FT   ACT_SITE        310
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         286..290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  34879 MW;  27B75201F22A61FE CRC64;
     MHVLDGSSGG GQLVRTALTC AAVSGESFRM RYVRRARSNP GLQAQHCAAV NAVADICDAA
     TDGVEVGSEA FSFEPEVAAE EADDDEEPTL GGTTSVEVGT AGSIPLVFDS LLPLAGALDE
     PITATLTGGT DAKWAPPMDY FQHVKLPLLR EHGIDATVSV DRRGFYPRGG GEATLTVEPS
     TPTPITLTER GDREALTAYS VAESSLADDE VAEQQATAAA PDAAHEIAYT DADSAGSAVV
     LAAEYEHSRA GFAALGERGV SADAVGENAA DALAAFESGP GAVDSHLADQ LVPVVAVAGG
     EVRAPEVTTH IETCVDLLAE FDYDIDIEHT DDGAVVLSA