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RTCA_METAC
ID   RTCA_METAC              Reviewed;         355 AA.
AC   Q8TH85;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=MA_4637;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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}.
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DR   EMBL; AE010299; AAM07971.1; -; Genomic_DNA.
DR   RefSeq; WP_011024505.1; NC_003552.1.
DR   AlphaFoldDB; Q8TH85; -.
DR   SMR; Q8TH85; -.
DR   STRING; 188937.MA_4637; -.
DR   EnsemblBacteria; AAM07971; AAM07971; MA_4637.
DR   GeneID; 1476531; -.
DR   KEGG; mac:MA_4637; -.
DR   HOGENOM; CLU_027882_0_0_2; -.
DR   InParanoid; Q8TH85; -.
DR   OMA; PKPGLSH; -.
DR   OrthoDB; 52581at2157; -.
DR   PhylomeDB; Q8TH85; -.
DR   Proteomes; UP000002487; 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; 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; 2.
DR   TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR   PROSITE; PS01287; RTC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..355
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_0000156425"
FT   ACT_SITE        325
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT   BINDING         300..304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ   SEQUENCE   355 AA;  38735 MW;  6E83259BA941176B CRC64;
     MIEIDGSYGE GGGQVVRTAV ALSAVTGKDV KVTNIRKNRP NPGLKQQHLK ALETAARICE
     ARVSGLFPGS SELFFSPVEI KGGKYEVDIG TAGSITLLLQ SLMPALPFAK EKVKLTIKGG
     TDVAWSPTID YLQHVTLRAL EQLGYAGIVT LKKRGYYPRG GGEVSAVFEP CKLRSFHFRR
     VKENRRTGEA RREEETRNEG RNQNQRIEIQ GISHASNLPA HVPARQAEAA ESLLLEAGYG
     SRTKIQSFEL LSTGSGITLW SGYCGGSALG KKGLPAEKVG RRAAEEIILE LSSKAPVDVH
     LADQLIPYMA LAGNSSYTVR ELTLHAATNI WVTEQFLDVK FRIEEKEGLF EVSVD
 
 
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