RTCA_SULTO
ID RTCA_SULTO Reviewed; 339 AA.
AC Q974U1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, 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=6.5.1.4 {ECO:0000255|HAMAP-Rule:MF_00200};
GN Name=rtcA {ECO:0000255|HAMAP-Rule:MF_00200}; OrderedLocusNames=STK_05700;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP CRYSTALLIZATION OF CYCLASE IN COMPLEX WITH AMP, AND ACTIVE SITE.
RX PubMed=18776333; DOI=10.1093/nass/nrn112;
RA Shimizu S., Ohki M., Ohkubo N., Suzuki K., Tsunoda M., Sekiguchi T.,
RA Takenaka A.;
RT "Crystal structures of RNA 3'-terminal phosphate cyclase and its complexes
RT with Mg2+ +ATP, ATP or Mn2+.";
RL Nucleic Acids Symp. Ser. 52:221-222(2008).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=19478432; DOI=10.1107/s1744309109014663;
RA Shimizu S., Ohki M., Okubo N., Suzuki K., Tsunoda M., Sekiguchi T.,
RA Takenaka A.;
RT "Crystallization and preliminary crystallographic studies of putative RNA
RT 3'-terminal phosphate cyclase from the crenarchaeon Sulfolobus tokodaii.";
RL Acta Crystallogr. F 65:565-570(2009).
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; BA000023; BAB65566.1; -; Genomic_DNA.
DR RefSeq; WP_010978549.1; NC_003106.2.
DR AlphaFoldDB; Q974U1; -.
DR SMR; Q974U1; -.
DR STRING; 273063.STK_05700; -.
DR EnsemblBacteria; BAB65566; BAB65566; STK_05700.
DR GeneID; 1458516; -.
DR KEGG; sto:STK_05700; -.
DR PATRIC; fig|273063.9.peg.652; -.
DR eggNOG; arCOG04125; Archaea.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR Proteomes; UP000001015; 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 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; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..339
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156437"
FT ACT_SITE 307
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200,
FT ECO:0000269|PubMed:18776333"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT BINDING 283..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ SEQUENCE 339 AA; 37505 MW; C49582296471599D CRC64;
MIEIDGSFGE GGGQILRTSL TLSALTKKPF RIYKIRANRP KPGLQRQHLT AVEAVKKLTN
AKVKGDFVGS TELVFEPEDI VEKGDFEFDV GTAGSVTLIL QTILPLLINR NIKVTIKGGT
DVPKSPSIDY IRLTFLSLLE KIGIRVNLIL IRRGHYPEGG GEIKITEVKG NPSSFSLMER
GELLMIKGIS HVSSLPSHIA ERQAKSAKEF LLSKIKIPVE IEIDVRENER SKGSGIALTA
IFEKTFLGSD SLGEKGKRAE IVGEEAAKSI YEEIISNATV DRHMSDMLML YASLYYGEYI
GSELTSHART NSEIIKKFLN VNIQISGEKP FIFRAKKEL
