RTCA_HYPBU
ID RTCA_HYPBU Reviewed; 359 AA.
AC A2BN21;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Hbut_1561;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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; CP000493; ABM81382.1; -; Genomic_DNA.
DR RefSeq; WP_011822700.1; NC_008818.1.
DR AlphaFoldDB; A2BN21; -.
DR SMR; A2BN21; -.
DR STRING; 415426.Hbut_1561; -.
DR EnsemblBacteria; ABM81382; ABM81382; Hbut_1561.
DR GeneID; 4781412; -.
DR KEGG; hbu:Hbut_1561; -.
DR eggNOG; arCOG04125; Archaea.
DR HOGENOM; CLU_027882_0_0_2; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR Proteomes; UP000002593; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..359
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000325189"
FT ACT_SITE 317
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 291..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ SEQUENCE 359 AA; 38709 MW; 3E819662376B17DB CRC64;
MIVIDGSIGE GGGQILRTTL ALAALLGKPV RIVNIRAKRP RPGLQRQHLT SVKAVAELAS
ARVEGLELGS TTLVFIPRGL RSGRFYFNIG TAGSITLVLQ ALLPVTAFAP GPVEVEIVGG
TDVPWSPPID YVRFVLRKLL AMFGFEFEII VKRRGHYPRG GGRVVLRVTQ PPHVLKPVKL
EERGKVLRVE GLSHAVRLPR HVAERQARSA EAVLRSKLPG VPISIDLEWY EPSRDPHLGP
GSGVVVWAVA EHSVLGSDSL GAKGKPAEAV GREAAEKLLE DLATGTALDR HASDMLIPYA
ALACGESILG GARLTMHAWT NIEVVKMLVP GAEMEFIEGG KLNEKFKLRV KGICYKPSS
