RTCA_KORVE
ID RTCA_KORVE Reviewed; 355 AA.
AC Q1IS76;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Acid345_1272;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(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; CP000360; ABF40274.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1IS76; -.
DR SMR; Q1IS76; -.
DR STRING; 204669.Acid345_1272; -.
DR EnsemblBacteria; ABF40274; ABF40274; Acid345_1272.
DR KEGG; aba:Acid345_1272; -.
DR eggNOG; COG0430; Bacteria.
DR HOGENOM; CLU_027882_0_0_0; -.
DR OMA; PKPGLSH; -.
DR Proteomes; UP000002432; 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; 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.
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_0000264792"
FT ACT_SITE 316
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT BINDING 291..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ SEQUENCE 355 AA; 37475 MW; CEB9354906316A89 CRC64;
MRCGPKGLNM IVIDGSQGEG GGQILRTALS LSMVTGQPFT IEKIRANRER GGLLRQHLTA
VLAAAEISGA NVTGAELGSR TLTFAPQRVT PGDYSFAVGT AGSATLVLQT LLPALMLANK
PSNVVVEGGT HNMAAPPFDF LAKTFAPIIE SMGPKLKLTL DRYGFYPAGG GKITAEIEPV
EKLKQLELLD RGEVLQQNAV ALLAHLPRHI ADRELETASN ILGLAPESTR ILGTKNSAGP
GNALMIEVQT ERHTEIFTAF GKVGISAEKV AEEAAVAAAQ YVASSAFACE HLADQLLLPI
ALAGGGSFTA VRQTMHARTN IEIIRLFLPV SFEISEEENC ARVALSTRDR AGVSA
