ID RTCA_ESCF3 Reviewed; 338 AA. AC B7LSC2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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=EFER_3388; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928158; CAQ90865.1; -; Genomic_DNA. DR RefSeq; WP_015953785.1; NC_011740.1. DR AlphaFoldDB; B7LSC2; -. DR SMR; B7LSC2; -. DR GeneID; 75060004; -. DR KEGG; efe:EFER_3388; -. DR HOGENOM; CLU_027882_0_0_6; -. DR OrthoDB; 9789235at2; -. DR Proteomes; UP000000745; 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; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1. DR Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 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 NCBIfam; TIGR03399; RNA_3prim_cycl; 1. DR PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1. DR PANTHER; PTHR11096:SF0; RNA 3'-TERMINAL PHOSPHATE CYCLASE; 1. DR Pfam; PF01137; RTC; 1. DR Pfam; PF05189; RTC_insert; 1. DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1. DR SUPFAM; SSF55205; EPT/RTPC-like; 2. DR SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1. DR PROSITE; PS01287; RTC; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding. FT CHAIN 1..338 FT /note="RNA 3'-terminal phosphate cyclase" FT /id="PRO_1000118705" FT ACT_SITE 308 FT /note="Tele-AMP-histidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" FT BINDING 103 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" FT BINDING 283..287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200" SQ SEQUENCE 338 AA; 35929 MW; A3B55F3678AB0937 CRC64; MKRMIALDGA QGEGGGQILR SALSLSMITG QPFTITGIRA GRAKPGLLRQ HLTAVKAATE ICGATVEGAE LGSQRLVFRP GTVRGGDYRF AIGSAGSCTL VLQTVLPALW FADGPSRVEV SGGTDNPSAP PADFIRRVLE PLLAKIGIHQ QTTLLRHGFY PAGGGVVATE VSPVASFNTL QLGERGNIVQ MRGEVLLAGV PRHVAEREIA TLAGSFSLHE QNIHNLPRDQ GPGNTVSLEV ESENITERFF VVGEKRVSAE VVAAQLVQEV KRYLASPAAV GEYLADQLVL PMALVGAGEF TVAHPSCHLL TNIAVVERFL QVRFCLIETD GVTRVSIK //