ID W4B0R6_9BACL Unreviewed; 410 AA. AC W4B0R6; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 10-APR-2019, entry version 15. DE RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000256|HAMAP-Rule:MF_01539, ECO:0000256|SAAS:SAAS01132686}; DE EC=6.3.4.- {ECO:0000256|HAMAP-Rule:MF_01539, ECO:0000256|SAAS:SAAS01132682}; GN Name=tmcAL {ECO:0000256|HAMAP-Rule:MF_01539}; GN ORFNames=C161_11088 {ECO:0000313|EMBL:ETT37049.1}; OS Paenibacillus sp. FSL R5-192. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT37049.1, ECO:0000313|Proteomes:UP000019041}; RN [1] {ECO:0000313|EMBL:ETT37049.1, ECO:0000313|Proteomes:UP000019041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT37049.1, RC ECO:0000313|Proteomes:UP000019041}; RX PubMed=24422886; DOI=10.1186/1471-2164-15-26; RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R., RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.; RT "Genomic comparison of sporeforming bacilli isolated from milk."; RL BMC Genomics 15:26-26(2014). CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) CC at the wobble position of elongator tRNA(Met), using acetate and CC ATP as substrates. First activates an acetate ion to form CC acetyladenylate (Ac-AMP) and then transfers the acetyl group to CC tRNA to form ac(4)C34. {ECO:0000256|HAMAP-Rule:MF_01539, CC ECO:0000256|SAAS:SAAS01132701}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP CC + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met); CC Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA- CC COMP:10694, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_01539, CC ECO:0000256|SAAS:SAAS01132695}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539, CC ECO:0000256|SAAS:SAAS01132697}. CC -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000256|HAMAP- CC Rule:MF_01539, ECO:0000256|SAAS:SAAS01132687}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01539}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETT37049.1}. 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; ASPR01000014; ETT37049.1; -; Genomic_DNA. DR RefSeq; WP_036670334.1; NZ_ASPR01000014.1. DR EnsemblBacteria; ETT37049; ETT37049; C161_11088. DR PATRIC; fig|1226754.4.peg.2268; -. DR Proteomes; UP000019041; Unassembled WGS sequence. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01539; UPF0348; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase. DR PANTHER; PTHR37825; PTHR37825; 1. DR Pfam; PF05636; HIGH_NTase1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132699}; KW Complete proteome {ECO:0000313|Proteomes:UP000019041}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132693}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132684}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132689}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132691}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132678}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539, KW ECO:0000256|SAAS:SAAS01132680}. FT NP_BIND 7 20 ATP. {ECO:0000256|HAMAP-Rule:MF_01539}. FT BINDING 102 102 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01539}. FT BINDING 168 168 ATP. {ECO:0000256|HAMAP-Rule:MF_01539}. FT BINDING 193 193 ATP. {ECO:0000256|HAMAP-Rule:MF_01539}. SQ SEQUENCE 410 AA; 44358 MW; 29BEA0575A6FD8BA CRC64; MKAVGVIVEY NPLHNGHVYH LQEARRLSGA DAVVAVMSGP FLQRGEPAIV GKRARTEMAL HAGADLVLEL PVAYAVQPAE WFAFGAVSLL HRTGVVDSLC FGSESGDLDS LQRIARVLAV EPAGMREDIA RRLREGASYP AAYAGAAAAL APGGVDAHDA AALLEQPNNS LGLHYLIALQ RLGSAIQPYT AARTGAAYHE ATPGPGAIAS ATAVRRLLMA DGPDAAAPYV PAATLAILHR EWQEGRAPIH WERFAQPLLH LAATRRASEL ERIAEVTEGL EHRLSRALAQ LPEPSVEALL NALKTKRYTR TKLQRMLAHL LLNHTKAECS PEQLATGPGY LRVLGFNAQG QSLLKQMKKT ASLPVVLKPS TFTHNQLELD IQAQVAYGLA CEHRDTRKMF SDYYESPVRL //