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Database: UniProt
Entry: J4UXE9_9FIRM
LinkDB: J4UXE9_9FIRM
Original site: J4UXE9_9FIRM 
ID   J4UXE9_9FIRM            Unreviewed;       416 AA.
AC   J4UXE9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000256|HAMAP-Rule:MF_01539};
DE            EC=6.3.4.- {ECO:0000256|HAMAP-Rule:MF_01539};
GN   Name=tmcAL {ECO:0000256|HAMAP-Rule:MF_01539};
GN   ORFNames=HMPREF1147_0777 {ECO:0000313|EMBL:EJP31262.1};
OS   Selenomonas sp. FOBRC9.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=936573 {ECO:0000313|EMBL:EJP31262.1, ECO:0000313|Proteomes:UP000006970};
RN   [1] {ECO:0000313|EMBL:EJP31262.1, ECO:0000313|Proteomes:UP000006970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOBRC9 {ECO:0000313|EMBL:EJP31262.1,
RC   ECO:0000313|Proteomes:UP000006970};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of elongator tRNA(Met), using acetate and ATP as
CC       substrates. First activates an acetate ion to form acetyladenylate (Ac-
CC       AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
CC       {ECO:0000256|HAMAP-Rule:MF_01539}.
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-COMP:10694,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01539};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539}.
CC   -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000256|HAMAP-
CC       Rule:MF_01539}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01539}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJP31262.1}.
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DR   EMBL; ALJR01000030; EJP31262.1; -; Genomic_DNA.
DR   RefSeq; WP_009658443.1; NZ_ALJR01000030.1.
DR   AlphaFoldDB; J4UXE9; -.
DR   PATRIC; fig|936573.3.peg.1615; -.
DR   eggNOG; COG1323; Bacteria.
DR   OrthoDB; 9769796at2; -.
DR   Proteomes; UP000006970; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01539; TmcAL; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase.
DR   PANTHER; PTHR37825; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR   PANTHER; PTHR37825:SF1; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR   Pfam; PF05636; HIGH_NTase1; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Transferase {ECO:0000313|EMBL:EJP31262.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01539};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539}.
FT   BINDING         7..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   416 AA;  46213 MW;  F616913347B5F4C9 CRC64;
     MRAIGIIAEY NPFHHGHRYQ LTELHRMFPS SDGIIIAMSG SFSQRGTPCI LDKWTRARHA
     VEGGADLVLE LPFVFSCRSA QDFARGGVSL LAALGIVERL AFGTETHDIA PLKYIAASID
     TPVVQGRLHS YISAGDSYAA ALSRAAADKS IPEEMLRLPN NILAIEYLRA LCRSTFEISP
     IAIPRSTASH NDTALYPGIT SASSIRSALY ESIPPWERLA DSVPPSVYAD LRTVYETKLP
     NENKLLSLLR YTLLTSSNSE REEILGVTEG IENRLIRTLQ KVNDYDDLLT AAATKRYTRS
     RIARLILHLL IKFKKAQAAR FDTHGATYIR PLAFNVRGQE LLRAIKEHTH LPIITRTAKF
     LTSNNRSFSG RLSLLQEMLA FDTLATDLRL LTVLQHTNQT SDFITPPCVI LSTPKG
//
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