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Database: UniProt
Entry: A0A373VWA2_9FIRM
LinkDB: A0A373VWA2_9FIRM
Original site: A0A373VWA2_9FIRM 
ID   A0A373VWA2_9FIRM        Unreviewed;       472 AA.
AC   A0A373VWA2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161,
GN   ECO:0000313|EMBL:RGG64209.1};
GN   ORFNames=DWX28_02465 {ECO:0000313|EMBL:RGG64209.1};
OS   Blautia sp. AF19-10LB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=2292961 {ECO:0000313|EMBL:RGG64209.1, ECO:0000313|Proteomes:UP000262342};
RN   [1] {ECO:0000313|EMBL:RGG64209.1, ECO:0000313|Proteomes:UP000262342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF19-10LB {ECO:0000313|EMBL:RGG64209.1,
RC   ECO:0000313|Proteomes:UP000262342};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000047, ECO:0000256|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
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:RGG64209.1}.
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DR   EMBL; QTWS01000002; RGG64209.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A373VWA2; -.
DR   Proteomes; UP000262342; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.30.465.60; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   NCBIfam; TIGR02433; lysidine_TilS_C; 1.
DR   NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR   PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF82829; MesJ substrate recognition domain-like; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          392..464
FT                   /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00977"
FT   BINDING         30..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   472 AA;  54422 MW;  A83BA5FBD84AB202 CRC64;
     MREKTFDKVK DFVKENEMLA RNCAVIAGVS GGNDSMTMLH LLRRLREIWH FHLRVVHVNH
     GIRGAEADRD QRMVETVCTE WNIPCSVYRY DVPELSVKWK LGTEETGRIV RRQAFDAETH
     KCRKQYAVVR TALAHNKNDL AETMLHHLAR GTGLRGLCSL KPVNGEVIRP LLCLERREID
     DYIRECGIPS VLDSTNLEDE YTRNRIRRHL LPVMEREINA KTVEHMAETS RLLSEAEEFL
     TDEAAQLAAD YYREPDGSYC LGEGFFQKKQ ILKSYGVRTI LEKLSGRSRD LTQTHIRQVL
     ELYSCRVSKR ISLPYGLEAV RTYDGVILRK KIQQKPGTEG RKEQEIPLPA TSEEVETPFG
     RFTIKVFSYS GEKILEKKYT KWFDCDKIKC GLSVRTRKTG DYLIVGRDGG RKKLTRCMID
     DKFPKETRDQ VPLIADGGEI LWIIGGRISE RYKITSCTRN VLEITYQGGT RL
//
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