ID D1NW89_9BIFI Unreviewed; 388 AA.
AC D1NW89;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN Name=trpS {ECO:0000313|EMBL:EFA22375.1};
GN ORFNames=BGLCM_0102 {ECO:0000313|EMBL:KFI60082.1}, BIFGAL_04136
GN {ECO:0000313|EMBL:EFA22375.1};
OS Bifidobacterium gallicum DSM 20093 = LMG 11596.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA22375.1, ECO:0000313|Proteomes:UP000003656};
RN [1] {ECO:0000313|EMBL:EFA22375.1, ECO:0000313|Proteomes:UP000003656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA22375.1,
RC ECO:0000313|Proteomes:UP000003656};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFI60082.1, ECO:0000313|Proteomes:UP000029074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11596 {ECO:0000313|EMBL:KFI60082.1,
RC ECO:0000313|Proteomes:UP000029074};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
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:EFA22375.1}.
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DR EMBL; ABXB03000004; EFA22375.1; -; Genomic_DNA.
DR EMBL; JGYW01000001; KFI60082.1; -; Genomic_DNA.
DR AlphaFoldDB; D1NW89; -.
DR STRING; 561180.BIFGAL_04136; -.
DR eggNOG; COG0180; Bacteria.
DR Proteomes; UP000003656; Unassembled WGS sequence.
DR Proteomes; UP000029074; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 42260 MW; BA02BC7B136E7A6F CRC64;
MTDTASSTAP ELTPDTTPDS AADAATANNL TAAGNEMSAS FLAAKKRSDA TLAKLEADPS
KFTMLTGDRP TGRLHLGHFF GSIRERVAMQ NRGVNTNIII ADYQVITDRD TTEHIEENVL
NLVLDYLAAG IDPTKTMIFT HSAVPAENQL MLPFLSLVTE AELHRNPTVK SEMEASGHAL
TGLLLTYPVH QACDILFCKA NVVPIGKDNL PHVEITRTIA RRFNERYAKK HPIFPEPAAI
LSEAPEIPGL DGRKMSKSYG NSIMLGATAE ETAKLIKKSP TDSERMITFD PVNRPQVSAL
LTTAGLVTGR DPREIAEEIG NGGAGTLKKY VTESVNEFLA PHRERRAELA QDMDSIRDIL
HEGNARANAI ANQTLDEVRD AMGMRYDA
//