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Database: UniProt
Entry: V2XN58_MONRO
LinkDB: V2XN58_MONRO
Original site: V2XN58_MONRO 
ID   V2XN58_MONRO            Unreviewed;       472 AA.
AC   V2XN58;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   13-SEP-2023, entry version 38.
DE   RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE            EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030268};
GN   ORFNames=Moror_8266 {ECO:0000313|EMBL:ESK94281.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94281.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK94281.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94281.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK94281.1}.
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DR   EMBL; AWSO01000147; ESK94281.1; -; Genomic_DNA.
DR   RefSeq; XP_007846425.1; XM_007848234.1.
DR   AlphaFoldDB; V2XN58; -.
DR   STRING; 1381753.V2XN58; -.
DR   KEGG; mrr:Moror_8266; -.
DR   HOGENOM; CLU_032621_0_1_1; -.
DR   OrthoDB; 540846at2759; -.
DR   Proteomes; UP000017559; 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; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 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|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53043 MW;  894B90AEEA711F76 CRC64;
     MSAPINLPEA LSADPTAPPT LSGIVNALAD ASLADRESVT PNSSTSSDPK EKGGTPVIKP
     VPADVSAHEQ VVTPWDVQGS VGQDGKQQAI DYDKLIEQFG TRRVDEALLQ RFEKLTGHRP
     HIFLRRGMFF SHREFDKILD RYEQGKPFFL YTGRGPSSDS MHLGHMIPFV FTKWLQDVFG
     VPLVIQLTDD EKFLFKHQLK VEQTKEFARM NARDIIACGF DLDKTFIFSN YDYVGGPFYE
     NVSKISRQIT YSQAKATFGF QDSDNIGKIH FAAIQATPSF SNSFPQIFGT QSNIPCLIPC
     AIDQDPYFRL TRDVAQKLKY PKPTLLHSKF FPALQGPQTK MSASDPNSSI YMSDTKNQIK
     NKVNRHGFSG GQETEEEHRR LGGDTEVDVA YQYLSFFLDD DNELVKMGED YRAGRLLTGQ
     LKARCIEVLQ KFVGDFQERK SKITEEQINA FMDKTRKIDP TVGKAKTTSA TA
//
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