ID A0A3N4L3R8_9PEZI Unreviewed; 382 AA.
AC A0A3N4L3R8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=P167DRAFT_531125 {ECO:0000313|EMBL:RPB17564.1};
OS Morchella conica CCBAS932.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Morchellaceae; Morchella.
OX NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB17564.1, ECO:0000313|Proteomes:UP000277580};
RN [1] {ECO:0000313|EMBL:RPB17564.1, ECO:0000313|Proteomes:UP000277580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB17564.1,
RC ECO:0000313|Proteomes:UP000277580};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000107};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
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DR EMBL; ML119105; RPB17564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4L3R8; -.
DR STRING; 1392247.A0A3N4L3R8; -.
DR InParanoid; A0A3N4L3R8; -.
DR Proteomes; UP000277580; 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 HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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 InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000277580}.
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42715 MW; 2B90F11ACB1204B2 CRC64;
MKRGSKVLDS LPHRSLQSQW YSPRYLPRGL QTSTSFTPKT IFSGIQPTGV PHLGNYLGAL
KQWTSFQNTE TESTKLIFCI VDLHAITSPQ KASNLRQWKK EMLTTLLAIG LNPDRCIIFE
QSRVPAHSEL MWILSCISST GRLSRMTQWK SKLGISEEHH SLEDKSTETL KLGLFSYPVL
QAADILVHRA THVPVGEDQA QHLELTRDIV GAFHHNYGKV FPLPATLLSP AKRVMSLSDP
TQKMSKSAPD PKSRILLTDS PTSVQGKIKV ALTDSLETYG ITYDPQKRPG LSNLIEIYAH
IQGREDFEHV ASEFEGLTKK VFKERVADCI NESLESIRSE YTRITETEGD GFLEKVVREG
SAKAANSAEE TMVKVREALG LL
//
