ID A0A1Y2I1Y0_9FUNG Unreviewed; 461 AA.
AC A0A1Y2I1Y0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BCR44DRAFT_34783 {ECO:0000313|EMBL:ORZ40876.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ40876.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ40876.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ40876.1,
RC ECO:0000313|Proteomes:UP000193411};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ40876.1}.
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DR EMBL; MCFL01000002; ORZ40876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2I1Y0; -.
DR STRING; 765915.A0A1Y2I1Y0; -.
DR OrthoDB; 540846at2759; -.
DR Proteomes; UP000193411; 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; 2.
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:UP000193411}.
FT REGION 431..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 51758 MW; 158BF3504DF10BDD CRC64;
MTEPVAIPVA VNSDHDQKVD PWDVQGAVVD GKPQPINYNK LIEQFGTKAI DQALLDRFER
VTGHKPHRFL RRGIFFSHRE LDHILTKFEK KEPFYLYTGR GPSSDSMHLG HFIPFMFCKW
LQDVFDVPIV IQLTDDEKFL FKQDLTVEQC FKFAQENAKD IIACGFDLNK TFIFSNLNYV
GGTFYHNMVR IAKCITYSTS KAAFGFTESD NIGKSHFVAV QATPSFSNSF PHIFGSRSDI
PCLIPCAIDQ DPYFRLTRDV AHKLGYPKPA LIHAKFFPAL QGSQSKMSAS VDTSAIFMSD
TAKKIKDKIN KYAFSGGQDT VELHRELGGD PDVDVAFQYL TFFLDDDEEL ERIRATYKTG
ELLTGHLKAR CIEVLQHLCG EFQQRKAEVT DQVVLEYMNA SKPMPWAVEK GLVKDPLLSA
FEILNLNAEQ AAGKGGKGGK KKVKKEKGGS KGADAAEVAK E
//