ID A0A2I1FW35_9GLOM Unreviewed; 418 AA.
AC A0A2I1FW35;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=RhiirA4_513070 {ECO:0000313|EMBL:PKY38533.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY38533.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY38533.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY38533.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) 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:PKY38533.1}.
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DR EMBL; LLXI01000031; PKY38533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1FW35; -.
DR VEuPathDB; FungiDB:FUN_002108; -.
DR VEuPathDB; FungiDB:GLOIN_2v1741857; -.
DR VEuPathDB; FungiDB:RhiirA1_431797; -.
DR OrthoDB; 540846at2759; -.
DR Proteomes; UP000234323; 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; 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.
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:UP000234323}.
SQ SEQUENCE 418 AA; 47618 MW; 2B2AA9930BF7E154 CRC64;
MENQHFLIRG SLIGFVIGGI GCCFYYSSNE QTVTPWDVDG NGRAIDYDKL IKKFGTRPID
KELLQRFETL TGKKCHTFLR RGIFFSHREF NKILDRYEQN KPFFIYTGRG PSSSSMHLGH
MIPFVFCKWL QDVFDVPIVI QLTDDEKFIF KPGLTLEETR KYAYDNAKDI VACGFDPDKT
FIFADTDYVG GPFYHNIVKI AKSITNSQSK ATFGFVDSDC IAKTHFVAVQ AAPSFSNSFP
QIFGTRSNIP CVIPCAIDQD PYFRLTRDVA QKLKYPKPSL IHAKFFPALQ GSQTKMSASL
DNSAIFMSDT PNQIKKKINK YAFSGGRVSA EEHRLKGGDP DVDVAYQYLS VFLDDDEELD
EIKKKYVSGE MMTGELKARC IQVLQKFVDE FKQRKSEVTG EILKKFMDPN KKIVVNET
//
