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Database: UniProt
Entry: N4V208_FUSC1
LinkDB: N4V208_FUSC1
Original site: N4V208_FUSC1 
ID   N4V208_FUSC1            Unreviewed;       646 AA.
AC   N4V208;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=glutamate--tRNA ligase {ECO:0000256|ARBA:ARBA00012835};
DE            EC=6.1.1.17 {ECO:0000256|ARBA:ARBA00012835};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030865};
GN   ORFNames=FOC1_g10010487 {ECO:0000313|EMBL:ENH75101.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH75101.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; KB730000; ENH75101.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4V208; -.
DR   STRING; 1229664.N4V208; -.
DR   VEuPathDB; FungiDB:FOC1_g10010487; -.
DR   HOGENOM; CLU_015768_7_0_1; -.
DR   OMA; QHPYLFW; -.
DR   Proteomes; UP000016928; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00808; GluRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363037};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363037};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363037};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016928}.
FT   DOMAIN          112..396
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   REGION          37..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  72745 MW;  8E5A657AB2E81A47 CRC64;
     MRPLLSHPTR LSRNLIQYRV LYHPIPLLVR RNFTSSVGRQ HDQNSDIAKK ASQSPSEELN
     EQGGKHDRSI KKPSRLAALK KRGQNVGNKE TKVKGGETNQ RYILGQSADK PIRTRFAPSP
     TGYLHLGSLR TALFNNLVAK ATEGGDFIIR IEDTDQNRLV PDAEERIFKD LEWAGLEWSE
     GPDKGGPYGP YRQSERLETY KEHTQTLLEN GSAYRCFCDQ TVLEAQKRAL HDAGKSTAYP
     GTCRTLPRSE SDERAAKGEA HIVRLDSTRF GTPKFKDAIY GPFQKKEPEE DFVLMKRDGY
     PTYHLANVVD DHLMKITHVI RGEEWLISTP KHLALYEAFG WEPPTFAHLG LLVSNNGSKL
     SKRDSSVDLS TYMDQNVFPM ALQAWLANLG ASTKRDAKTP RTLSDVAENL TYKFTRGGIK
     LNPTKLDFFQ HEYRNLLTKT PTADHTSREQ ELIRDYLVTP LVNEVHAITT SSQSISDDYK
     PIQPTGTPLD WPAPLSPVPA MLSSESSQSY TSKIIFQETV RYASVANLAR LLPYFFWRPP
     PDIYRAAIVS ETPRLDLVEL VNKTVQGNDD WETVVDRLFE SIPSDQAPDL HAILRLIAIG
     DSQAVSKSSR ILFDVLGQDE WRFRANLVAS LLGELESSGQ LSVRTG
//
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