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Database: UniProt
Entry: A0A0U1LL36_TALIS
LinkDB: A0A0U1LL36_TALIS
Original site: A0A0U1LL36_TALIS 
ID   A0A0U1LL36_TALIS        Unreviewed;       607 AA.
AC   A0A0U1LL36;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=PISL3812_01058 {ECO:0000313|EMBL:CRG83703.1};
OS   Talaromyces islandicus (Penicillium islandicum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Islandici.
OX   NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG83703.1, ECO:0000313|Proteomes:UP000054383};
RN   [1] {ECO:0000313|EMBL:CRG83703.1, ECO:0000313|Proteomes:UP000054383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG83703.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007894}.
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DR   EMBL; CVMT01000001; CRG83703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LL36; -.
DR   STRING; 28573.A0A0U1LL36; -.
DR   OMA; YHYLRWA; -.
DR   OrthoDB; 5404395at2759; -.
DR   Proteomes; UP000054383; 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:0000049; F:tRNA binding; IEA:InterPro.
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; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
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; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
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|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054383}.
FT   DOMAIN          48..365
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          527..566
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   REGION          492..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  67764 MW;  DA0F7025DBBEA208 CRC64;
     MISPRYRILS ARPAWTCIQC RANSSVASRA ASPHVHRNKT VLLDKAARTR FAPSPTGYLH
     LGSLRTALFN YLLAKRTGGQ FLLRLEDTDQ KRTIPGAEER LYEDLQWAGL EWDEGPNVGG
     QYGPYRQSER TAIYRAYADS LISSGHAYRC FCSAERLDTL ARHRNEVGLP LGYDRKCADI
     GHDEAEERAA GGETHVVRLK TDGYPMFRDI VYGKTGQNRT GGKKPMDFID RVYEDPILLK
     SDGHPTYHLA NVVDDHEMKI THVIRGTEWM ASTPMHVALY NAFNWTPPEF AHVPLLVDKN
     GQKLSKRNAD IDISHFRDSG IMAPTLLNFA ALLGWSHTSR SDVLTLKDME EMFNLKITKG
     NTVVAFEKMW FLQKAHAQRI AATGGPELEE LEDKSEAAAE KLVAGTEARF ETSHRDVVRL
     LLQADAKSYT TPEEFIDRNK TFFIAPSNRP AYEPAAKDSA VPISTLHTAA AAMSLVPEDH
     WTVENHRFNI KSYNTDPPTA QTETDKADGE LSPSSAASII AQDKAFKKEL YHYLRWALSA
     GAPGPGIPET LAILGRAESV RRLEEARRLT KPEVTHANTC RVPKTPIQSP SVENADKSWM
     GSLAPKE
//
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