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Database: UniProt
Entry: A0A165QKE3_EXIGL
LinkDB: A0A165QKE3_EXIGL
Original site: A0A165QKE3_EXIGL 
ID   A0A165QKE3_EXIGL        Unreviewed;       841 AA.
AC   A0A165QKE3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN   ORFNames=EXIGLDRAFT_600271 {ECO:0000313|EMBL:KZW03745.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03745.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW03745.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03745.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-
CC         glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662,
CC         Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521,
CC         ChEBI:CHEBI:456215; EC=6.1.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000948};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; KV425882; KZW03745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165QKE3; -.
DR   STRING; 1314781.A0A165QKE3; -.
DR   InParanoid; A0A165QKE3; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00807; GlnRS_core; 1.
DR   Gene3D; 1.10.10.2420; -; 1.
DR   Gene3D; 1.10.8.1290; Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR004514; Gln-tRNA-synth.
DR   InterPro; IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
DR   InterPro; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR   InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
DR   InterPro; IPR042559; Gln-tRNA-synth_Ib_RNA-bd_N_2.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00440; glnS; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF04558; tRNA_synt_1c_R1; 1.
DR   Pfam; PF04557; tRNA_synt_1c_R2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 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:UP000077266}.
FT   DOMAIN          14..167
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04558"
FT   DOMAIN          170..242
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04557"
FT   DOMAIN          249..558
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          562..662
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   REGION          179..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  93282 MW;  392CF69212AD213D CRC64;
     MPPKIDLNDP AVAELVNLFQ SIGLDARKAQ DAAIGKHSAS LRELIESNGL AGKGIDTKRG
     VLLSAFAVNA GKLGAPERAY GVDAIVDGRL KTNDQVAAAS KYLESHSAPI NDAEFDDVCG
     VGFSITNEEI YNAVTGYIQS AAVTSWGNLS GVLASLRTSP TLRWASPLEV KNTVERVFTE
     TFGPKGSTKP PPKEPKAAPT ASTSAPEEAP PPAKTVFEEG FLGALHAPGG NPQIHPRLRE
     QHLSATGGKV FTRFPPEPNG YLHIGHSKAI FVNFGYAAHH GGKCYLRYDD TNPAAEEARY
     FESILEVVRW LGFEPFRITY SSDYFQQLYD LGVELIKRDK GYCCSCTAEK VKADRGGDDH
     GPRRACEHRD RPIEESLKIF EDMKNGKYEK GTMTMRMKQD LESGNPQMWD LVAYRVVREP
     HHRTLDKWCI YPTYDFTHCL CDSFENISHS LCTTEFIDSR VSYEWLCDAL EVYKPRQSEY
     GRLNIEGTVM SKRKLIKLVK DGHVRGWDDP RMYTLVGLRR RGIPPGAILS FVSTLGVSTA
     KTNIQAVRFE QSVRQYLENT VPRLMMVLRP LKVIIEDMPE GEVLWVEKPL HSKVPELGTS
     KVPFTRTVYI DQDDFRLEDS KDYFRLAPGK TVGLLQAPYP VVYVSHKTDP ATGAVTEVVV
     RFDKVTKKPK AFIQWVAEHK PSGSPVVVDE TRIINRLFMS DDPAALDNFL TDINPNSLEI
     VKGALVEVGF FALAKSSYED AKKEAAERQE KANKLEQEAA AAPQLVGTGG HGDEPKAAAE
     QLVGNECVRF QGMRVAYFAL DKDAKLASFN EGPKAEPRRH DGDYIVLNHI VSLKEDVGKS
     A
//
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