ID M2QUZ0_CERS8 Unreviewed; 844 AA.
AC M2QUZ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glutaminyl-tRNA synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_111474 {ECO:0000313|EMBL:EMD40893.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD40893.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD40893.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD40893.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445792; EMD40893.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QUZ0; -.
DR STRING; 914234.M2QUZ0; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000016930; 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:UP000016930}.
FT DOMAIN 12..166
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 169..245
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04557"
FT DOMAIN 253..561
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 564..665
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT REGION 180..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94140 MW; 2DB575750965679E CRC64;
MAPKADNTET TELIELFKSL GLTQSKAAEA AKSAKSAATL KDIIQTHGLV EKNLEEKQAV
LLASLAVQGA KLGEAERGYV VGAVLDGRLK STDQVTAAVK YLEARPLPIQ QADFDEHCGV
GFSITPEELF AKVKEYVSSA AVQGWANLGA TIGVLKNIPE LRWANPLEVK TAVENAFTER
FGAKETGKPK SRESKKDNAS KPSATAEAST SAASSSKSVF AEGFLGRLHK VGDNPQIHPH
LREQHLAATG GIVHTRFPPE PNGFLHIGHS KAIFVNFGYA AYHGGRCYLR FDDTNPEAEE
GRYFESILEA IRWLGYEPWK ITYSSDHFDE LYALAVELIK RDKGYVCHCT AEEIYANRGG
DERGPRKACV HRTRPVSESL AEFEKMKNGH YKPGEAILRM KQDIESGNTM MWDLVAYRVL
NASHHRTHDK WKIYPTYDFT HCLCDSFENI THSLCTTEFI ASRESYEWLC DALEVYKPRQ
SEYGRLNLTG TIMSKRKILQ LVKEEYVRDW DDPRLYTLIA LRRRGVPPGA ILSFVSSLGV
STAASNIQAV RFEQTVRQYL ESTASRLLMV LKPLKVTIEN LPEDYLLWLE KPLHPKVPEL
GISKVPFTRT IYIDADDFRL EDSKDYFRLA PGKTVGLFQA PHPITCTSYK TDPVTGQVTE
LICRMEKGEG KKPKAFIQWV AEHKPSGSPV VVDETRIFHQ LFNSENPSAA VPDFKADINP
DSLEIIKGAM VEIGFWPLVK RAYADARKES EARTKKALEA NAVSGADQAE KGPEDDTPKA
TSEQLIGKEC IRFQGLRVAY FTVDKDAKLT CLNESENVEP GRKEGDYIVL NRIVSLKEDS
GKAA
//
