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Database: UniProt
Entry: S7QIF6_GLOTA
LinkDB: S7QIF6_GLOTA
Original site: S7QIF6_GLOTA 
ID   S7QIF6_GLOTA            Unreviewed;       849 AA.
AC   S7QIF6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Glutaminyl-tRNA synthetase {ECO:0000313|EMBL:EPQ59008.1};
GN   ORFNames=GLOTRDRAFT_54660 {ECO:0000313|EMBL:EPQ59008.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ59008.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ59008.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59008.1};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363037}.
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DR   EMBL; KB469297; EPQ59008.1; -; Genomic_DNA.
DR   RefSeq; XP_007861843.1; XM_007863652.1.
DR   AlphaFoldDB; S7QIF6; -.
DR   SMR; S7QIF6; -.
DR   STRING; 670483.S7QIF6; -.
DR   GeneID; 19307000; -.
DR   KEGG; gtr:GLOTRDRAFT_54660; -.
DR   eggNOG; KOG1148; Eukaryota.
DR   HOGENOM; CLU_001882_2_3_1; -.
DR   OMA; TWCIYPM; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000030669; 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; 1.10.8.1290; 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; IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
DR   InterPro; IPR042558; Gln-tRNA-synth_Ib_RNA-bd_N_1.
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   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:UP000030669}.
FT   DOMAIN          19..172
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04558"
FT   DOMAIN          257..566
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          569..670
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   REGION          190..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  94609 MW;  4D2498AEEA9010D4 CRC64;
     MGPPKPKAAS AGGADVDGLV ELFKTIGLAQ SKAAEAAKSP KSAAVLKELI QRHDLPGKNL
     DEKQGTLMAA LATQGGRLGE GERSYVLNAI LDGRLKSTDQ VNAAVKHLDS HPLPVDQKEF
     DRECGVGYSI TPEELYTKVT EYVSSAAVSG WNNLGASIGA LKGTPELRWA NPLELKSSVE
     RAFTERFGSR EAAKAKGKEV KKEAPSKPTA ASAAPAPEAS TSSVFEQGFL GSLHKVGENP
     QLHEHLRQAH LEFTKGKVHT RFPPEPNGFL HIGHSKAIFV NFGYAAHHGG HCYLRYDDTN
     PEKEEARYFE SILEMVRWLG YEPWMITYSS DHFQRLYDLA VELIRRDKGY VCNCTPEEIK
     ANRGGEMRGP RIACAHRTRP ISESLAEFQK MKDGHYKPGQ AVLRMKQDLE DGNPQMWDLI
     AYRVLETPHH RTGDKWKIYP TYDFTHCLCD SFENITHSLC TTEFIASRQS YEWLCDALEV
     YKPRQSEYGR LNIEGTLMSK RKILALVNEG YVNGWDDPRL YTLIALRRRG VPPGAIVSFV
     SGLGVSTAAS NIQVARFEQS VRSYLENTAP RLLMVLNPLR VTIENIPDGE VVWVEKPLHP
     KVPELGMSRI PFTKHIFIDK DDFRTVDSKE YFRLAPHKTV GLFQAPHPIT CTSYKTDPAT
     GEVTELICRL EDGKDGKAPQ KPKAFIQWVA ELPEAGSPVR VDETRIFHRL FRSDNPAAVE
     PDFRVDINPN SLEVVKGALV EVGFWELAKK AYEDAKREGK ERTDAARANQ ATNVNALASD
     DTPVATSEQL VGKECVRFQG LRVAYFALDK DSWVACLDEK EGVKPGRREG DYIVLNRIVS
     LKEDAGKSA
//
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