ID A0A067P0Q8_PLEOS Unreviewed; 834 AA.
AC A0A067P0Q8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glutaminyl-tRNA synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PLEOSDRAFT_176102 {ECO:0000313|EMBL:KDQ29451.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ29451.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL198007; KDQ29451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067P0Q8; -.
DR STRING; 1137138.A0A067P0Q8; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_176102; -.
DR HOGENOM; CLU_001882_2_3_1; -.
DR InParanoid; A0A067P0Q8; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000027073; 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 InterPro; IPR049437; tRNA-synt_1c_C2.
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; PF20974; tRNA-synt_1c_C2; 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:UP000027073}.
FT DOMAIN 14..171
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 174..246
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 DOMAIN 677..731
FT /note="tRNA synthetases class I (E and Q) anti-codon
FT binding"
FT /evidence="ECO:0000259|Pfam:PF20974"
FT REGION 184..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 93098 MW; FF4DEE3656C42BDB CRC64;
MSSKTSKLDA SGDPLIALFK SIGLNQAKAA EAAKSPKAAA ILKDTIEKHS LATASLDEKQ
ASLFAALASA ISKASDVGEQ ETSYIVARIL DGKLKSVDQV SVAVKYIESH RVPIDDVGFD
AQCGVGFTIT SEELLVQVNE HITSNAIAGW DKLGSVITSI RNSPSLRWAN PLDIKNAVET
AFNDTFGPKQ AGKPKTKEPK AAKKESPAAS AQPSTSRKSV FEEGFLGQLH RPGGNPQIHP
HLREAHLATT GGQVWTRFPP EPNGYLHIGH SKAIFVNFGY AAHNGGKCYL RYDDTNPEKE
EARYFESILE MVRWLGFEPW KITYSSDYFD KLYELAIELI KRDKAYVCHC TQEQIKADRG
EKRGQPRPCI HRDRPVSESL AEFVNMKDGK YRPKEANLRM KQDLEDGNPQ MWDLTAYRVL
DASHHRTGDK WKIYPTYDYT HCLVDSFENI SHSLCTTEFV SSRQSYEWLC DALELYKPRQ
SEYGRLSLEG AIMSKRKILA LVEEGYVDGW DDPRLYTLIA LRRRGVPPGA IISFVSTLGV
STAVTSIEVA RFEHAVRQYL ESTAPRLLMV MRPLKVTIEN LPEDYLLTIE KPLHPKVPEL
GTTSVPFTRT IYIDADDFRL EDSKDYFRLA PGKTVGLFQA PYPITCTSYK TDPSTGEIVE
LLCKLENEGP PKKPKAFIQW VAEHPPSGSP VRIDETRVFH RLFKSDNPPA DFRSDINPDS
LEVIKGAMVE VGFWPLSKQL MNEARHDGKA RTAKALESSA PAADDETPHA TSEQLVGKEC
VRFQGLRVAY FALDKDSRIA ALDNDVDVEP SREQGDYLVL NRIVSLKEDS GKTA
//
