ID A0A238F8W5_9BASI Unreviewed; 847 AA.
AC A0A238F8W5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
GN ORFNames=BQ2448_1039 {ECO:0000313|EMBL:SCV69645.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV69645.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363037}.
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DR EMBL; FMSP01000005; SCV69645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238F8W5; -.
DR STRING; 269621.A0A238F8W5; -.
DR OrthoDB; 934at2759; -.
DR Proteomes; UP000198372; 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:UniProtKB-EC.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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:UP000198372}.
FT DOMAIN 12..170
FT /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04558"
FT DOMAIN 273..574
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 586..687
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT codon binding"
FT /evidence="ECO:0000259|Pfam:PF03950"
FT REGION 371..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 94898 MW; 97E8EE164DBF2E1D CRC64;
MAPPPLDPAQ NELCRYLQQC GLSQVRSTET ARSKTSANVQ AFFRKHELDK MGLSDKQALL
MLQVVKDANR VGDMGQRYLV KRVKEGGLEK AEQVTAAVKY LSSHTGEEVN EATFDKACGV
GFSATPDQVL SHVRDYVESH KDEITKVGWP GINKVSAQIK LNDDFLRWVN MLELRDAFNA
VYVEVLGEKP DPKAVAAGAA AGGAAKNGKG TAKDASKKVS TTPAAATTWA AVPDDKPKDM
FGTGWLARLH KPGGNEQVYP ERMEEHLKAT EGKVFTRFPP EPNGFLHIGH SKAIAVNFGY
AKYNKGHCYL RYDDTNPEAE EQIYFDKTLE AVRWLGYEPY KITHSSDHFQ KLYDLAKELI
KAGLAYTSDD TPEDIAAQRG GKEHGPRHES KDRNKPIEQS LKEFQDMKNG KYKPGEMTLR
MKQDMTSPNP TMWDIIAYRV LLTPHHRTGT DWCIYPTYDF THCLCDSFEN ISHSLCTTEF
IGARAAYEWL CDALKVYKPR QSEYGRLSLE GAITSKRKLL RLVKEGHVSG WDDPRLHTLI
ALKRRGVPPA AIIAFVSHLG VSPNSSLVPL ARFEQTVRQH LEMSTPRLMM VLKPIKVVLD
NVDDDFYLEI EKALHPKIPE MGSNKIPFTK TFYIDGDDFR ADGDLKDFFR LCPGATVGLL
QVPHAVTYLS HEVDEKGEVK EVRCRYEVGK TIKPKAWIQW VAEHAPSRSP VPIKQARIFK
RLFKSDDPAS LGDKYIDDID PNSLTKVDGA MIEPGIWEVI EQSLKRAKEI VEERKKEAEK
NGTDAPPQVE GLEVVRFQGM RVAYFALDSD SKLKKGRRAC GAAEGEDEIV LNLIAPLKQD
AAAGKKV
//
