GenomeNet

Database: UniProt
Entry: A0A1E5REL3_9ASCO
LinkDB: A0A1E5REL3_9ASCO
Original site: A0A1E5REL3_9ASCO 
ID   A0A1E5REL3_9ASCO        Unreviewed;       827 AA.
AC   A0A1E5REL3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=glutamine--tRNA ligase {ECO:0000256|ARBA:ARBA00012836};
DE            EC=6.1.1.18 {ECO:0000256|ARBA:ARBA00012836};
DE   AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030466};
GN   ORFNames=AWRI3579_g1842 {ECO:0000313|EMBL:OEJ85337.1};
OS   Hanseniaspora osmophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ85337.1, ECO:0000313|Proteomes:UP000095728};
RN   [1] {ECO:0000313|Proteomes:UP000095728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEJ85337.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LPNM01000007; OEJ85337.1; -; Genomic_DNA.
DR   STRING; 56408.A0A1E5REL3; -.
DR   InParanoid; A0A1E5REL3; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000095728; 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   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; IPR001412; aa-tRNA-synth_I_CS.
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.
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:UP000095728}.
FT   DOMAIN          14..180
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04558"
FT   DOMAIN          183..269
FT                   /note="Glutaminyl-tRNA synthetase class Ib non-specific
FT                   RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04557"
FT   DOMAIN          276..589
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          593..696
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib anti-
FT                   codon binding"
FT                   /evidence="ECO:0000259|Pfam:PF03950"
FT   DOMAIN          708..764
FT                   /note="tRNA synthetases class I (E and Q) anti-codon
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF20974"
FT   REGION          203..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   UNSURE          84
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:OEJ85337.1"
SQ   SEQUENCE   827 AA;  94594 MW;  5A616D0EA0F3FF5F CRC64;
     MTTTTSNNTP SVDQLTESFS KIGFEDGKIK EILKNNKLSV ILLELIQLSD NTASAQSFGK
     IERGLIHNLA SFINKSKSVG AKDLSQFKIV VDYILNGKLK TNLQVEAAFK YVADDLSKTT
     DESFDQYCGV GVVVTEDQIR SRVMDYVQQH XEEIKEKRYV IVPALFANIK ALPELKWAEP
     KYFKPIIDAE ILKVLGPKDE RDFVKKEKKK SANNNNNNNN KNGEKKDNKN GNSNAALHKE
     RNMFAEGFLG DLHKVGENPQ AYPELMEQHL KVTQGKVRTR FPPEPNGYLH IGHSKAIMVN
     FGYAKYHDGV CYLRFDDTNP EAEAPEYFES IKSMVSWLGF KPWKITYSSD YFDELYALAE
     VLIKNGKAYV CHCTGDEIKR SRGIKEDGTP GGERKACIHR TQTVEETLSK FRDMRDGKYQ
     PGEATLRMXQ NLESPSPQMW DLIAYRVLNA PHPRTGTKWK IYPTYDFTHC LVDSFENITH
     SLCTTEFYLS RESYEWLCDQ VHVFRPAQRE YGRLNITGTV LSKRKIAKLV TGGYVRGWND
     PRLFTLEAIR RRGVPPGAIL SFINTLGVTT STTNIQVVRF ESAIRKYLED TTPRLMFVQD
     PILVEIENLD DDFELDCSIP YRPGCPEFGE RVVKFTNKVY IERSDFSNDA NNKEFFRLTP
     NQPVGLIRVP HNLVFKSLET DPKDPSKITK IVCHYDVEKT TKKPKTYIQW VPVATGIKIH
     ETRIYNQLFK SENPLSVENY LDDLNPESEV VLTNSVIEPN FNEVVAKSPW VMDAVKKSEF
     YVEEADPTRK EVVRFQAMRC GYFCLDSDST NDKIVLNRIV SLKDGSK
//
DBGET integrated database retrieval system