(data stored in SCRATCH zone)

SWISSPROT: Q2IMP1_ANADE

ID   Q2IMP1_ANADE            Unreviewed;       323 AA.
AC   Q2IMP1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00346794};
DE            Short=Glu-Q-RSs {ECO:0000256|HAMAP-Rule:MF_01428};
DE            EC=6.1.1.- {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00346799};
GN   Name=gluQ {ECO:0000256|HAMAP-Rule:MF_01428};
GN   OrderedLocusNames=Adeh_0295 {ECO:0000313|EMBL:ABC80071.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80071.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate
CC       in presence of ATP and the subsequent transfer of glutamate onto a
CC       tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-
CC       dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the
CC       wobble position of the QUC anticodon. {ECO:0000256|HAMAP-
CC       Rule:MF_01428}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01428};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01428};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. GluQ subfamily. {ECO:0000256|HAMAP-Rule:MF_01428,
CC       ECO:0000256|SAAS:SAAS00542009}.
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DR   EMBL; CP000251; ABC80071.1; -; Genomic_DNA.
DR   RefSeq; WP_011419354.1; NC_007760.1.
DR   STRING; 290397.Adeh_0295; -.
DR   EnsemblBacteria; ABC80071; ABC80071; Adeh_0295.
DR   KEGG; ade:Adeh_0295; -.
DR   eggNOG; ENOG4106F3G; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01885; -.
DR   OMA; WLLRMED; -.
DR   BioCyc; ADEH290397:G1G5W-302-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01428; Glu_Q_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR022380; Glu-Q_TRNA(Asp)_Synthase.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   TIGRFAMs; TIGR03838; queuosine_YadB; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMP1.
DR   SWISS-2DPAGE; Q2IMP1.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315323};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315316};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315306,
KW   ECO:0000313|EMBL:ABC80071.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|SAAS:SAAS00315314};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01428,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00315320};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01428, ECO:0000256|SAAS:SAAS00315315}.
FT   DOMAIN        4    313       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   REGION        6     10       Glutamate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01428}.
FT   MOTIF         9     19       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   MOTIF       250    254       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   METAL       106    106       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       108    108       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       130    130       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   METAL       134    134       Zinc. {ECO:0000256|HAMAP-Rule:MF_01428}.
FT   BINDING      42     42       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     194    194       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     212    212       Glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01428}.
FT   BINDING     253    253       ATP. {ECO:0000256|HAMAP-Rule:MF_01428}.
SQ   SEQUENCE   323 AA;  34295 MW;  5B3A46B52106BDE5 CRC64;
     MSSRGRFAPS PTGPLHLGNA RTALLSWLAA RTAGSAYVMR VEDLDGPRVR PGLEARILEE
     LRWLGLDWDE GPDVGGPLGP YRQSERLPRY AAALERLRAA GLAYPCFCSR AEIAAASQAP
     HGASDEGPRY PGTCRELSPA EVARRSASRR PAWRLRVEPG PVAFEDGVHG PVAHDVAAEV
     GDFVVARADG VPAYQLAVVV DDAAMQVGEV VRGDDLLPST ARQLLLYRAL DLAPPRFAHV
     PLVVGPDGAR LAKRHGALSL GELRSRGADP RAVVALLAGL SGLAAGHPHD ACTPRELIGR
     FSLARLPRAP AVLSPERIAA LLP
//

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