(data stored in SCRATCH zone)

SWISSPROT: D1CDJ3_THET1

ID   D1CDJ3_THET1            Unreviewed;       492 AA.
AC   D1CDJ3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000256|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000256|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=Tter_0077 {ECO:0000313|EMBL:ACZ40999.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40999.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40999.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
CC       {ECO:0000256|HAMAP-Rule:MF_00022, ECO:0000256|SAAS:SAAS00986951}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00022, ECO:0000256|SAAS:SAAS01118679};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022,
CC       ECO:0000256|SAAS:SAAS00986956}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022,
CC       ECO:0000256|SAAS:SAAS00986955}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00022, ECO:0000256|SAAS:SAAS00986945}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00022}.
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DR   EMBL; CP001825; ACZ40999.1; -; Genomic_DNA.
DR   RefSeq; WP_012874034.1; NC_013525.1.
DR   STRING; 525904.Tter_0077; -.
DR   EnsemblBacteria; ACZ40999; ACZ40999; Tter_0077.
DR   KEGG; ttr:Tter_0077; -.
DR   eggNOG; ENOG4105C20; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252720; -.
DR   KO; K01885; -.
DR   OMA; AYYAFDT; -.
DR   OrthoDB; 1409413at2; -.
DR   BioCyc; TTER525904:G1GGS-77-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00808; GluRS_core; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 1.10.8.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020752; aa-tRNA-synth_I_codon-bd_sub1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDJ3.
DR   SWISS-2DPAGE; D1CDJ3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00986958,
KW   ECO:0000313|EMBL:ACZ40999.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00986943};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|SAAS:SAAS00986961};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00986946};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00986944};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000256|SAAS:SAAS00986963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN        4    321       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   COILED      395    415       {ECO:0000256|SAM:Coils}.
FT   MOTIF        11     21       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   MOTIF       252    256       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   BINDING     255    255       ATP. {ECO:0000256|HAMAP-Rule:MF_00022}.
SQ   SEQUENCE   492 AA;  55666 MW;  6F0374557C5527BA CRC64;
     MNSEVRVRFP PSPTGYLHVG NLRTAVFNWL LARHHGGKFI LRIEDTDRAR VVPGAVEVIY
     ETLRWIGIDW DEGPDIGGPH APYVQSERKE IYREYAELLI SQGKAYRCFC SQERLEALRE
     EQRKNNLPTR YDRKCRYLGP EEAKRLVDSG QPYVVRFATP LEGTTTMVDL LRGPVTYQND
     QIDDFVILKS DGYPPYHFAV VVDDHLMGIT HVLRGDEYIS SGARDILLHE ALGWNPPLYA
     HTAIILGPDR SRLSKRHGAL PALEYRDIGI IPEAMFNYLA LLGASYSADR EIFSREELIE
     LFDIDKMSPS PAIFDANKLE WMNAYYINHV LSVDDLASRV KPILENAGLV KTEDLDEGYL
     IEVIGLVKDR IKLLPDVVEL TDFFFRDPDP SAEEIAGKKL TLQEAQELLQ KVKDRVSPID
     NWSEEILETE LRSMASELGV KTGTLFMLIR VAITGKTASP GLFETMAVLG KDRTISRIGR
     AIDKLDLVVH GG
//

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