(data stored in ACNUC7421 zone)

SWISSPROT: A0LFC2_SYNFM

ID   A0LFC2_SYNFM            Unreviewed;       644 AA.
AC   A0LFC2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Threonine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00184};
DE            EC=6.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00184};
DE   AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184};
DE            Short=ThrRS {ECO:0000256|HAMAP-Rule:MF_00184};
GN   Name=thrS {ECO:0000256|HAMAP-Rule:MF_00184};
GN   OrderedLocusNames=Sfum_0424 {ECO:0000313|EMBL:ABK16124.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16124.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16124.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+)
CC         + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-
CC         COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215;
CC         EC=6.1.1.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00184,
CC         ECO:0000256|SAAS:SAAS01116705};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00184};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00184};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184,
CC       ECO:0000256|SAAS:SAAS00711700}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00184,
CC       ECO:0000256|SAAS:SAAS00711584}.
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DR   EMBL; CP000478; ABK16124.1; -; Genomic_DNA.
DR   RefSeq; WP_011697297.1; NC_008554.1.
DR   STRING; 335543.Sfum_0424; -.
DR   EnsemblBacteria; ABK16124; ABK16124; Sfum_0424.
DR   KEGG; sfu:Sfum_0424; -.
DR   eggNOG; ENOG4105C22; Bacteria.
DR   eggNOG; COG0441; LUCA.
DR   HOGENOM; HOG000003880; -.
DR   KO; K01868; -.
DR   OMA; FYYDFAY; -.
DR   OrthoDB; 900765at2; -.
DR   BioCyc; SFUM335543:G1G7I-432-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451; PTHR11451; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR01047; TRNASYNTHTHR.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFC2.
DR   SWISS-2DPAGE; A0LFC2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711497, ECO:0000313|EMBL:ABK16124.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711575}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711491};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711703};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS01079684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711709};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711504};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00184};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00184};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00184, ECO:0000256|SAAS:SAAS01079676}.
FT   DOMAIN      242    533       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   REGION      242    533       Catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
FT   COILED      118    138       {ECO:0000256|SAM:Coils}.
FT   METAL       334    334       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
FT   METAL       385    385       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
FT   METAL       510    510       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
SQ   SEQUENCE   644 AA;  72788 MW;  4C37A020242C3BC0 CRC64;
     MSAEISVTLA DGTTKSFPRG VSAGEVLKAS GGPNGWVAAK VNGVPVDLIV GIEEDAAVEG
     IRADSEVGLE ILRHSAAHVM AQAVKSLFPE ARVAIGPAID NGFYYDFEVE RPFTQDDLDR
     IEAKMKELVG AKLKFERKVL PRDEAIDFFT RRGEGYKVEL LQGFSDPTVS FYTQGDFVDL
     CRGPHVPHSG YVRAFKLTSV AGAYWRGDEH NAMLQRIYGT AFADRDALKK YLHFLEEAQK
     RDHRRLGREL DLFSFSDEVG AGMVIYHPRG ALLRHILEAF EKREHLRRGY HIVMGPTLLK
     TELWKRSGHF EHYRENMYFT EIEEQSYGIK PMNCLAHMLI YKSRLRSYRD LPLRYFELGT
     VHRHERSGVL HGLTRVRQFT QDDAHILCTP EQLHGEIQSI IDFVIEVMGI FGFNHEMEIS
     TRPAKSIGSD EDWERATSAL IDALEDKGIP YQVCEGEGAF YGPKIDVKLR DALDRKWQCA
     TIQCDFTLPD RFDLTYVGVD GNRHRPVMVH RVVLGSLERF IGVLVEHFAG AFPTWLAPVQ
     AIVVTVTDGQ IEFARNMYDR LREAGVRVEL DDRNEKLGYK IREAQMQKVP YMLVIGDREV
     AAGGVAPRRR DGTQLELIAP EAFAAMIQKE CLEATKGRVG LGIV
//

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