(data stored in SCRATCH zone)

SWISSPROT: A4AWS3_MARSH

ID   A4AWS3_MARSH            Unreviewed;       646 AA.
AC   A4AWS3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
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=FB2170_00005 {ECO:0000313|EMBL:EAQ99590.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99590.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99590.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a
CC       two-step reaction: L-threonine is first activated by ATP to form
CC       Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
CC       {ECO:0000256|SAAS:SAAS00889270}.
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       ECO:0000256|SAAS:SAAS00711729}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184,
CC       ECO:0000256|SAAS:SAAS00230800}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00184,
CC       ECO:0000256|SAAS:SAAS00711584}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00184}.
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DR   EMBL; CP002157; EAQ99590.1; -; Genomic_DNA.
DR   RefSeq; WP_013304699.1; NC_014472.1.
DR   STRING; 313603.FB2170_00005; -.
DR   EnsemblBacteria; EAQ99590; EAQ99590; FB2170_00005.
DR   KEGG; fbc:FB2170_00005; -.
DR   eggNOG; ENOG4105C22; Bacteria.
DR   eggNOG; COG0441; LUCA.
DR   HOGENOM; HOG000003879; -.
DR   KO; K01868; -.
DR   OMA; FYYDFAY; -.
DR   OrthoDB; 900765at2; -.
DR   BioCyc; MSP313603:G1GNS-274-MONOMER; -.
DR   Proteomes; UP000001602; 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; 3.10.20.30; -; 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; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
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; PF02824; TGS; 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   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AWS3.
DR   SWISS-2DPAGE; A4AWS3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711497, ECO:0000313|EMBL:EAQ99590.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00711575};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00230803};
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:SAAS00750945};
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:UP000001602};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00909903};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00184,
KW   ECO:0000256|SAAS:SAAS00909895};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00184, ECO:0000256|SAAS:SAAS00750967}.
FT   DOMAIN      242    541       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
FT   METAL       337    337       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
FT   METAL       388    388       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
FT   METAL       518    518       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_00184}.
SQ   SEQUENCE   646 AA;  73326 MW;  D9DD92A8E3C06F0E CRC64;
     MIKITLPDGT VKEYSKGSTA MDIAKSISEG LARNVISAKF NDTIIETVTP IIEDGSLTLF
     TWNNDEGKKA FWHSSSHIVA QALEELFPGA KLTIGPAIEN GFYYDVDFGE HTVSDKDFPA
     IEKKALEIAR GKHDFKMRSV SKQEALEKYK SQKNEFKVEL IENLEDGTIT FCDHDTFTDL
     CRGGHIPNTG IVKAIKILSV AGAYWRGDEK NKQLTRVYGI SFPKQKELTA YLQLLEEAKK
     RDHRKLGKEL ELFTFSQKVG QGLPLWLPKG AALRERLEQF LKKAQKKAGY EMVVTPHIGQ
     KELYVTSGHY AKYGEDSFQP IHTPKDDEEF LLKPMNCPHH CEIYNSRPFS YRELPKRYAE
     FGTVYRYEQS GELHGLTRVR GFTQDDAHIF CTPDQLDQEF KDVIDLSLYV LSSLGFENFK
     AQVSVRDLDT PEKYIGSVEN WEKAENAIIN AAKEKGLDFV VESGEAAFYG PKLDFMVKDA
     LGRNWQLGTI QVDYNLPERF DLTYKGSDNE SHRPVMIHRA PFGSMERFVA LLLEHTGGNF
     PLWLIPEQAI ILPVSEKHEK YAEKVLNSLE NNEIRALIDN RNETVGKKIR EAEMGKLPFM
     LIVGESEEEN NTIAVRRHGG EDIGSINVQA FVDLVTKEIN STLKSF
//

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