(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHP4_GEOS0

ID   A0A0F6BHP4_GEOS0        Unreviewed;       466 AA.
AC   A0A0F6BHP4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=GY4MC1_0089 {ECO:0000313|EMBL:ADP72945.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72945.1};
RN   [1] {ECO:0000313|EMBL:ADP72945.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72945.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC         cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC         Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC         ChEBI:CHEBI:456215; EC=6.1.1.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00041, ECO:0000256|SAAS:SAAS01120893};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041,
CC       ECO:0000256|SAAS:SAAS00043683}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS01085510}.
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DR   EMBL; CP002293; ADP72945.1; -; Genomic_DNA.
DR   RefSeq; WP_013399825.1; NC_014650.1.
DR   EnsemblBacteria; ADP72945; ADP72945; GY4MC1_0089.
DR   GeneID; 29237275; -.
DR   KEGG; gmc:GY4MC1_0089; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; GSP581103:G1GOQ-116-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHP4.
DR   SWISS-2DPAGE; A0A0F6BHP4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043709, ECO:0000313|EMBL:ADP72945.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043696}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043701};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043689,
KW   ECO:0000313|EMBL:ADP72945.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043657};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043715};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043668};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043692}.
FT   DOMAIN          354..417
FT                   /note="DALR_2"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   COILED          310..330
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          397..441
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           32..42
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           267..271
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   METAL           30
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   METAL           210
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   METAL           235
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   METAL           239
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         270
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   466 AA;  54136 MW;  A78AA5D65F203FD6 CRC64;
     MSSIRLYNTL TRKKEPFEPL EPNKVKMYVC GPTVYNYIHI GNARAAIVFD TIRRYLEFRG
     YEVKYVSNFT DVDDKLIKAA RELGEDVPTV AERFIQAYFE DITALGCKKA DVHPRVTENM
     DTIIEFIQAL VEKGYAYEVD GDVYYRTRKF AEYGKLSHQS IDELKAGARI EIGEKKEDPL
     DFALWKAAKE GEICWDSPWG KGRPGWHIEC SAMARKYLGD TIDIHAGGQD LTFPHHENEI
     AQSEALTGKP FAKYWLHNGY LNINNEKMSK SLGNFVLVHD IIRQIDPQVL RFFMLSVHYR
     HPINYSEELL ENAKKGLERL KTAYFNLKHR LQSSTNLTDD DEQWLARIQE QHEAFIREMD
     DDFNTANGIA VLFELAKQAN LYLHEKNTSE RVIHAFLREL EQLLDVLGIT LQEEELLDEE
     IEALIQKRNE ARKNRNFALA DQIRDELRAK NIILEDTPQG TRWKRG
//

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