(data stored in SCRATCH zone)

SWISSPROT: C8W3W4_DESAS

ID   C8W3W4_DESAS            Unreviewed;       500 AA.
AC   C8W3W4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Dtox_0265 {ECO:0000313|EMBL:ACV61218.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61218.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61218.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00041,
CC       ECO:0000256|SAAS:SAAS01085510}.
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DR   EMBL; CP001720; ACV61218.1; -; Genomic_DNA.
DR   RefSeq; WP_015755939.1; NC_013216.1.
DR   STRING; 485916.Dtox_0265; -.
DR   EnsemblBacteria; ACV61218; ACV61218; Dtox_0265.
DR   KEGG; dae:Dtox_0265; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; DACE485916:G1GFV-275-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
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; C8W3W4.
DR   SWISS-2DPAGE; C8W3W4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043709, ECO:0000313|EMBL:ACV61218.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043696};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043701};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043689, ECO:0000313|EMBL:ACV61218.1};
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   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043668};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043692}.
FT   DOMAIN      367    432       DALR_2. {ECO:0000259|SMART:SM00840}.
FT   MOTIF        29     39       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   MOTIF       264    268       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   METAL        27     27       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       207    207       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       232    232       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       236    236       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   BINDING     267    267       ATP. {ECO:0000256|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   500 AA;  56880 MW;  2BAA059B6B49574E CRC64;
     MLLYNTLSRQ KEEFVPAIPG RVSMYVCGPT TYNFIHLGNA RPLVFFDTVR RYLIYKGYQV
     LYVQNFTDID DKIIKRAAEE KLDPSALAFK YTEEYYIDAT SLNVMMADIH PKVSDHMAEI
     IELVEKLVQK GFAYQSDGDV YFEVRRFKDY GKLSGRALED MLAGARVEVN EKKRDPMDFA
     LWKAAKPGEP SWNSPWGQGR PGWHIECSAM SLKYLGENFD MHGGGADLIF PHHENEIAQS
     EAATGEPLAR YWLHNGFITV NQEKMSKSLG NFFLVREILD KFSPEVVRFF LLGTHYRSPL
     DFDDEKLAVV EKGLDRIRTS IQLLGEACQR AGVDFSMINA KEKPARVTSI IDTRHSSMKA
     FIKIKTSFEQ AMEDDFNTAL AVGSLFELAK ETNILVQSLG PKISEQEKAC LLQAAELFKL
     FNQVLGIFKE DLCTGYPLVT PVDESGDGML EAVMQMLLDI RNEARKNKNW ALSDRIRDAL
     KDINVILEDT PQGTRWKKQA
//

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