(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBV7_SEGRD

ID   D6ZBV7_SEGRD            Unreviewed;       467 AA.
AC   D6ZBV7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
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=Srot_0447 {ECO:0000313|EMBL:ADG96934.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96934.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96934.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96934.1; -; Genomic_DNA.
DR   RefSeq; WP_013137390.1; NC_014168.1.
DR   STRING; 640132.Srot_0447; -.
DR   EnsemblBacteria; ADG96934; ADG96934; Srot_0447.
DR   KEGG; srt:Srot_0447; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; SROT640132:G1GLH-447-MONOMER; -.
DR   Proteomes; UP000002247; 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; D6ZBV7.
DR   SWISS-2DPAGE; D6ZBV7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043709, ECO:0000313|EMBL:ADG96934.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043696};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:ADG96934.1};
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:UP000002247};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043692}.
FT   DOMAIN      338    399       DALR_2. {ECO:0000259|SMART:SM00840}.
FT   MOTIF        31     41       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   MOTIF       263    267       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   METAL        29     29       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     266    266       ATP. {ECO:0000256|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   467 AA;  51509 MW;  2CEF744964F61194 CRC64;
     MTLRLYDTRT RVVREFAPLR PGQVSVYLCG ATVQGKPHVG HLRSAVVFDV LRRWLLAKGF
     DVLFIRNVTD IDDKILAKAA EAGRPWWEWA ATHEREFSNA YNRLGVLPPS AEPRATGHIT
     QMTTCIERLI ERGHAYTGAG DVYFDVRSLP EYGKLSGHQP DDVHQGESAG AGKRDPRDFT
     LWKGSKPGEP WWPTPWGPGR PGWHLECTAM ATAYLGSEFD IHCGGMDLVF PHHENELAQA
     HGAGDQFARF WLHNGWLSLG GEKMSKSLGN VLSLEELLTA VRPQELRYYL GCAHYRSTQE
     FSIEAVVEAA VAYQRLESFV LRAAEQFGEI PVGQVADEFA SALDDDLAVP KALAELQRQA
     KQGNTELADA DPAAAATAAS VRAMLAVLGC DPFDPMWASG REREEKAAFR AVDVLVEAEL
     SRREAARAGK DWATADDVRD RLRKAGIIVT DGPDGPKWSL ETNGGQP
//

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