(data stored in ACNUC7421 zone)

SWISSPROT: C4KJK7_SULIK

ID   C4KJK7_SULIK            Unreviewed;       470 AA.
AC   C4KJK7;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
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=M164_0091 {ECO:0000313|EMBL:ACR40727.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40727.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40727.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys). {ECO:0000256|HAMAP-
CC       Rule:MF_00041}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00041}.
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DR   EMBL; CP001402; ACR40727.1; -; Genomic_DNA.
DR   RefSeq; WP_012735372.1; NC_012726.1.
DR   ProteinModelPortal; C4KJK7; -.
DR   EnsemblBacteria; ACR40727; ACR40727; M164_0091.
DR   KEGG; sid:M164_0091; -.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; HECEIAQ; -.
DR   OrthoDB; POG093Z01UF; -.
DR   BioCyc; SISL426118:GI01-91-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; C4KJK7.
DR   SWISS-2DPAGE; C4KJK7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000313|EMBL:ACR40727.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000313|EMBL:ACR40727.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   DOMAIN      355    414       DALR_2. {ECO:0000259|SMART:SM00840}.
FT   MOTIF        33     43       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   MOTIF       266    270       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   METAL        31     31       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       209    209       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       234    234       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       238    238       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   BINDING     269    269       ATP. {ECO:0000256|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   470 AA;  55172 MW;  9CF64970203B5322 CRC64;
     MDFRIRIYNS LGRKLEEFNT INPNLVKMYV CGPTVYDYVH IGHGRTFVVF DAISRYLRLK
     GYTVIRVQNI TDIDDKIIKK SRDTGKDWNE IVNYYTKDYL DMLSQLKVKI DIHPRVTHHI
     KEIINFVQKL IDKGHAYVAP SGSVYFDVDT YPDYGELSNT KKEEWNQGEE FVKEKKHSYD
     FALWKAWKPG EPYWESPWGK GRPGWHIECS TMSTRYLGER FDIHGGGADL VFPHHENERA
     QTEALTGEKW VSYWVHSAFV TIRKEKMSKS LGNIIPLNEA IKKWGPSVLR YWYLTSHYRS
     PIDFSEEALE QAKSALQRIK DSMAIIRNII SEGPKFYAKD DDIKVYREIL NNLDSFHTAM
     SNDFDTSTAL SYIHEIVRLV FSTLQYSRDF LGAMLAFEAL SQFNEVFGVM DEEFYPTYDK
     MYKVIDAVVD IRNQLRQMKL YEISDKIREE LLKAGVRILD SKDKSTWRFE
//

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