(data stored in SCRATCH zone)

SWISSPROT: C6WGL3_ACTMD

ID   C6WGL3_ACTMD            Unreviewed;       464 AA.
AC   C6WGL3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=Amir_0360 {ECO:0000313|EMBL:ACU34329.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34329.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34329.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys). {ECO:0000256|HAMAP-
CC       Rule:MF_00041, ECO:0000256|SAAS:SAAS00676348}.
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:SAAS00676353}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00041,
CC       ECO:0000256|SAAS:SAAS00676344}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001630; ACU34329.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6WGL3; -.
DR   STRING; 446462.Amir_0360; -.
DR   EnsemblBacteria; ACU34329; ACU34329; Amir_0360.
DR   KEGG; ami:Amir_0360; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; HECEIAQ; -.
DR   OrthoDB; POG091H004K; -.
DR   Proteomes; UP000002213; 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; C6WGL3.
DR   SWISS-2DPAGE; C6WGL3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676352, ECO:0000313|EMBL:ACU34329.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676343};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676342};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676349, ECO:0000313|EMBL:ACU34329.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676351};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676346};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00676350};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00676347}.
FT   DOMAIN      339    400       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   464 AA;  51201 MW;  EFBD71122A81E874 CRC64;
     MSLHIYDTAS RELREFRPQI SGTASIYVCG ATVQGVPHIG HVRSGLNFDV LRRWLARTHE
     RVVLVRNVTD IDDKILVKSA QHDRTWWDWA FEHERAFDDA YEALGCLPPT YAPRATGHVT
     QMVELMRRLI DAGHAYAANG DVYFSVSSFP EYGKLSGQRV DEVQQGESEL TGKRDPRDFT
     LWKAAKPGEP SWPTPWGDGR PGWHLECSAM ATEYLGSTFD VHGGGIDLIF PHHENEQAQS
     RAVGDGFARY WMHNAWVTLS GEKMSKSLGN TVSIPAMLEQ VRAPELRYYL VGPHYRSTIE
     YSPTALDEAV TAYRRIESFL RRVVERTGAV DAGGELGEDF VSSMDDDMGT PGALAAVHKR
     VREGNTALES GDDTGARAAA SSVRAMTAVL GLDPLSERWS ASAGRESGTS RALKALVDRV
     LADRVAARKE RDFARADALR DSLLAAGIAV EDTPDGPLWT LKDS
//

If you have problems or comments...

PBIL Back to PBIL home page