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Database: UniProt
Entry: E1QTX4_VULDI
LinkDB: E1QTX4_VULDI
Original site: E1QTX4_VULDI 
ID   E1QTX4_VULDI            Unreviewed;       491 AA.
AC   E1QTX4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=Vdis_0366 {ECO:0000313|EMBL:ADN49771.1};
OS   Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS   IC-017).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Vulcanisaeta.
OX   NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN49771.1, ECO:0000313|Proteomes:UP000006681};
RN   [1] {ECO:0000313|EMBL:ADN49771.1, ECO:0000313|Proteomes:UP000006681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC   {ECO:0000313|Proteomes:UP000006681};
RX   PubMed=21304741;
RA   Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA   Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA   Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT   017).";
RL   Stand. Genomic Sci. 3:117-125(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC   {ECO:0000313|Proteomes:UP000006681};
RX   DOI=10.4056/sigs.1113067;
RA   Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA   Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA   Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT   017T).";
RL   Stand. Genomic Sci. 3:117-125(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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001080, ECO:0000256|HAMAP-
CC         Rule:MF_00041};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00041}.
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DR   EMBL; CP002100; ADN49771.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1QTX4; -.
DR   STRING; 572478.Vdis_0366; -.
DR   KEGG; vdi:Vdis_0366; -.
DR   eggNOG; arCOG00486; Archaea.
DR   HOGENOM; CLU_013528_0_1_2; -.
DR   Proteomes; UP000006681; 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; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00041};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000006681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT   DOMAIN          367..430
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   MOTIF           38..48
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           280..284
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   491 AA;  56726 MW;  7274060866811F4D CRC64;
     MYANSKELPI IVYNTASKNL EKITLLRPGL ARIYVCGLTP YDSMHVGHAR TFVFYDIFRR
     YLEYLGVEVR FVTNFTDIDD KIINRARQEF GGELINRWYE VPSRYIKEFF DAMDRLYVKR
     AYAYPKVTEN INDMLKWIQE LVSKNLAYVS PDGSVYFDIT KVPRYGEFSG QKIEDLIAGA
     RVEPEPGKRN PLDFALWKSW SEGEPWWNSP WSPGRPGWHL ECVVMSSKYL GVPFDIHGGG
     QDLIFPHHEN EIAIARVYFG IDYFARYWIH VGLVTIRGQK MSKSLGNIIP IMEVLRKYDG
     EVLRLYYAMT QYRKPMDFDP DALDQVRNSL MSVYAAYDML TEAINEAPDT GDRDNELLSK
     VNEFVNSFEE SLNNDINTSG AVAALMDFAR YIASTVIYNT QHYSRNALTN ALTAFSDLAN
     ILGILNRTRL PPSLVSLIDT LIRIRAQLRA RKMFDVADEI RNELSKLGVV VSDVGNKTYW
     YIDRDKITQW H
//
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