UniProt: A0A1L8GE24

Database: UniProt
Entry: A0A1L8GE24_XENLA

LinkDB:  A0A1L8GE24_XENLA 
Original site:  A0A1L8GE24_XENLA

All links

Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (7)   
   InterPro (6)   
   Pfam (1)   
All databases (15)   

Download RDF

ID   A0A1L8GE24_XENLA        Unreviewed;       823 AA.
AC   A0A1L8GE24;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Cysteine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00039362};
DE            EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN   Name=cars1.S {ECO:0000313|RefSeq:XP_018114920.1,
GN   ECO:0000313|Xenbase:XB-GENE-5825997};
GN   Synonyms=cars {ECO:0000313|RefSeq:XP_018114920.1}, cars.S
GN   {ECO:0000313|RefSeq:XP_018114920.1}, cars1
GN   {ECO:0000313|RefSeq:XP_018114920.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018114920.1};
RN   [1] {ECO:0000313|RefSeq:XP_018114920.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018114920.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018114920.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the ATP-dependent ligation of cysteine to
CC       tRNA(Cys). {ECO:0000256|ARBA:ARBA00037196}.
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:ARBA00036537};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC         Evidence={ECO:0000256|ARBA:ARBA00036537};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_018114920.1; XM_018259431.2.
DR   AlphaFoldDB; A0A1L8GE24; -.
DR   STRING; 8355.A0A1L8GE24; -.
DR   MaxQB; A0A1L8GE24; -.
DR   PaxDb; 8355-A0A1L8GE24; -.
DR   GeneID; 380479; -.
DR   AGR; Xenbase:XB-GENE-5825997; -.
DR   CTD; 380479; -.
DR   Xenbase; XB-GENE-5825997; cars1.S.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 380479; Expressed in stomach and 19 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00672; CysRS_core; 1.
DR   CDD; cd10310; GST_C_CysRS_N; 1.
DR   Gene3D; 1.20.1050.130; -; 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; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_018114920.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          121..528
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
SQ   SEQUENCE   823 AA;  94457 MW;  C7874628D77E2A9B CRC64;
     MTESWEQVLS ISEDKVSMKA LNDFLSTRSY IQGYTYSQAD VQAFMQLEGP PPDHLFHVIR
     WYKHIAALST EAAKHSDFRN GQSCKGRRTQ PPWSAPNTNE QPGLRLYNSL TRSKELFFPQ
     VGRKVTWYCC GPTVYDASHM GHARSYISFD ILRRVLRDYF KYDVFYCMNI TDIDDKIIKR
     ARQRHLFQQY RESNPPHSDL LQDVNTALIP FLQRISETND PDKKQMLERI QTAVSAALLP
     LQDALNKNTG AEELQKHSQV LMEAAVDLLS DWLDEKHGAQ IADNSIFSQL PKYWEGEYHK
     DMEALNVLTP DVLTRVSEYV PEIVAFVQKI VDNGYGYVSN GSVYFSTAKF HDSENHFYAK
     LVPEAVGDQK ALQEGEGDLS ISADRLSEKQ SPNDFALWKA SKPGEPSWES PWGKGRPGWH
     IECSAMAGSI LGESMDIHGG GFDLRFPHHD NELAQSEAYF DNDHWVRYFL HTGHLTIAGC
     KMSKSLKNFI TIKDALQKNT ARQLRLAFLM HSWKDTLDYS NNTMESAVQY EKFMNEFFLN
     VKDLLRAPTD ITGQFVKWEV LEIELNNCFY SKKAAIHEAL CDNIDTRTVM EEMRSLVSQC
     NSYIASKKVA KQFPNRMLLR SISSYLTSML KVFGAIEGEE VIGFPIGGSE NSMNLESTVM
     PYLQVLSQFR EGVRQIARQH KVTEVLQLSD LLRDDILPEL GVRLEDHEGL PTVVKLVDRE
     TLLKEKEEKR KAEEEKQRKK EEAARKKQQQ EAAKLEKMKI SPSQMFTLET DKYSQFDESG
     FPTHDTEGKE LSKGQTKKLR KLFEVQEKLH KEYLQMVQNG TTA
//

DBGET integrated database retrieval system