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Database: UniProt
Entry: A0A2I3SS26_PANTR
LinkDB: A0A2I3SS26_PANTR
Original site: A0A2I3SS26_PANTR 
ID   A0A2I3SS26_PANTR        Unreviewed;       747 AA.
AC   A0A2I3SS26;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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 {ECO:0000313|Ensembl:ENSPTRP00000079343.1,
GN   ECO:0000313|VGNC:VGNC:11276};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000079343.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000079343.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000079343.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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};
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DR   EMBL; AACZ04062768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3SS26; -.
DR   Ensembl; ENSPTRT00000086288.1; ENSPTRP00000079343.1; ENSPTRG00000003188.6.
DR   VGNC; VGNC:11276; CARS1.
DR   GeneTree; ENSGT00390000006347; -.
DR   Proteomes; UP000002277; Chromosome 11.
DR   Bgee; ENSPTRG00000003188; Expressed in fibroblast and 21 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   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; 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; 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};
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:UP000002277};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          43..451
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  85452 MW;  CD8A4FA8C1277886 CRC64;
     LLDHSGQGKG RRVQPQWSPP AGTQPCRLHL YNSLTRNKEV FIPQDGKKVT WYCCGPTVYD
     ASHMGHARSY ISFDILRRVL KDYFKFDVFY CMNITDIDDK IIKRARQNHL FEQYREKRPE
     AAQLLEDVQA ALKPFSVKLN ETTDPDKKQM LERIQHAVQL ATEPLEKAVQ SRLTGEEVNS
     CVEVLLEEAK DLLSDWLDST LGCDVTDNSI FSKLPKFWEG DFHRDMEALN VLPPDVLTRV
     SEYVPEIVNF VQKIVDNGYG YVSNGSVYFD TAKFASSEKH SYGKLVPEAV GDQKALQEGE
     GDLSISADRL SEKRSPNDFA LWKASKPGEP SWPCPWGKGR PGWHIECSAM AGTLLGASMD
     IHGGGFDLRF PHHDNELAQS EAYFENDCWV RYFLHTGHLT IAGCKMSKSL KNFITIKDAL
     KKHSARQLRL AFLMHSWKDT LDYSSNTMES ALQYEKFLNE FFLNVKDILR APVDITGQFE
     KWGEEEAELN KNFYDKKTAI HKALCDNVDT RTVMEEMRAL VSQCNLYMAA RKAMRKRPNQ
     ALLENIALYL THMLKIFGAV EEDSSLGFPV GGPGTSLSLE ATVMPYLQVL SEFREGVRKI
     AREQKVPEIL QLSDALRDDI LPELGVRFED HEGLPTVVKL VDRNTLLKER EEKRRVEEEK
     RKKKEEAARR KQEQEAAKLA KMKIPPSEMF LSETDKYSKF DENGLPTHDM EGKELSKGQA
     KKLKKLFEAQ EKLYKEYLQM AQNGSFQ
//
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