ID A0A2K5HSC3_COLAP Unreviewed; 832 AA.
AC A0A2K5HSC3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000007247.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000007247.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5HSC3; -.
DR STRING; 336983.ENSCANP00000007247; -.
DR Ensembl; ENSCANT00000026913.1; ENSCANP00000007247.1; ENSCANG00000023607.1.
DR Proteomes; UP000233080; Unplaced.
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};
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:UP000233080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 128..536
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 737..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 94809 MW; 15D46A01817A8AF1 CRC64;
QTPSSGQKHA PDYRSILSIS DEAARAQALN EHLSTRSYVQ GYSLSQADVD AFRQLSTPPA
DPQLFHVARW FRHIEALLGS PCGKGQPCRL QASKGRRVQP QWSPPAGTQP RRLHLYNSLT
RNKEAFIPQD GKKVTWYCCG PTVYDASHMG HARSYISFDI LRRVLKDYFK FDVFYCMNIT
DIDDKIIKRA RQNHLFEQYL EKRPEAAQLL EDVQAALKPF SVKLNETTDP DKKQMLERIQ
HEVQLATEPL EKAVQSRLTG EEVNSCVEVL LEEAKDLLSD WLDSTLGSDV TDNSIFSKLP
KFWEGEFHRD MEALNVLPPD VLTRVSEYVP EIVNFVQKIV DNGYGYVSNG SVYFDTAKFA
SSEKHSYGKL VPEAVGDQKA LQEGEGDLSI SADRLSEKRS PNDFALWKAS KPGEPSWLCP
WGKGRPGWHI ECSAMAGTLL GASMDIHGGG FDLRFPHHDN ELAQSEAYFE NDCWVRYFLH
TGHLTIAGCK MSKSLKNFIT IKDALKKHSA RQLRLAFLMH SWKDTLDYSG NTMESALQYE
KFLNEFFLNV KDILRAPVDI TGQFEKWGEE EAELNKNFYD KKTAIHEALC DNVDTRTVME
EMRALVSQCN LYMAARKAVR KRPNRALLEN IALYLTHMLK IFGAIEEESS LGFPVGGSGT
GLDLESTVMP YLQVLSEFRE GVRKIAREQK VPEVLQLSDA LRDDILPELG VRFEDHEGLP
TVVKLVDRNT LLKEREEKRQ VEEEKRKKKE EAARRKQEQE AAKLAKMKIP PSEMFLSETN
KYSKFDENGL PTHDAEGKEL SKGQAKKVKK LFEAQEKLYK EYLQMPQNGS FQ
//