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Database: UniProt
Entry: A0A2K5HSC3_COLAP
LinkDB: A0A2K5HSC3_COLAP
Original site: A0A2K5HSC3_COLAP 
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
//
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