ID A0A3Q2GJB7_CYPVA Unreviewed; 837 AA.
AC A0A3Q2GJB7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000027340.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000027340.1}
RP IDENTIFICATION.
RG Ensembl;
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};
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DR AlphaFoldDB; A0A3Q2GJB7; -.
DR STRING; 28743.ENSCVAP00000027340; -.
DR Ensembl; ENSCVAT00000029900.1; ENSCVAP00000027340.1; ENSCVAG00000013626.1.
DR GeneTree; ENSGT00390000006347; -.
DR Proteomes; UP000265020; 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; 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:UP000265020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 135..546
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 744..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 95093 MW; 248BD1474BB55F67 CRC64;
MSFADFSATC CSAGNSANVC PLVSAAFEFG FLLQINEEAV LTAALNDYLT SRSYLAGFGP
SQVDLRAFRL LPRPPDPQHV HALRWYRHIS ALQQDLAADG SMKGRRVQPP WSPPAGTEVP
QLRLYNSLTR TKEPFVPQKG NRVTWYCCGP TVYDASHMGH ARSYISFDIL RRILRDYFKY
DVFYCMNITD IDDKIIKRAR QNHLLDQYRE KQPKAAKILQ DVLSARVPFQ EQLVSTTDPD
KKQMLERLDA AVTSALQPLQ GAMEKNAADE VLQPLAQVLL EKSKDLLSEW LDKQFGSQVT
ENSIFSVLPK YWEGEFHKDM EALNVLPADV LTRVSEYVPE IVEFVEKVVS NGYGYESNGS
VYFDTQKFDS SPQHSYAKLV PEAVGDQKAL QEGEGDLSIS ADRLSEKKSQ NDFALWKASK
PGEPSWDSPW GKGRPGWHIE CSAMAGSILG ESMDIHGGGF DLRFPHHDNE LAQSEAFFEN
DHWVRYFLHT GHLTIAGCKM SKSLKNFITI KDALAKNTAR QLRLAFLMHS WKDTLDYSSN
TMESAVQYEK FLNEFFLNVK DILRAPTDLT GRFEKWEAAE IELNNSFYDR KSAVHQALCD
NMDTRGAMEE MRLLVSHSNS YIAGRKSSKL RPNRLLLESI ASYLTNMLKI FGAIEGSDPI
GFPVGGQTVD LESTVMPYLA VLSDFRENVR RIAREQKVTA LLQLCDVVRD DTLPELGVRL
EDHEGQPTVV KLVDKETLLK EKEDKKKMEE EKKRKKEEAA RRKQEQEMAK LAKMKVPPCE
MFRSETDKYS SFDDTGFPTH DAEGKELSKG QAKKLRKLYE AQEKLHNEYL QMNQNGN
//
