ID A0A3Q2VJ91_HAPBU Unreviewed; 750 AA.
AC A0A3Q2VJ91;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000011827.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000011827.1}
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; A0A3Q2VJ91; -.
DR Ensembl; ENSHBUT00000032270.1; ENSHBUP00000011827.1; ENSHBUG00000013664.1.
DR GeneTree; ENSGT00390000006347; -.
DR Proteomes; UP000264840; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000264840};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 48..457
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 706..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..687
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 750 AA; 85405 MW; 648BA4FC25653C1A CRC64;
MCKSVLGYVA DVSGIKGKRV QPPWSPPAGT DVPQLRLYNS LTRAKELFVP QKGNKVTWYC
CGPTVYDASH MGHARSYISF DILRRILRDY FKYDVIYCMN ITDIDDKIIK RARQNYLLDQ
YKEKQPQAAQ ILQDVLSART PFQAQLASTT DPDKKQMLEK LDSAVTASLQ PLQAAMESKA
ADEVIRPLVL LENSKDLLAD WLDKQFGSHV TENSIFSLLP KYWEEDYHKD MKALNVLPPD
VLTRVGEYVP EIVEFVRKIV SNGYGYESNG SVYFDTLKFD SSPQHSYAKL VPEAVGDQKA
LQEGEGDLSI SAERLSEKKS PNDFALWKAS KPGEPSWGSP WGKGRPGWHI ECSAMAGSIL
GESMDIHGGG FDLRFPHHDN ELAQSEAFFE NDYWVQYFLH TGHLTISGCK MSKSLKNFIT
IKDALAKNTA RQLRLAFLMH SWKDTLDYSS NTMESAVQYE KFMNEFFLNV KDILRAPTDI
TGQFEKWETA EVELNNSFCD RKSAVHEALC DNVDTRTAME EMRTLVSQSN GYIASKKSAK
LRPNRMLMES IAAYLTNMLK IFGAVEGSDP IGFPMGGQSQ SVDLESAVMP YLTVLSDFRE
RVRKIAREQK VTELLQLCDV VRDDMLPELG VRLEDHEGLP TVVKLVDKET LLKEREEKKR
MEEEKKMKKL EAAKKKQEQE MAKLAKMKIP ASEMFRSETD KYSKFDETGF PTHDVEGKEL
SKGQAKKLRK LYETQEKLHN EYLQMNQNGN
//
