ID A0A182JSK3_9DIPT Unreviewed; 1322 AA.
AC A0A182JSK3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR001485-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR001485-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR001485-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Mitochondrial cysteine-specific aminoacyl-tRNA synthetase
CC that catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
CC {ECO:0000256|ARBA:ARBA00043868}.
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:ARBA00043713};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17775;
CC Evidence={ECO:0000256|ARBA:ARBA00043713};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 43041.A0A182JSK3; -.
DR EnsemblMetazoa; ACHR001485-RA; ACHR001485-PA; ACHR001485.
DR VEuPathDB; VectorBase:ACHR001485; -.
DR OrthoDB; 3612432at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
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; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 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:SF27; CYSTEINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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 Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 849..1131
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 222..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..381
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 422..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 482..555
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 151047 MW; E5E94960E00E8032 CRC64;
MPDSSRTFGD IDDIDGAELR TQLKHWIEEE GIETNIQLQM KKKLIEKMSR TALGKKIALK
LQTQQGIVLS PLVLVLNTLV AEFLYTQNCH FSLSIFTNEV PFKNTLPDFT RSSKFRLNRA
ELGEIFEALG MEHYDGLVEK YEKFCTDQGS RSLLYIVFKT VLSAVKTQEA KLRHLKRLDK
RKTSAQTLLK KLKVEQLHKN VEKLLHRVKA VGKAIVELEK SQQQTVQGDA NVEQRTNVEE
KTNPDDDEQP SARSLRLCSE SVSKLVERLE TCTKMFEQLI EAVRQQRTDD GPETVEHEDA
VDDVGEPSDK PKEKRKTYTE FLRELKTTEH GKKYVAKLQK QVAKLLDKEK HQIETKYGKE
LRKLEQEYED KLAKALATKR NETIVVKQTP QPIPIVHITE PHHMDSRSEE SQHFMRKIDE
RLDQLYRQER NVDDKLATLR NDLQQQEQRQ SRYFESLKAA KTKETKLQVL HNVERELMAT
FEDETNAIIQ NAKQTIEQLE KESDKINHSF QRYLRKQRED KRKLIDEKVQ IWTRYNDEKL
ELNQRELLNE EFEQKVTETV AIVPEITVPV QQPQKDTPFE NPFRSFDPLK YLKQSRPMES
HMVDVAISTI SDVGMQTSRD DEPIQEDAIE RPIPAARTTS NAQLSDVLAK DTRDLRQSIE
ENLQKLDQMS RSYSKAQGSS EKRTYDVVPQ TVVRQPASPL PTVEPSSNRS LDDCSSTELG
LSDGEVVLSN VPKPNASQDL IDYATRNIFN EQLKVGPQSA VAVSYSDLSI SSISGASKLT
YDKSQSMDGE LDRISTGARS NASHNSWSVS PCFSGYFENI LPPSSPKTCA STMDDSRKRF
HSKSDPLNLY DSAHIGHASC YVRLDILQRI LRQHFHLPLI TAMNITDIDD KIITRALEQQ
IDWKQLARRY EDEFWSDLQR LNVRAPDVKL RVTDHIPAII HFIQTLVEKG FAYPTADGSV
YFETGKYERY GKLQKVIIEP ESATAKDSKR HQSDFALWKA SKPGEPFWTA PGFGIGRPGW
HIECSTLASH LFGSELDFHA GGLDLRFPHH ENEETQSCCY HDVPDWVTHW MHTGQLHLEG
QTHKMSKSLK NTVSIAELLK EYSADEFRML CLLSHYRSVI DYGPEAMATA RNVLRKFESF
FSDSKAYIDG LKPASCDAAS TENLLKKLSE TRKIVEEFLK NDFNTANSVL ALGELASNVQ
RIINCHEQTA SDASLIGSSN VGSVLAVTEY IRQELLSYGI ESTSTISSHH SQMASESDQS
FGKLIEAFVA TRSEIRLQAM ETKNAQLFKV CDLLRDRLKV ANVEVKDHGK TSSWSLRERS
VK
//
