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Database: UniProt
Entry: A0A2U3XMH6_LEPWE
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ID   A0A2U3XMH6_LEPWE        Unreviewed;       559 AA.
AC   A0A2U3XMH6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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};
GN   Name=CARS2 {ECO:0000313|RefSeq:XP_006732661.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006732661.1};
RN   [1] {ECO:0000313|RefSeq:XP_006732661.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006732661.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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}.
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DR   RefSeq; XP_006732661.1; XM_006732598.2.
DR   AlphaFoldDB; A0A2U3XMH6; -.
DR   STRING; 9713.A0A2U3XMH6; -.
DR   GeneID; 102739874; -.
DR   KEGG; lww:102739874; -.
DR   CTD; 79587; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000245341; 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; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_006732661.1};
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:UP000245341};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          68..360
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
SQ   SEQUENCE   559 AA;  61725 MW;  F5F5F28C54F08E6A CRC64;
     MLRKRGAAVG PRLLRAALGL GSRLGPARAA SGVRGQGWLQ PAGHDTGVKV YNSLTQRKDP
     LIVASVDAAS WYSCGPTVYD HAHLGHACSY VRFDIIRRIL TRVFGCNIIM VMGITDVDDK
     IIHRAAEMNV SPASLANLYE EDFKQDMAAL KVLPATVYLR VTENIPQIIS FIEGIIANGH
     AYPTAQGNVY FDLQSRGDKY GKLVSVVPGP VREPVDSDKR HASDFALWKA AKPQEVFWAS
     PWGKGRPGWH IECSTISSLV FGSQLDIHSG GVDLAFPHHE NEIAQCEAFH QCRQWGNYFL
     HSGHLHVKGE EEKMSKSLKN YITIKDFLKM FSPDVFRLFC MRSSYRSAID YSDGTMLEAK
     HLLLAAAAFV EDARAYMRGQ LVCGPIRDDV LWERLRHAKQ AVKAALADDF DTPAAVDAVM
     DLIHHGNRQL TAPAEEPGGP RSPAVFGSIV SYVEQFFETV GISLADRQSV SGDGSRATLH
     SVVEQLVQFR LQVRQFALAT GAATREGRRQ QLLDTQPLLE ACDALRRDLV AHGISIKDRS
     STSTWELLDQ RTEGPRPGS
//
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