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Database: UniProt
Entry: A0A328SKH2_9EURY
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Original site: A0A328SKH2_9EURY 
ID   A0A328SKH2_9EURY        Unreviewed;       458 AA.
AC   A0A328SKH2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   ORFNames=BZ138_02590 {ECO:0000313|EMBL:RAP52646.1};
OS   Methanosphaera sp. rholeuAM270.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=1945577 {ECO:0000313|EMBL:RAP52646.1, ECO:0000313|Proteomes:UP000249457};
RN   [1] {ECO:0000313|EMBL:RAP52646.1, ECO:0000313|Proteomes:UP000249457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RholeuAM270 {ECO:0000313|EMBL:RAP52646.1};
RA   Hoedt E.C., Parks D.H., Rosewarne C.P., Denman S.E., Mcsweeney C.S.,
RA   O Cuiv P., Hugenholtz P., Tyson G.W., Morrison M.;
RT   "Culture- and metagenomics-based expansion of the genus Methanosphaera
RT   reveals their evolutionary depth and metabolic versatility.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001080, ECO:0000256|HAMAP-
CC         Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAP52646.1}.
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DR   EMBL; MUZX01000077; RAP52646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328SKH2; -.
DR   Proteomes; UP000249457; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; IPR015273; Cys-tRNA-synt_Ia_DALR.
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; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
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   ECO:0000256|HAMAP-Rule:MF_00041};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000249457};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          350..417
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   MOTIF           29..39
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           263..267
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   458 AA;  53019 MW;  21B8C8C7ADF86A24 CRC64;
     MIKVYNTMTR EKEDLKVVNN KLKLFVCGPT VYDFSHIGHA RTYISFDVIV RYLKYKGISV
     FYLQNITDID DKIINRAKEN GEDPLELSHR FEKEYLEDMA LLNVKNVNFY ARATEHMDEI
     ITQIQNLIEK GFAYDTETGV YFDVSKFEDF GKLSNRNLDD LQNTRIEVDT TKKDVKDFAL
     WKKQDEEPYW NSPWGNGRPG WHIEDTAITE SYFGPQYNIH GGGLDLIFPH HDAEIAQMEA
     ASGKEPLVEY WMHTGFLNVR GEKMSKSLGN FITIKELLKE YSPEVYRFFV LSTHYRSPID
     FSDDILKQAE NSLRRIQNTG STLLEKSNDT YLPEEDLSDI SSDLDLFKKE FFEAMDNDFN
     TPIALSSLFD FIHKVNKVLN GNEVSYNTLN SIIDTLRSIE EILGFSIIVS EDVGSDLSND
     LLNIITDVRQ DLRAKKDWDL ADKIRDNLAE LDISLEDK
//
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