ID A0A1F3ENA6_9BACT Unreviewed; 485 AA.
AC A0A1F3ENA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00014738};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
DE Flags: Fragment;
GN ORFNames=A2046_00150 {ECO:0000313|EMBL:OFX56695.1};
OS Bacteroidetes bacterium GWA2_30_7.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797313 {ECO:0000313|EMBL:OFX56695.1, ECO:0000313|Proteomes:UP000178829};
RN [1] {ECO:0000313|EMBL:OFX56695.1, ECO:0000313|Proteomes:UP000178829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:OFX56695.1}.
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DR EMBL; MENC01000131; OFX56695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3ENA6; -.
DR Proteomes; UP000178829; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OFX56695.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 371..440
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT NON_TER 485
FT /evidence="ECO:0000313|EMBL:OFX56695.1"
SQ SEQUENCE 485 AA; 55411 MW; 6D91FBD268A8C265 CRC64;
MTKLLIYNTI SRKKEIFEPI NSKHVGMYVC GPTVYGDPHL GHARPAITFD LLFRYLQKLG
YKVRYVRNIT DVGHLENDAD SGEDKIAKKA RLEELEPMEI VQYYTERYHN AMASLNVKSP
SIEPRASGHI MEQLEMIEKI VENGFAYEKN GSIYFDVEKY SKSFHYGKLS GRILEDLFAN
TRDLDGQDEK KNSFDFALWK KASPEHIMRW TSKWSDGFPG WHMECSAMGI KYLGEKFDIH
GGGMDLLFPH HECEIAQSTA ALGFESVKYW LHNNMITING QKMGKSLGNF INLEEFFNGS
HKLLTQAYSP MTIRFFLLQA HYRSTLDFSN EALQAAEKGL ARLMNAYNAI EKLKVSEKST
VSINLDELNN NCFEAMNDDL NSPIVISYLF EAVKTINLVI AGNEQINQVD IDKLKTIFNT
FVIEVLGLLP QKGSTNEAVL NDVINLMLNL RMEAKSNKNF ELSDKIRNEL NKIGIEIKDK
KDGFD
//
