ID A0A0G1VZ88_9BACT Unreviewed; 398 AA.
AC A0A0G1VZ88;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=UY50_C0009G0006 {ECO:0000313|EMBL:KKW11620.1};
OS Parcubacteria group bacterium GW2011_GWA2_49_9.
OC Bacteria.
OX NCBI_TaxID=1618852 {ECO:0000313|EMBL:KKW11620.1, ECO:0000313|Proteomes:UP000034328};
RN [1] {ECO:0000313|EMBL:KKW11620.1, ECO:0000313|Proteomes:UP000034328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW11620.1}.
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DR EMBL; LCQF01000009; KKW11620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VZ88; -.
DR STRING; 1618852.UY50_C0009G0006; -.
DR PATRIC; fig|1618852.3.peg.294; -.
DR Proteomes; UP000034328; 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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
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 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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKW11620.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 289..342
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
SQ SEQUENCE 398 AA; 44971 MW; E3E5512DFB6497AC CRC64;
MNITDVGHLT SDNDDGDDKM IKALKREGKP FTFEAMQEIA RKYETAFTED LKALNIELPD
AMPRASDNIA EDIEIVQKLL EKGSAYKTSD GIYFDTSKFP SYGTRGGFKL GDLREGARIA
INAEKKNPRD FSLWKFSSTD LGWDFPPYGK GFPGWHIECS AMSRKFLGQP FDIHTGGIDH
IPTHHQNEIA QSEAAYDTPL ANFWLHNEFV NMGDTKMAKS GENFITLQTL KDEGIHSLAY
RYFLLLAKYS TPIKYVGLPV LLGAGLQSLR REICELPEGG RINQSYKDRF LDAINDDLNT
AVGLSVLFAV RDDLKISPEE KRATILDFDK VLGLELDKRD LITSDKPIPE AIKKLATARE
DARKVKDFKK SDELRDQIQK EGYEVMDTDF GPIIRKKL
//
