SYC2_PHOPR
ID SYC2_PHOPR Reviewed; 457 AA.
AC Q6LHY2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative cysteine--tRNA ligase 2;
DE EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00041};
DE Short=CysRS 2 {ECO:0000255|HAMAP-Rule:MF_00041};
GN Name=cysS2 {ECO:0000255|HAMAP-Rule:MF_00041}; OrderedLocusNames=PBPRB1226;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00041}.
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DR EMBL; CR378678; CAG23098.1; -; Genomic_DNA.
DR RefSeq; WP_011221283.1; NC_006371.1.
DR AlphaFoldDB; Q6LHY2; -.
DR SMR; Q6LHY2; -.
DR STRING; 298386.PBPRB1226; -.
DR EnsemblBacteria; CAG23098; CAG23098; PBPRB1226.
DR KEGG; ppr:PBPRB1226; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_6; -.
DR OMA; VHHSNEI; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000000593; Chromosome 2.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..457
FT /note="Putative cysteine--tRNA ligase 2"
FT /id="PRO_0000159454"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 457 AA; 52294 MW; EC931FE165B1B0CA CRC64;
MSQPELLLFD TMARELRPFN SIRANKVGLY ACGPTVYDYA HAGNLRTYLF VDVLRRTLEI
NGYEVNHVMN ITDVGHLVSD ADTGEDKMEK GARKQNKSAW EIAQFFEQAF FDDLKLLNIS
TPSVTCRATE HIQEQIKFIQ ELETKGFTYQ TSDGVYFNTD RLADYGKLAR LDKQGLEAGI
RVEMAEKKHP TDFALWKFSG DKPRQMEWQG PWGIGFPGWH IECSAMAEKY LGDVFDIHVG
GEDHIPVHHT NEIAQCQAKN GHVQANYWLH GYFLQLKKEK ISKSGTSLRL DALVAKGYEP
MAYRYLTLTS HYRSHLSFTW EGLSGAQKAL HRLRNKVAFL PSNGNVDESY RELFMRHINR
DLNMPQALAL VWDVLNSELL PENKRATALF FDRILGLDIH KIETVEIPEH ISRLVELRTQ
VKRQGNFKKA DAIRNQIHDL GYQVNDSGDG STVTIRS