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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
 
 
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