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SYS_MYCCT
ID   SYS_MYCCT               Reviewed;         422 AA.
AC   Q2SR32;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
DE            Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
GN   Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; OrderedLocusNames=MCAP_0839;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is involved in tRNA binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00176}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00176}.
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DR   EMBL; CP000123; ABC01676.1; -; Genomic_DNA.
DR   RefSeq; WP_011387665.1; NC_007633.1.
DR   AlphaFoldDB; Q2SR32; -.
DR   SMR; Q2SR32; -.
DR   PRIDE; Q2SR32; -.
DR   EnsemblBacteria; ABC01676; ABC01676; MCAP_0839.
DR   GeneID; 23778208; -.
DR   KEGG; mcp:MCAP_0839; -.
DR   HOGENOM; CLU_023797_0_1_14; -.
DR   OMA; SPCFRRE; -.
DR   OrthoDB; 353391at2; -.
DR   PhylomeDB; Q2SR32; -.
DR   UniPathway; UPA00906; UER00895.
DR   Proteomes; UP000001928; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR43697; PTHR43697; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00414; serS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..422
FT                   /note="Serine--tRNA ligase"
FT                   /id="PRO_1000019736"
FT   BINDING         231..233
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         262..264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         285
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         349..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT   BINDING         384
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
SQ   SEQUENCE   422 AA;  48791 MW;  CF73317C45F18F4E CRC64;
     MLDINYIEQN LDEVIQRLNK RNQQDYSDDL KYVVSKNLKR KEILVKSEAL KSRKNQLSKE
     IGTLLKEKKV DQSEQAKIEV INLNEQIIKL DEELRVVNDQ ILEKLLYIPN LPHKDIYFGK
     SDEDNVEIRK SNHSNLLKHS TPHWQIATKL GLVDFEKGVK LSGTRFLIYT GLGSKLVRSI
     ADLLLKRHEK HGYKEIFCPL IVNKSAMLGT GQLPKFSEDM YQVGEQYLIP TSEVPLTNLH
     ANEILAYDVL PLKYTSFTQC FRQEAGSAGR DTKGMIRLHQ FNKVELVKIV HPEESMNELE
     MLIKDAEDVL NMFDLPYRVV ELCSGDIGFS SAKTYDLEVW FPEQNKYREI SSCSNCTDFQ
     ARNMQTRFKD KDSKIKLVHT LNGSGVAVDR LIAAILENYW DGEKLILPTL LRPYFDNQEF
     IK
 
 
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