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MSRA_SOLLC
ID   MSRA_SOLLC              Reviewed;         196 AA.
AC   P54153;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Fruit-ripening protein E4;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
DE   AltName: Full=Protein-methionine-S-oxide reductase;
DE   Flags: Fragment;
GN   Name=E4;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2562553; DOI=10.2307/3869003;
RA   Cordes S., Deikman J., Margossian L.J., Fischer R.L.;
RT   "Interaction of a developmentally regulated DNA-binding factor with sites
RT   flanking two different fruit-ripening genes from tomato.";
RL   Plant Cell 1:1025-1034(1989).
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; S44898; AAB23481.2; -; Genomic_DNA.
DR   PIR; JQ0988; JQ0988.
DR   RefSeq; NP_001307131.1; NM_001320202.1.
DR   AlphaFoldDB; P54153; -.
DR   SMR; P54153; -.
DR   STRING; 4081.Solyc03g111720.2.1; -.
DR   PaxDb; P54153; -.
DR   PRIDE; P54153; -.
DR   EnsemblPlants; Solyc03g111720.3.1; Solyc03g111720.3.1; Solyc03g111720.3.
DR   GeneID; 101253577; -.
DR   Gramene; Solyc03g111720.3.1; Solyc03g111720.3.1; Solyc03g111720.3.
DR   KEGG; sly:101253577; -.
DR   eggNOG; KOG1635; Eukaryota.
DR   HOGENOM; CLU_031040_3_0_1; -.
DR   InParanoid; P54153; -.
DR   OMA; AGPFYYA; -.
DR   OrthoDB; 1383773at2759; -.
DR   PhylomeDB; P54153; -.
DR   BRENDA; 1.8.4.11; 3101.
DR   Proteomes; UP000004994; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..>196
FT                   /note="Peptide methionine sulfoxide reductase"
FT                   /id="PRO_0000138636"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         196
SQ   SEQUENCE   196 AA;  21918 MW;  FD251E1A6A123423 CRC64;
     MEGNNSSSKS TTNPALDPDL DSPDQPGLEF AQFAAGCFWG VELAFQRVGG VVKTEVGYSQ
     GNVHDPNYKL ICSGTTEHAE AIRIQFDPNV CPYSNLLSLF WSRHDPTTLN RQGNDVGKQY
     RSGIYYYNDA QAQLARESLE AKQKEFMDKK IVTEILPAKR FYRAEEYHQQ YLEKGGGRGC
     KQSAAKGCND PIRCYG
 
 
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