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Database: UniProt
Entry: C5LXB3_PERM5
LinkDB: C5LXB3_PERM5
Original site: C5LXB3_PERM5 
ID   C5LXB3_PERM5            Unreviewed;       226 AA.
AC   C5LXB3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 36.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Pmar_PMAR016905 {ECO:0000313|EMBL:EEQ98662.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Alveolata; Perkinsea; Perkinsida; Perkinsidae; Perkinsus.
OX   NCBI_TaxID=423536;
RN   [1] {ECO:0000313|EMBL:EEQ98662.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 {ECO:0000313|EMBL:EEQ98662.1};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; GG686414; EEQ98662.1; -; Genomic_DNA.
DR   RefSeq; XP_002765945.1; XM_002765899.1.
DR   STRING; 423536.XP_002765945.1; -.
DR   EnsemblProtists; EEQ98662; EEQ98662; Pmar_PMAR016905.
DR   GeneID; 9062446; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   InParanoid; C5LXB3; -.
DR   OMA; YLICNAS; -.
DR   OrthoDB; 1353361at2759; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN       33    113       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      120    219       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        57     57       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       105    105       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       191    191       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   226 AA;  25236 MW;  FB73EAD963770835 CRC64;
     MLSVAGHRFA SLATTPVLRM GLARCFSSVT GPFQCPPLPY VKNALEPHMS AETLTYHHDK
     HHQTYVDTLN SIAAENSTIA SKTLEQIIKT ETGKPFNQAA QVYNHTFFFN NLAPNGGGEP
     TGKIAELITR DFGSFEKFKE EFSAAAVGHF GSGWVWLIAD DGKLKIVQGH DAGNPIRESK
     TPLMNIDVWE HAYYIDYRNA RAQYVKNYWN LVNWDFVNDN VAKAGL
//
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