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Database: UniProt
Entry: A0A1V6RMA7_9EURO
LinkDB: A0A1V6RMA7_9EURO
Original site: A0A1V6RMA7_9EURO 
ID   A0A1V6RMA7_9EURO        Unreviewed;       249 AA.
AC   A0A1V6RMA7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PENVUL_c037G07193 {ECO:0000313|EMBL:OQE02905.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE02905.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|EMBL:OQE02905.1, ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|EMBL:OQE02905.1,
RC   ECO:0000313|Proteomes:UP000191518};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (AUG-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OQE02905.1}.
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DR   EMBL; MDYP01000037; OQE02905.1; -; Genomic_DNA.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000191518};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT   DOMAIN       44    124       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      139    238       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        69     69       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       117    117       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       205    205       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       209    209       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   249 AA;  27434 MW;  96FA7737F724C4BB CRC64;
     MSPKMGIQGD LGGLFIVYTS TPPFHSSLHL THAYIHNSSM ASQTHTLPPL PYAYDALEPV
     ISKQIMELHH QKHHQTYINN LNAAISAQAS AASSNNAPTL IALQQKLRFN GGGHINHSLF
     WNNLTPPGTP GNNIDSAPTL RKAIASRWGT QDTFVEAFNA ELLNLQGSGW GWLVSKGGAK
     GQLDIVTTKD QDPVNGPNVP VFGVDMWEHA YYLQYLNNKA DYVEGIRRII HWAEAEKRYA
     SGLESLLKL
//
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