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Database: UniProt
Entry: A0A1C7N9Y6_9FUNG
LinkDB: A0A1C7N9Y6_9FUNG
Original site: A0A1C7N9Y6_9FUNG 
ID   A0A1C7N9Y6_9FUNG        Unreviewed;       184 AA.
AC   A0A1C7N9Y6;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1_1 {ECO:0000313|EMBL:OBZ85942.1};
GN   ORFNames=A0J61_06004 {ECO:0000313|EMBL:OBZ85942.1};
OS   Choanephora cucurbitarum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae;
OC   Choanephoroideae; Choanephora.
OX   NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ85942.1, ECO:0000313|Proteomes:UP000093000};
RN   [1] {ECO:0000313|EMBL:OBZ85942.1, ECO:0000313|Proteomes:UP000093000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ85942.1,
RC   ECO:0000313|Proteomes:UP000093000};
RA   Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT   "Choanephora cucurbitarum.";
RL   Submitted (MAR-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:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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:OBZ85942.1}.
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DR   EMBL; LUGH01000343; OBZ85942.1; -; Genomic_DNA.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000093000; 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   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000093000};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093000};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    184       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008889564.
FT   DOMAIN       40    178       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   184 AA;  19573 MW;  0E56E92E7EE88EAA CRC64;
     MFFSKLTTAF AAIIFFGATM TSAEPVEAVA YMTSANTEAN GSILGTIKLT QDDYHSPTRV
     IVDVEGLTEG NHGIHIHTFG DISNGCENTG PHFNPFNRTH GDLKAKNRHA GDLGNLWADK
     DGHGHLDVTS DLVFLSGKFS TIGRAIVIHA DEDDLGLGNN SNSTLTGNSG KRWACGVIGF
     ANPV
//
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