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Database: UniProt
Entry: A0A197JGU4_9FUNG
LinkDB: A0A197JGU4_9FUNG
Original site: A0A197JGU4_9FUNG 
ID   A0A197JGU4_9FUNG        Unreviewed;       223 AA.
AC   A0A197JGU4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=K457DRAFT_150270 {ECO:0000313|EMBL:OAQ24402.1};
OS   Mortierella elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota;
OC   Mortierellomycotina; Mortierellomycetes; Mortierellales;
OC   Mortierellaceae; Mortierella.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ24402.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ24402.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ24402.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P.,
RA   Wu S., Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A.,
RA   Zienkiewicz K., Morin E., Tisserant E., Splivallo R., Hainaut M.,
RA   Henrissat B., Ohm R., Kuo A., Yan J., Lipzen A., Nolan M., Labutti K.,
RA   Barry K., Goldstein A., Labbe J., Schadt C., Tuskan G., Grigoriev I.,
RA   Martin F., Vilgalys R., Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis
RT   in the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-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}.
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DR   EMBL; KV442095; OAQ24402.1; -; Genomic_DNA.
DR   EnsemblFungi; OAQ24402; OAQ24402; K457DRAFT_150270.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000078512; 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:UP000078512};
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:UP000078512}.
FT   DOMAIN       24    105       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      114    217       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        49     49       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        97     97       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       184    184       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   223 AA;  25321 MW;  00A56B2E6B17168D CRC64;
     MLRSIPRTFA AINKPSAFAG LRYKHTLPAL PYAYEALEPY ISGEIMKIHH AKHHQTYINN
     LNAAEEKLGS AFKGNDVNEE ISIQSAIKFN GGGHINHTLF WENLAPGNKE VPKPSGELLK
     EIEKTWGSFD QFVSKFNTQT AAVQGSGWGW LGYNKEFKRL EIATTANQDP LKPTTGLIPL
     LGIDVWEHAY YLQYKNVRPD YLNAIWHVIN WKTVTDRFTK AHK
//
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