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Database: UniProt
Entry: A0A165IFW7_9PEZI
LinkDB: A0A165IFW7_9PEZI
Original site: A0A165IFW7_9PEZI 
ID   A0A165IFW7_9PEZI        Unreviewed;       231 AA.
AC   A0A165IFW7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   23-MAY-2018, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=L228DRAFT_243569 {ECO:0000313|EMBL:KZF24839.1};
OS   Xylona heveae TC161.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF24839.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF24839.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF24839.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J.,
RA   Amirebrahimi M., Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M.,
RA   Grigoriev I.V., Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal
RT   endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; KV407455; KZF24839.1; -; Genomic_DNA.
DR   RefSeq; XP_018190394.1; XM_018331719.1.
DR   EnsemblFungi; KZF24839; KZF24839; L228DRAFT_243569.
DR   GeneID; 28896856; -.
DR   Proteomes; UP000076632; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0030145; F:manganese ion binding; IEA:EnsemblFungi.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
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:UP000076632};
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:UP000076632}.
FT   DOMAIN       39    118       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      128    229       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        62     62       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       110    110       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       196    196       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       200    200       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   231 AA;  25088 MW;  40B16F9DD011FC34 CRC64;
     MSASLFRTSF ARAALRAGAA STPKAAGVAG MTFARGKATL PDLAYDFGAL EPSISGKIME
     LHHNMHHKTY VNSFNEASEK LAAAKESNDI AAQIALQPLI NFHGGGHINH SLFWENLAPK
     SQGGGEPPSG ALGKAIDDTF GSLESFQGKF NTALAGIQGS GWAWLVKDNQ TGNIGIKTYA
     NQDPVVGQFT PILGIDAWEH AYYLQYQNRK AEYFKAIWEV INWKTAEKRF Q
//
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