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Database: UniProt
Entry: E3Q599_COLGM
LinkDB: E3Q599_COLGM
Original site: E3Q599_COLGM 
ID   E3Q599_COLGM            Unreviewed;       208 AA.
AC   E3Q599;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   23-MAY-2018, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GLRG_01010 {ECO:0000313|EMBL:EFQ25866.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N.,
RA   Altmueller J., Alvarado-Balderrama L., Bauser C.A., Becker C.,
RA   Birren B.W., Chen Z., Choi J., Crouch J.A., Duvick J.P., Farman M.A.,
RA   Gan P., Heiman D., Henrissat B., Howard R.J., Kabbage M., Koch C.,
RA   Kracher B., Kubo Y., Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I.,
RA   Moore N., Neumann U., Nordstroem K., Panaccione D.G., Panstruga R.,
RA   Place M., Proctor R.H., Prusky D., Rech G., Reinhardt R.,
RA   Rollins J.A., Rounsley S., Schardl C.L., Schwartz D.C., Shenoy N.,
RA   Shirasu K., Sikhakolli U.R., Stueber K., Sukno S.A., Sweigard J.A.,
RA   Takano Y., Takahara H., Trail F., van der Does H.C., Voll L.M.,
RA   Will I., Young S., Zeng Q., Zhang J., Zhou S., Dickman M.B.,
RA   Schulze-Lefert P., Ver Loren van Themaat E., Ma L.-J.,
RA   Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi
RT   deciphered by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697333; EFQ25866.1; -; Genomic_DNA.
DR   RefSeq; XP_008089886.1; XM_008091695.1.
DR   ProteinModelPortal; E3Q599; -.
DR   EnsemblFungi; EFQ25866; EFQ25866; GLRG_01010.
DR   GeneID; 24406375; -.
DR   OrthoDB; EOG092C4NQ6; -.
DR   Proteomes; UP000008782; 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:UP000008782};
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:UP000008782}.
FT   DOMAIN        5     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    192       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        30     30       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       159    159       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23026 MW;  C0B22E4AE66E225E CRC64;
     MASPQYILPK LPYAYDALEP HISAQIMELH HSKHHQAYVT NLNKAIETYN ANPLQNRIAV
     LAALNFNGGG HINHSLFWEN LSPASSGDAS PDAAPKLVAE ITRVWGGLDQ FKQAFNTTLL
     GITGSGWGWL VKDDITGLSI ITTKDQDPVT KGVPIFGIDM WEHAYYLQYL NGKAAYVENI
     WNVLNWKTAE SRFSGSRDDA FTALKAVL
//
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