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Database: UniProt
Entry: G2QWW5_THITE
LinkDB: G2QWW5_THITE
Original site: G2QWW5_THITE 
ID   G2QWW5_THITE            Unreviewed;       250 AA.
AC   G2QWW5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=THITE_2108025 {ECO:0000313|EMBL:AEO63129.1};
OS   Thielavia terrestris (strain ATCC 38088 / NRRL 8126) (Acremonium
OS   alabamense).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thielavia.
OX   NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO63129.1, ECO:0000313|Proteomes:UP000008181};
RN   [1] {ECO:0000313|EMBL:AEO63129.1, ECO:0000313|Proteomes:UP000008181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
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; CP003009; AEO63129.1; -; Genomic_DNA.
DR   RefSeq; XP_003649465.1; XM_003649417.1.
DR   STRING; 578455.XP_003649465.1; -.
DR   EnsemblFungi; AEO63129; AEO63129; THITE_2108025.
DR   GeneID; 11517530; -.
DR   KEGG; ttt:THITE_2108025; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000008181; Chromosome 1.
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:UP000008181};
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:UP000008181}.
FT   DOMAIN       44    124       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      137    237       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        68     68       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       116    116       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       204    204       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       208    208       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   250 AA;  27061 MW;  165696EAD5927A53 CRC64;
     MVNIGSLWQY LAAHSPLQST LSSLSTTTMS GGALNLTQMG LAPYSLPPLP YAYDALEPHI
     SAQIMELHHG KHHQAYVTNL NAALASHVSA VAAGDVAAQI ALQQAIKFNG GGHINHSLFW
     KNLAPPGTEE TNPAVAKELV SAIEKKWGSL ESFKKAFSAA LLAIQGSGWG WLVKEAGNGA
     GLRIVTTKDQ DPVVGGDVPI FGVDMWEHAY YLQYLNGKAA YVENIWNVIN WRTAEDRFVG
     RNEENVKTEL
//
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