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Database: UniProt
Entry: G0QMQ3_ICHMG
LinkDB: G0QMQ3_ICHMG
Original site: G0QMQ3_ICHMG 
ID   G0QMQ3_ICHMG            Unreviewed;       221 AA.
AC   G0QMQ3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-DEC-2018, entry version 21.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=IMG5_051060 {ECO:0000313|EMBL:EGR33509.1};
OS   Ichthyophthirius multifiliis (strain G5) (White spot disease agent)
OS   (Ich).
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Ophryoglenina; Ichthyophthirius.
OX   NCBI_TaxID=857967 {ECO:0000313|Proteomes:UP000008983};
RN   [1] {ECO:0000313|EMBL:EGR33509.1, ECO:0000313|Proteomes:UP000008983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G5 {ECO:0000313|EMBL:EGR33509.1,
RC   ECO:0000313|Proteomes:UP000008983};
RA   Coyne R., Brami D., Johnson J., Hostetler J., Hannick L., Clark T.,
RA   Cassidy-Hanley D., Inman J.;
RL   Submitted (JUL-2011) 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; GL983435; EGR33509.1; -; Genomic_DNA.
DR   RefSeq; XP_004037495.1; XM_004037447.1.
DR   ProteinModelPortal; G0QMQ3; -.
DR   EnsemblProtists; EGR33509; EGR33509; IMG5_051060.
DR   GeneID; 14909687; -.
DR   InParanoid; G0QMQ3; -.
DR   Proteomes; UP000008983; 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:UP000008983};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EGR33509.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008983}.
FT   DOMAIN       21    100       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      116    214       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        44     44       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        92     92       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       185    185       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   221 AA;  25760 MW;  3896E5D4C4C1F772 CRC64;
     MKNLQFPLRR FFSLRSTIPA TIPKLKFGLN DLEPILSKNL LEYHYGKHHQ TYINNLNDIY
     NQIKEASANN DVHKVALLQS GLRFNLGGHV NHALYWENLA PSKQGGGQLP ESNSPLTLAI
     TQKWGSYENF IAEFNKRTAS IQGSGWGWLG YDTVSKTLRM FELGNQEMPE WNSIVPLLTI
     DVWEHAYYLD YQNLRVKYLT EIWKIIDWKV VEQRYREATK Q
//
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