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Database: UniProt
Entry: A0A182JYQ4_9DIPT
LinkDB: A0A182JYQ4_9DIPT
Original site: A0A182JYQ4_9DIPT 
ID   A0A182JYQ4_9DIPT        Unreviewed;       219 AA.
AC   A0A182JYQ4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 2.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|Proteomes:UP000075881, ECO:0000313|VectorBase:ACHR003636-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075881, ECO:0000313|VectorBase:ACHR003636-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881,
RC   ECO:0000313|VectorBase:ACHR003636-PA};
RA   Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:ACHR003636-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|VectorBase:ACHR003636-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
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   VectorBase; ACHR003636-RA; ACHR003636-PA; ACHR003636.
DR   Proteomes; UP000075881; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075881};
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:UP000075881}.
FT   DOMAIN       24    105       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      111    214       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       54     74       {ECO:0000256|SAM:Coils}.
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       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   219 AA;  24526 MW;  41304F572CA29813 CRC64;
     MLSVRGVLFS TAKNCSAVLG CRSKHTLPDL PYDFGALEPV VCREIMELHH QKHHNAYVTN
     LNAAEEQLQD AVAKQDVSKI IQLGNAIKFN GGGHINHSIF WKNLSPDRSD PSAELQKAVN
     RDFQSMENFK KEMKAAAVAV QGSGWAWLGY NKKTKLLQIA ACPNQDPLEA TTGLVPLLGI
     DVWEHAYYLQ YKNLRPNYVD AIFDVVNWKD VSERLAKAH
//
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