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Database: UniProt
Entry: A0A182LPY6_9DIPT
LinkDB: A0A182LPY6_9DIPT
Original site: A0A182LPY6_9DIPT 
ID   A0A182LPY6_9DIPT        Unreviewed;       219 AA.
AC   A0A182LPY6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 2.
DT   05-DEC-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
OS   Anopheles coluzzii.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=1518534 {ECO:0000313|Proteomes:UP000075882, ECO:0000313|VectorBase:ACOM041705-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075882, ECO:0000313|VectorBase:ACOM041705-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mali-NIH {ECO:0000313|Proteomes:UP000075882,
RC   ECO:0000313|VectorBase:ACOM041705-PA};
RX   PubMed=20966253; DOI=10.1126/science.1195755;
RA   Lawniczak M.K., Emrich S.J., Holloway A.K., Regier A.P., Olson M.,
RA   White B., Redmond S., Fulton L., Appelbaum E., Godfrey J., Farmer C.,
RA   Chinwalla A., Yang S.P., Minx P., Nelson J., Kyung K., Walenz B.P.,
RA   Garcia-Hernandez E., Aguiar M., Viswanathan L.D., Rogers Y.H.,
RA   Strausberg R.L., Saski C.A., Lawson D., Collins F.H., Kafatos F.C.,
RA   Christophides G.K., Clifton S.W., Kirkness E.F., Besansky N.J.;
RT   "Widespread divergence between incipient Anopheles gambiae species
RT   revealed by whole genome sequences.";
RL   Science 330:512-514(2010).
RN   [2] {ECO:0000313|VectorBase:ACOM041705-PA}
RP   IDENTIFICATION.
RC   STRAIN=Mali-NIH {ECO:0000313|VectorBase:ACOM041705-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   ProteinModelPortal; A0A182LPY6; -.
DR   VectorBase; ACOM041705-RA; ACOM041705-PA; ACOM041705.
DR   Proteomes; UP000075882; 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:UP000075882};
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:UP000075882}.
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;  24537 MW;  DE3C67829DDEB101 CRC64;
     MLAVRGALFS TAKNCSAVLG CRSKHTLPDL PYDFGALEPV ICREIMELHH QKHHNAYVTN
     LNAAEEQLQD AVAKQDVSKI IQLGNAIKFN GGGHINHSIF WKNLSPDRSD PSAELQKALN
     RDFQNMENFK KEMKAAAVAV QGSGWAWLGY NKKTKLLQIA ACPNQDPLEA TTGLVPLLGI
     DVWEHAYYLQ YKNLRPNYVD AIFDVVNWKD VSERLAKAH
//
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