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Database: UniProt
Entry: A0A182HX08_ANOAR
LinkDB: A0A182HX08_ANOAR
Original site: A0A182HX08_ANOAR 
ID   A0A182HX08_ANOAR        Unreviewed;       153 AA.
AC   A0A182HX08;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 22.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS   Anopheles arabiensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=7173 {ECO:0000313|Proteomes:UP000075840, ECO:0000313|VectorBase:AARA005837-PA};
RN   [1] {ECO:0000313|Proteomes:UP000075840, ECO:0000313|VectorBase:AARA005837-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dongola {ECO:0000313|Proteomes:UP000075840,
RC   ECO:0000313|VectorBase:AARA005837-PA};
RA   Neafsey D.E., Howell P., 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 arabiensis DONG5_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000075840, ECO:0000313|VectorBase:AARA005837-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dongola {ECO:0000313|Proteomes:UP000075840,
RC   ECO:0000313|VectorBase:AARA005837-PA};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., 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 arabiensis DONG5_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|VectorBase:AARA005837-PA}
RP   IDENTIFICATION.
RC   STRAIN=Dongola {ECO:0000313|VectorBase:AARA005837-PA};
RG   VectorBase;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [4] {ECO:0000313|VectorBase:AARA005837-PA}
RP   IDENTIFICATION.
RC   STRAIN=Dongola {ECO:0000313|VectorBase:AARA005837-PA};
RG   VectorBase;
RL   Submitted (OCT-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:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; APCN01005111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   VectorBase; AARA005837-RA; AARA005837-PA; AARA005837.
DR   Proteomes; UP000075840; 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   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000075840};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       10    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   153 AA;  15676 MW;  A034C01A8D9C95ED CRC64;
     MPLKAVCVLN GEVKGTIFFE QSGESDPVKV TGSVTGLKPG DHGFHIHEFG DNTNGCMSTG
     AHFNPYAKTH GGPDAEERHA GDMGNIVADE NGEAKVDLTA TQIALSGALN VVGRSLVVHA
     DPDDLGVGGH ELSKTTGNAG ARLACGVIGL CKI
//
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