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Database: UniProt
Entry: A0A164YSN1_9CRUS
LinkDB: A0A164YSN1_9CRUS
Original site: A0A164YSN1_9CRUS 
ID   A0A164YSN1_9CRUS        Unreviewed;      1719 AA.
AC   A0A164YSN1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Dual oxidase 2 {ECO:0000313|EMBL:KZS15559.1};
GN   ORFNames=APZ42_018745 {ECO:0000313|EMBL:KZS15559.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15559.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS15559.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15559.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS15559.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZS15559.1}.
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DR   EMBL; LRGB01000868; KZS15559.1; -; Genomic_DNA.
DR   STRING; 35525.A0A164YSN1; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09823; peroxinectin_like; 2.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 2.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF4; LD42267P; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR   PROSITE; PS50292; PEROXIDASE_3; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1719
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007854721"
FT   BINDING         1391
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1719 AA;  192666 MW;  EDA6E1E00693402F CRC64;
     MAPKEMRYCF PLARILLLIC LCCASHAIHF DSGFTDKVII DGQQQLVRTR RDTLVKHKTQ
     HLKPAIEIEP INEKVRVAMP HFNVQDLTTY ANQAASAIAA RFDEFEPTLL ASNESRLQTS
     SAAWFMAASH KTKVVAKNIS RIALMAEETT KYFAQGLKLT KEQITFALPT MDVRNTVLAD
     QCPLEVDFPC QPRKYRAYNG YCNNVQNPRW GNANTRYLRF LPPDYSDGVS IPRQASDGTF
     LPSARDISLA VHKDVDNPHL HLTAMAAIWG QLVHNDISHT PQMAGFLGQR LRCCGVNLHE
     FHPECYPIRL PDSDPVNGQI NIKCQEYVRS GTAPRVGCTL GPREQINQVT SFLDGSTIYG
     SSVEEANDLR LFRAGLMKTQ AGPRGTTKGL LPPDDNIIDC NTKNKDVKCF KAGDVRVNEH
     TELTALHVIL IREHNRLAEE LAVINSHWSD ETLFQEARRI VGAEMQHITY SEFLPVILGQ
     TIMEKYGLEP ESTGYFTGYD ININPGVANS VAASALRFVA SLLPKNMGLY RNGRKISEQK
     MGSSFYAPFE LYEANGLDEI IEGLARTLSQ SEDPSINDVM TNHMFQEKPG TAGLDLAAQI
     IQHGRDHGIP GYVKWREFCG LPVITTFDQL TDVMNGATIA TLKSIYRHVN DIDLFTGGLA
     ETPSAGAVVG RTLGCLIGRQ FHYLRRGDRY WYENELPPSS FTKDQLHAIR KVSLARLICD
     NSDSINQIQP RVFLINDPFL NADMSCHDGV IPKMDLGAWK TASPHFVIPE TLLEESVVRA
     KREAEDYLTL EETLQLTAAV GAASTRPKRQ ISSFNPITNL SAWTRTANQN TDKRANFLTL
     HSLVTPAPLN RRQMSPQTIL TTIHPSLRAW LAPLIFPRLR TAHHEGHGFE ERQSFEQPRF
     HGASAQALNQ YNLDQHLLNL LLASYGEGEV ETDSYGPRKR EAVDVLQDSA RVAHHVNGLL
     ADYESQRKGA DPKSPVGTAF SFSRPKRQAS AIANISRVLQ FASKRFVNSF LNLVNQKDVE
     SQPQPSTLQE LMKVLPNIDV SEVVDIPKVF QCDEQTLPCD HTSKYRTMTG WCNNLNFPEL
     GKSLRAFVRL LPPKYEDGLS TMRATAVSGR PLPSARMISA NIHNDVSAPH TRYSLMVMQY
     AQLLDHDLTF TPVNRGFGGS IIDCNSCDSA KTVHPECAPI AVPPNDPWFP HIERSTGRPK
     CIPFTRSLPG QLTLGHREQL NQVTAFVDGS STYGSDVCEM RKLRAFVGGR LNSTRHPIRG
     KDLLPLTGEH LECKSPSGVC FTGGDTRASE QPGLTSIHTI FMREHNRIVT ELAKINPHWN
     DEQLFQNGRR IMSAEFQHVS YNEFLPRVLG WNAIQLYELK VLTEGYYNGY DPTCNPTIFT
     EFSSAAFRFG HSLLKEQFKR MGANFVDRKS NVKLRDVFMN PDIIYQVGMI DDLLRGMLGT
     SMETMDQFIT HEVTNHLFEE KAKPFSGLDL AALNIQRARD HGIRPYNDYR SLCNLKRART
     FEDLSREVTP EIITRLKQTY EHVDDIDLFP GGLAETSLHG GLVGPTFACI IAMQFRQLRK
     CDRFWYENGD PLIRFTEAQL AEIRKATVSK LLCDNSDGID TTQRSAFDQS EPFLNPRVPC
     RSLPSIDLEL WKERVSCTVG STNIEVGKAD RISPCVMCTC TREGPICQSL KVVNCFQLAQ
     TFSPAAILND HVCKVQCAFA FRAFPQVAAA QDPNQLGFS
//
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