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Database: UniProt
Entry: A0A182SX63_9DIPT
LinkDB: A0A182SX63_9DIPT
Original site: A0A182SX63_9DIPT 
ID   A0A182SX63_9DIPT        Unreviewed;       840 AA.
AC   A0A182SX63;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   RecName: Full=Haem peroxidase 3 {ECO:0008006|Google:ProtNLM};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM015230-PA, ECO:0000313|Proteomes:UP000075901};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMAM015230-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM015230-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   AlphaFoldDB; A0A182SX63; -.
DR   EnsemblMetazoa; AMAM015230-RA; AMAM015230-PA; AMAM015230.
DR   VEuPathDB; VectorBase:AMAM015230; -.
DR   OrthoDB; 4560at2759; -.
DR   Proteomes; UP000075901; 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; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF109; CHORION PEROXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
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}.
FT   REGION          510..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..545
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..806
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         299
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   840 AA;  93758 MW;  06E70E41E456A7BB CRC64;
     MVCKVQKAGS TESEAIVRSR ASMSRSVTGA TLPSARFVSL VVHGSRNEEA PVTMMLALWG
     QLIDHDITAT AQPRSINGST PRCCNGGEES THPSCLPIKV PQDDPWLSHL GVRCLEFLRS
     APAQRRDCLL SWREQTNQAT SFLDASPIYS SNPRSSDNAR IFRNGMLLFG RGPPHEDVCL
     RAALANQCIR PGDSRSGEQP GLLMMHMIWV NEHNQMATRL SDINPHWSDE KVYQETRRIV
     GALFQHITYR EFLPLVLGKE VCRLFDLELE TSGYYRNYDG NVNPTIANEF SAAAFRFGHS
     LIQSTYMRAD RHHRFIANNV SLHEDTSEGD FGGPGSLHRL LRGMVNQRAL KRDEFITAEL
     TNHLFQTKSF PFGLDLAAIN IQRGRDHGLP AYVNWRGPCG LSTIKDWSDL ERVMAERPVV
     GGIVGPTFSC IIAQQFSNLR KGDRFWYENP GFESSFTPAQ LESIRQVAFS QVLCRALGGG
     GTLQPFVFLP SDFGQNERLP CESRLMTPID LTPWKERDPF NNDTGDEDED DDDDDNDEED
     DDEPTPGNGT VPIADQATAQ SSTFSSTTTT TRRPSLVPET SSNVINKVDL ITNGNTGVQP
     NRQRPHSSTL TVGPTVIISN KVDLTPTSNR PASPSGQSST PTVIDHKLDL KVTTKPTQKR
     KPTRKTTTKK RPTSSGTRPL VTSNLDFSAS RNTNGTITSD EQPTDRQELV RTRRALNKVR
     DVDARYGYYQ TPSPPPDYND YDEDYNTDYE PPPPYIAYGY HRPTTTTTTT TTKPPPYGYY
     SPYGGGYYTA PPTPPPPPPP PNPYFDTRRP LRTTTPRRRL SDKLTLNADL PQHAPQRPRT
//
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