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
//