ID A0A3F2Z099_ANOME Unreviewed; 658 AA.
AC A0A3F2Z099;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chorion peroxidase {ECO:0008006|Google:ProtNLM};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM019493-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
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 merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM019493-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM019493-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR AlphaFoldDB; A0A3F2Z099; -.
DR STRING; 30066.A0A3F2Z099; -.
DR EnsemblMetazoa; AMEM019493-RA; AMEM019493-PA; AMEM019493.
DR VEuPathDB; VectorBase:AMEM019493; -.
DR VEuPathDB; VectorBase:AMEM21_016086; -.
DR Proteomes; UP000075903; 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 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:SF142; CHORION PEROXIDASE; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..658
FT /note="Chorion peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017767392"
FT BINDING 423
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 658 AA; 75151 MW; 25A1993845E3D24C CRC64;
MVHYFFRQRW IAFPLWICTV LQLQRMVEVE SSYRLEDQPV TYVSYDMQCG YQSKCCSDNS
CPSLDGLHSL ERKARKKAIL ELLNNEATVN DPRFLMDGTD FDVRFFNTIA IQPSEQLGVR
DTLTTQKVLK TYRSYDGSCN NLDHPRWGMR GTALKHPIAP CFDDVVSQPA RSKSGASLPQ
NRKLIAELAA MLKEREISTT AELNMCSVFL SEFFTLDMIG RSTKRTKRGT DGFRGCRADG
HDRSPFVTPL FNPLLVSPND PYYGPLGVRC LNFSPQERAN DRCELKHMTD RNLQSSYFDL
SNLYTEQATY DKDGKLLLQQ CGAPETITNR RPMSVQFFAV AGLFAKLHNY CVDRAPMKGS
GPVEERCRAF TIAVYQKIIY EQLIPVLFGE QFYSECDFSC EYNPDEECAV SQVYKHGPGR
FQHVWIGETM LYKPARGEVE WRSFNDFFHN YESFDCLGAL AGSLDTPINV GNLASASVDK
FVTVDGYRGT SLPCIDLARN RDAGLCPLVT YKHHVEQLFG EESRCYSTFE DLSDIFAPDV
IEFFSRHYEH PDDIDVLFAN MDQRFHPGAN LPKMVAQLTC LEMKRLKCTD RFFYTWNPNL
GEGRARQLIE AIDFTVLLAL VTEMEEVPLQ PFFVGSPTVA SCDVRDYMQS LDHLFSDL
//
