ID A0A0N4WKW3_HAEPC Unreviewed; 1306 AA.
AC A0A0N4WKW3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Chorion peroxidase {ECO:0000313|WBParaSite:HPLM_0001174501-mRNA-1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001174501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001174501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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DR WBParaSite; HPLM_0001174501-mRNA-1; HPLM_0001174501-mRNA-1; HPLM_0001174501.
DR OMA; MYTIWMR; -.
DR Proteomes; UP000038042; Unplaced.
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; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF131; PROTEIN CBG17660; 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}.
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1013
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 1306 AA; 146401 MW; C5D505517CA6A0AE CRC64;
LPSASDVAAL FTPAPRGHAT CSLMLAQWAS FIYDDIAHVA TNQLVKEGFF PGSKHLPLPC
CSSSTNHPEC FPIIAADGKC VSYSRSLPAP RENCSLGPRE QGNTVSGYLD ASQIYGSSQE
IVDKMRSFKD GLLNLRILSA SHGGLPQADD DEDCKSRTLS SEPCFMAGSS RINLLPSNAV
MYTIWMRQHN LIAGKLKEVN PVWSDEKLFQ EARRIVIAQI QHITYNEFIP VIVGKENLKR
YALDLQVNGY DSRYDMKVDG STLNVFAAAV GQFFLTLLPD KITVIDSFGN TKREDPLGRV
FNDPSFIYQR NRLDAVLRFL TRSPIMKPGL HMTPELKHAF KRGIGTGEKG IDMAAQIIQM
GRDHGIPGYL EWRRHCQLDN VQSFASMSAR LLPSVNASLF EQLYESPEDV DLIVGGLAEA
PLPGSLLGPT LSCLFAKQME KTKRGDRFWY ENFFYPSAFS TSQLEEIRKT TLARIICDNS
DDLRFIQHNV FSLQDEYGSH AGDDFSESGN KEKKEEMGRN CPVSCSSSVI DSIDFSAWKD
EEPKRALPIT KATLEKAIRL GIEQYNRLQA AEGRRIRAQG PPPNAAGQSA VFTHAALMAP
KRESIDIART AGVLREATQV LIKGTGLNEG ERLPLGLDVS TLQQLLPDVE VESIIGNFTP
FLGHDPLPKE QCLPQPLPCD HTSKYRSYSG WCNNLQFPKY GNAFVGMRRL LDPAYDDGFD
APRTKARSGG ELPSARVVSN VVHNDAPEFH VRFTHMLMQF GQILDHDMMH SPIARGPNNT
ILNCSSCDSQ ERLSIHCFPI KIGKDDPFFP ATHQDGRPRC MPFTRSLLGQ LTLGYRNQLN
QLTAFLDASS VYGSTECEAN QLRLFSMGKL NFTDLGFNKE ALPQGRQERD CRSVLSSTQK
RCFVAGDERN NEQPGLTVIH TILLREHNRI ASQLRRVNNF WTDEQLYQEA RRINIAKLQH
VIFKEWLPVV LGCETMAKYD LMPKKSGYFT GYDPHCDPAI SQEMSTAAFR FGHTLIRAKF
PRLTDTYRNM SDDDHFSDPS PLYERQNGHL ESMLMGLIGS ESMAFDRHIT NAVRNHLFAK
PGGPLTGIDL PAVNIQRGRD HGVQPYNKYR ALCGLRPAQK FDDLRSTMDD SAVEALRKVY
EHVDDIDLFP GIMSERSMKD QLAEIRKTTF AKIICENSQF ARKIQPNVFL MADELTNAPT
SCSELPDTDL FEWLDREYCL VDHRVINLGK TKRITPCVTC TCTREGPECH SITIDHCDRL
FDDYLASEIA KVGMLLQPED RLRAKAFLGS GLRDPMCSIC QGASSE
//