ID   A0A0N4ZT87_PARTI        Unreviewed;       965 AA.
AC   A0A0N4ZT87;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Peroxidasin {ECO:0000313|WBParaSite:PTRK_0001171600.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001171600.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001171600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0N4ZT87; -.
DR   STRING; 131310.A0A0N4ZT87; -.
DR   WBParaSite; PTRK_0001171600.1; PTRK_0001171600.1; PTRK_0001171600.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; cd09826; peroxidasin_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF58; PEROXIDASIN; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 2.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
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   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..965
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005892204"
FT   DOMAIN          42..128
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          135..222
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         696
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   965 AA;  110038 MW;  F216558CCF2C994C CRC64;
     MGQKYRGILF FILLILSNNF LNGQVESNRR NNRQPRPNNN APRFTYTSNN QGYREGSSVT
     INCEVSGNPA PSVSWAFKGR QIHDSRKYQM KQRNSHLTIY PFLEGDVGKY TCVAMNRYGT
     VSHEIDLKII QSVPPFITEG PQSQRVKPSE RVTFRCKAKG EPKPHITWFF EGSEIQNLAG
     HFQASHDETE LIITHVTRQD NGVFTCMAGN DVGAMTADAT LTVEAPTLNR IDHSLDDNKL
     QEIVRKATEN VDRAIAETQR DLKYSMTDPR NLIKLFKFAA PRATEITKAR EIYEESLRLI
     EKHVEDGLRL PLNELPTNIS YESILAVSHI QTLMELSGCM NGQFREPCDK NMCFHQKYRS
     YDGQCNNFDN PMWGVSQMPF LRLLPPIYEN GFNTPVGWEK EKLYHGFKKP NARLVSMEVI
     SSKDITPHFR YSSLLMQWGQ FLDHDITFKA PALSRKIYAT GGICNRTCEN ITPCFNIILP
     PGDPKLKHAR GKFPCMEFDR SAAVCGSGET SPIFQRVSYR EQVNIITSFI DASNVYGSTE
     VDAINLRDLY NDHGLLRFDI VSGSEKPYLP FERDSDMECR RNVSEDNPIR CFLAGDFRAN
     EQLGLTALHT IFLREHNRIA GKFLQINPNW DGETIFQETR KILGAVAQHI TYEHWLPKVL
     GEDGIKHHLG EYKGYDETVN PGITNAFATA AFRFGHTLIN PKLIRLDKNF EPIQQGHISL
     HEAIFAPERL LSEGGIDPIV RGLFASPMKL PRSDQILNKE LTEMLFHKES EVPLDLAALN
     IQRGRDHALP GYTEYRRYCN LSVPNTFEEM TTYVTDPAVL PKLKKLYGHP GNIDLFVGGV
     VEKKLADALI GPTFSCIIGE QFKRLRDGDR FFYKNSGVFT QLQLTQIKKY TISKIICNNG
     DDIDRIQKDS FMFVGDKKPS FQKCDELPDL NLHMWSSCCD GTCNNPDSPL DSKRRKRNQH
     FYSRS
//