ID A0A0N4ZC99_PARTI Unreviewed; 697 AA.
AC A0A0N4ZC99;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=ShKT domain-containing protein {ECO:0000313|WBParaSite:PTRK_0000515300.1};
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_0000515300.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000515300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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; A0A0N4ZC99; -.
DR STRING; 131310.A0A0N4ZC99; -.
DR WBParaSite; PTRK_0000515300.1; PTRK_0000515300.1; PTRK_0000515300.
DR Proteomes; UP000038045; 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; 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 InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF61; PEROXIDASE MLT-7; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00254; ShKT; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51670; SHKT; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..697
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005891477"
FT DOMAIN 32..71
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT BINDING 467
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 697 AA; 76975 MW; 08C80A7F4D44D455 CRC64;
MRHISTIILI IFFCIEKISS ELSPPITEKF KCLRNGCCDQ HEWCRFWASI GECRTNSEWM
NISCQLACNT CKSSSRGTEP ISHQSSDSSL SKDLGSCEGI RKNPSTAIED LKKSGLITPV
EDISSRIILS IDDITRSVPT GCVPQIASAD CRKALCYHLS YRTFDGTCNN LDNPLKGAAF
RQYLRLLPPA YDGGSMGEPV DSLNPTRPTA REACRLLLSS GQVVNHDTFN TLMMQFGQFL
SHDMSKTTLQ PTSQCKNCSP VPSKCIPIKI SPKDRNEGFK KKECLKMSRS APICGTGQTT
PRQQLNENSG FIDGSAIYGS STKDLHKFRE GRTGFLKMTA FNNKLFLPFD TSKCVSKQNC
VASFTTGDIR GNLFVGLASL HILFAREHNR IARSLQAMNP GWSGDRVFQE ARKINGGVLQ
HIVYTQYLPK IMGTAMDSII GSYKGYDNTV DPTVSNVFVT AGFRFGHGMI QEVFKRIDGS
GNSIPDGPLN FGDGVFKSAK LLFEGGIDPI VRGLLLQPVK RPHRMTPAIT ERMFGSTDLG
AVNINRGREH GTPSYNAWRE FCGGKRATSF EDFSDHILDK NVRGGLAKAY QSPDDVDLYV
GAMLEDPVVG GLIGSTLSCI VGNQFKRSRD GDRFYYENPG IFTPEQLQQI KNGSLSRIIC
DNGDSFQVIT EDAFLVPKNG MTACKNLPIV DLSKWKE
//