ID A0A0N5C564_STREA Unreviewed; 1050 AA.
AC A0A0N5C564;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=ShKT domain-containing protein {ECO:0000313|WBParaSite:SPAL_0001309300.1};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001309300.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001309300.1}
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}.
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DR AlphaFoldDB; A0A0N5C564; -.
DR STRING; 174720.A0A0N5C564; -.
DR WBParaSite; SPAL_0001309300.1; SPAL_0001309300.1; SPAL_0001309300.
DR Proteomes; UP000046392; 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:SF85; SHKT DOMAIN-CONTAINING PROTEIN; 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1050
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005895372"
FT DOMAIN 40..79
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT REGION 203..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 822
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 1050 AA; 117704 MW; 604684B8D6836C24 CRC64;
MSIPLGGMRR WIIELIIIGV LLLIIAESKD DNPITKNFKC RRNGCCDQHE WCRFWASAGE
CMVNKKWMEE NCQLACNACK RLNPKVVPTK KAASKIPIPR ALLLSKPIAS THIASKPPTL
LNEVNKKIIF VKSPSQGTLK IPASNTRFIN NKPQTISRLQ VVTRKPITIL KQPPLSRVAT
TPQISNVIKP LQHPLRIPSK PSTKPFDNAQ RPNNNNHFMP SHTPRILEKP KIVTTTVQPP
PKQDSFNGTL TTPHNKIIIS GSIDDVPSSA VSTKIITHEV TDKSILSQNN PQITPILPID
VVKNESLSSS SLSLKNDTIL NKEDSHLLLN DNIDKILLNN TFILPIDRPN SQKGENLGIV
QPKSEAKRPT HKIGNFKSQT RTFLQSISST PPTLHLPTPS HIVFQTKETV PLKTTLRPVI
QTMKIISTSL RQTTVSPINK SKNVLGSKIE LCRRLLSDPT NIAVNIKKNN LVFTAEDNDG
RRTLSLDDVI RSNLANACTP RLDDSNCERN LCYNLYFRTM DGTCNNLEKP LQGASYRPYN
RLLPPEYDDG LGAPVSSIKI NRPSPREINR NLLSSQAIVH ADDYNSLLMQ FGQFISHDMA
KTTLVPSSKC PGCSNIEGRC MAIKLSANET NKNFLREGCI KVSRSSSICG SGRTKPRQQL
NENTGYIDGS PIYGSSVDDL HKFRQGKTGF LKLSTFMGQR TLPFDQSRCK NDKNCNVIFI
AGDSRVNLFI GLSSIHILFT REHNRIAGIF KRINPQWSDE RVFQETRKLV GAQIQAIVYR
EYLPKILGSA FMTAIGPYKG YNPNVDATIV NEFTSSAFRY GHGMIQETFP RLGENFRNIS
FGSYNFVKGT LNSQMLVKQG GIDPVLRGMM LTKLKRPQRL TSIITENMFE STDLGSINIQ
RGRDHGLPPY NKFRDLCGLN KARTFEELSK EILSPFTRSK LQKIYGSVDT VDLFVGAILE
DPVLHGLIGP TITCIIGPQF KRTRDGDRFY YENPGIFTPQ QLKEIRKSSF SRILCDNGDN
INLVTKEAFR VSNLTPCTQI PKMDLSKWKE
//