ID A0A0K0EPD6_STRER Unreviewed; 651 AA.
AC A0A0K0EPD6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ShKT domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001132000.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0001132000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0001132000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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; A0A0K0EPD6; -.
DR STRING; 6248.A0A0K0EPD6; -.
DR WBParaSite; SSTP_0001132000.1; SSTP_0001132000.1; SSTP_0001132000.
DR Proteomes; UP000035681; 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 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:SF4; LD42267P; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 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 Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01005};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..651
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005328583"
FT DOMAIN 30..64
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT BINDING 422
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"
FT DISULFID 30..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 651 AA; 74719 MW; DB1E91095685D6E0 CRC64;
MNCIIWSIFV YYLLLLPSIY SQQNKCIGNC CDKNDNCEFW ARKNECQRTS EYMLINCPKS
CNFCEKQNSS TKEIDKLNFS GCNHVQTRET TRRQAMNAGI FSQVVISRNC GPENVPNNCS
QSICYHRQFR SMDGSCNNLK HSLYGAAFTS YVRLQEPLYE DNFNQPVGRR IYRPDVRDVT
RFLLVHDKNI NSKYNQLAMQ WGQFIAHDIL ANGRHESCRC EMRNADHCQN IYFKFGDPKF
GRIPCIRLAR TVNKCGTGIF GVPREQMNQA TAYIDGSPIY GNNIGNMESL RSRQFLRAQR
SNGKEFPPIG ITAVGGHALI TGDNRADIFS GLSALHTIFV RYHNNIARQL IEINKSWSVD
RVFHETRKIV GSVLQVITFK EFLPAILGKK NSDKLIPPYS GYNENVDATI SNEFAAAGFR
LHGTIAQHYP LIDENYRTIA NNDFIQNVET FIREYSTKIS FLFRGMIASP LKKAQRINPQ
ITERFFGGTV DISSMNLQRG RDHGLRTYND YRRLCKLDPV RSFETWADVT DPSVRRKAKE
LYLDVENIDL FTGATLEEPL EGSVVGPTFA CIIAEQFVRI RDGDRFWYEN NQLFTPKQIN
NLNKMSIASV ICKTEPEIGR IPKKAFITDR GQKAKRCEEI PQLDLSLWKS F
//
