ID A0A0V0V135_9BILA Unreviewed; 771 AA.
AC A0A0V0V135;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=Peroxidase mlt-7 {ECO:0000313|EMBL:KRX57225.1};
DE Flags: Fragment;
GN Name=mlt-7 {ECO:0000313|EMBL:KRX57225.1};
GN ORFNames=T09_967 {ECO:0000313|EMBL:KRX57225.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57225.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57225.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57225.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX57225.1}.
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DR EMBL; JYDN01000106; KRX57225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V135; -.
DR SMR; A0A0V0V135; -.
DR STRING; 181606.A0A0V0V135; -.
DR Proteomes; UP000054681; 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:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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 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 Oxidoreductase {ECO:0000313|EMBL:KRX57225.1};
KW Peroxidase {ECO:0000313|EMBL:KRX57225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT DOMAIN 80..114
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT BINDING 539
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 80..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX57225.1"
SQ SEQUENCE 771 AA; 86513 MW; B133C7E2F418F563 CRC64;
LIGKLVVVFI WKEYFNVAVY VAKIRRTCCQ RKIKDDIGMS KMHDFHIQAI TFCLLGSFIG
LLSHGADPIT KNFRCISANC CDQHEWCGFW AGIGECETNK NWMTRNCQIS CKKCDDTNTI
VNSTTAAPVT ESAKAKKVSQ PSVSTTKKQT AAPPRQMLRR GHDPLFCAEM LRLNGSERFQ
EMSRNGAIVV FEDATSRRLL SARDMVTNNQ MMGCFREQDT SDCSRNMCFH AMYRTLDGTC
NNLRNPLIGA AGTTFNRILP AVYEDGISTP ISTRPGSRPS AREATRFLLS SPQLVTSSKG
NMLLMPFGQF IVHDISRTSL LPADRCGSCT DIPGRCFPIK VETVDPRFGC ARPPCCLFFT
RSSPLCGTGA QSKREQVNEN TAFLDGSAIY SSSLPDSLRL KDSKTGMMRI TFFNNHVMPP
FNPHTCFGPN NCNANLDVGD NRGTLFLSLV GVHAVFLREH NRIAQQLLKL NPSWSAERVF
QETRKIVGSI IQAITYKEYL PKILGIRYNS LMGNYTGYNP NVNPSIINEF TTAAMRFGHA
MITEFYERAD EHGNAVPNGK IRFDQGVLRP ARLLFEGGIE PVMRGHLIME VKRPQRVTTS
VTENMFGSTD LASTNVQRGR DHGLPSYNKY REFCGLKKAR TFDDLSNEIL DPNLRNNLHQ
TYKHTDHIDL YVGGLLEDPV IDGLVGPTFA CLIAEQFRRL RDGDRFFYQN PEIFRPDQLA
EIEKVSMSKL LCDNMKGISK VPKDAFTVMK ESEAVSCSSL PSMNLSKWAT R
//
