ID A0A0V1CTI6_TRIBR Unreviewed; 1443 AA.
AC A0A0V1CTI6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Peroxidase mlt-7 {ECO:0000313|EMBL:KRY52472.1};
GN Name=mlt-7 {ECO:0000313|EMBL:KRY52472.1};
GN ORFNames=T03_2671 {ECO:0000313|EMBL:KRY52472.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52472.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52472.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52472.1};
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:KRY52472.1}.
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 EMBL; JYDI01000104; KRY52472.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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 CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 3.
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; 3.
DR Pfam; PF01549; ShK; 2.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00254; ShKT; 2.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS50292; PEROXIDASE_3; 2.
DR PROSITE; PS51670; SHKT; 2.
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:KRY52472.1};
KW Peroxidase {ECO:0000313|EMBL:KRY52472.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 93..127
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 807..841
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT BINDING 514
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 93..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 807..841
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 1443 AA; 161106 MW; FC5ADB85DA1E71FD CRC64;
MILDNINVGY KTAAATAATS LTFSVEILRN IGMSKMHDFH IQAITFCLLG SFIGDESILD
NLLGDIEFLK FTGLLSHGAD PITKNFRCIS ANCCDQHEWC GFWAGIGECE TNEKWMIGNC
QISCKKCDDV NSTTAAPVTE SVGVPTSDKG NSTLPRLKLR RGNDPLFCAD MLRLNGSERF
QEMVRNEAIV VFEDMMMNNQ MMGCFREQES GDCSRNLCFH AMYRTLDGTC NNLRSPLVGA
AGTAFNPIRL GSRPSAREAT RFLLSSPQLV TSGKWNMLLM QFGQFIVHDI SKTSLLPADR
CGSCTDIPGR CFPIKVETVD PRFGCVRPPC CLFFTRSSPL CGTGAQSKRE QVNENTAFLD
GSAIYSSSLP DSLRLKDSKT GMMRITFFNN HVMPPFDPHT CFGPNNCNAN FDIGDNRASI
FIALVGVHTV FLREHNRIAE QFLAMNPTWS VERVFQETRK IIGAMIQAIT YKEWLPKILG
IRYNSLMGNY TGYNPNVNPS IINEFTTAAM RFGHGMITEF YERVDEHGKS IPHAKLRFDQ
GVLKPAKLLF EGGIEPVIRG LLMMEVKKPQ RVTSSVTENM FGSTDLASTN VQRGRDHGLG
SYNDYREFCG LKKALTFDEL SSEILDPNLR NNLQQSYKHT DHIDLYVGGL IEEPVVDGLV
GPTFACLIAE QFRRLRDGDR FFYQNPEIFK PDQLAEIEKV SMSKLLCENL KGFSRTPKDG
FAVMKDAEAV ACSSLPSNIN VGYKTAAATA ATSLTFSVEI LRNIGMSKMH DFHIQAITFC
LLGSFIGLLS HGADPITKNF RCISANCCDQ HEWCGFWAGI GECETNKNWM TRNCQISCKK
CDDTNTIVNS TTAAPVTESA KAKKVSQPSV STTKKQTAAP PRQMLRRGHD PLFCAEMLRL
NGSERFQEMS RNGAIVVFED ATSRRLLSAR DMVTNNQMMG CFREQDTSDC SRNMCFHAMY
RTLDGTCNNL RNPLIGAAGT TFNRILPAVY EDGITTRPGS RPSAREATRF LLSSPQLVTS
SKGNMLLMPF GQFIVHDISR TSLLPADRCG SCTDIPGRCF PIKVETVDPR FGCARPPCCL
FFTRSSPLCG TGAQSKREQV NENTAFLDGS AIYSSSLPDS LRLKDSKTGM MRITFFNNHV
MPPFNPHTCF GPNNCNANLD VGDNRGTLFL SLVGVHAVFL REHNRIAQQL LKLNPSWSAE
RVFQETRKIG VLRPARLLFE GGIEPVMRGH LIMEVKRPQR VTTSVTENMF GSTDLASTNV
QRGRDHGLPS YNKYREFCGL KKARTFDDLS NEILDPNLRN NLHQTYKHTD HIDLYVGGLL
EDPVIDGLVG PTFACLIAEQ FRRLRDGDRF FYQNPEIFRP DQLAEIEKVS MSKLLCDNMK
GISKVPKDAF TVMKESEAVS CSSLPSMNLS KWATHLFLKT YHPRVVSDNR NDQKICFVQT
DVG
//
