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Database: UniProt/TrEMBL
Entry: B3RSQ8_TRIAD
LinkDB: B3RSQ8_TRIAD
Original site: B3RSQ8_TRIAD 
ID   B3RSQ8_TRIAD            Unreviewed;       592 AA.
AC   B3RSQ8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV26560.1};
GN   ORFNames=TRIADDRAFT_22758 {ECO:0000313|EMBL:EDV26560.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26560.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV26560.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26560.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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DR   EMBL; DS985243; EDV26560.1; -; Genomic_DNA.
DR   RefSeq; XP_002110556.1; XM_002110520.1.
DR   AlphaFoldDB; B3RSQ8; -.
DR   STRING; 10228.B3RSQ8; -.
DR   EnsemblMetazoa; TriadT22758; TriadP22758; TriadG22758.
DR   GeneID; 6751769; -.
DR   KEGG; tad:TRIADDRAFT_22758; -.
DR   CTD; 6751769; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_006087_2_2_1; -.
DR   InParanoid; B3RSQ8; -.
DR   OMA; KHPGNID; -.
DR   OrthoDB; 4560at2759; -.
DR   PhylomeDB; B3RSQ8; -.
DR   Proteomes; UP000009022; 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; IBA:GO_Central.
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   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF58; PEROXIDASIN; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 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   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   BINDING         352
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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EDV26560.1"
SQ   SEQUENCE   592 AA;  67581 MW;  E285C9CA4507F5A1 CRC64;
     TPIHEQILSK VSSCKPVLKP KRCRKNKFNR LYRTEDGTCN NFRQTTWGAA PTLFRRAIPS
     RYANYINKPV GWSHANYLPS PRLVSNRVIS SRKITLSSRY TDLMMHWGQF IDHDLTLTVT
     VDKKIEKICS QSCKKYSHCF PIPVSKQDSK FSCEKCLQFT RAAAACGTGL TSIVYGSARP
     REQINGITAF IDSSNVYGSS KKESNLLRKR RSKGLLKVGK RVSRGKFLLP FAKKGQTECQ
     PSDILKPCFL AGDKRANVQI GLTAIHTIWV REHNRIAKRL ARINPRWNSD RVYQETRKIV
     IAQNQHVIFY HYLPKLLGVT FPTLIPDYSG YKKRVDPSIM ASFAAAAFRI GHTLINPVLH
     RLDSNYQPIP QGSIRLKDAF FAPHRILNEG GIDPILRGIT GKYGKLKSPS RLVSKEVTDH
     LFEVDHQMAM DLASLNIQRG RDFGLPSYNT WRKRCGLRKA RRFSQLSGEI DRKTIAKLAQ
     VYDHPNDIDL WVGGVSEKNI RKGVMGPTFA CIIAKQFIKI RDGDRFWYEK PGVFTSQQLR
     QIKQSSLARV ICDNSDGITR IQEDVFRDYN TTGNAFVDCN TIPRINLRKW KD
//
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