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
//