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Database: UniProt
Entry: U4TZ38_DENPD
LinkDB: U4TZ38_DENPD
Original site: U4TZ38_DENPD 
ID   U4TZ38_DENPD            Unreviewed;       697 AA.
AC   U4TZ38;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=D910_02714 {ECO:0000313|EMBL:ERL85293.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL85293.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL85293.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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DR   EMBL; KB631673; ERL85293.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4TZ38; -.
DR   Proteomes; UP000030742; 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   PANTHER; PTHR11475:SF140; CARDINAL; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 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:UP000030742}.
FT   BINDING         432
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"
SQ   SEQUENCE   697 AA;  79083 MW;  30336E8806836235 CRC64;
     MKTNDRGNWD HAMQEGEMFL ESKDSIEKNA SSLPIDSPSY RHQRVMGTSD KARELSRKGY
     QLEGAARFLY GSNQTKSRKE FTCPANYSDP FLREMCSNET TTCNGLLMYR SYNGTCNNIK
     YPNTYGVAYR PFRRAIQPDY ADGISKPRES KNGPLPSART ISLEVHRTFH KDDVKFSVMV
     AVWGQFLDHD ITATALSQKK NGSSISCCVK NEISSPDCFP VIISNADPLS MYNVTCMEFV
     RSAPSPQCCL GPREQMNQAS AFIDGSVVYG SDESKALSLR TMSKGLLKMY TTDDNRTLLP
     ISDDMTDGCN REDEISKGRY CFLSGDSRAN ENLHLTSMHL IWARQHNFLA NNLSSSNPHW
     SDERVFQETR RIIAAQMQHI TYNEFLPILL GKTLMKKHGL LPKSKGYFEK YNASIDASIS
     NEFAAAAFRF AHTLIPGLVK TLASDTSNPE FIQMHKMLFN PFQLYQSGQL DSTIKGAMNT
     SIAASDSYFT DELKSHLFER DSEQNVAPRK LGLDLVSLNI QRGRDHGLPG YVFWKEHCGF
     KRSRTFEDLE DIMEAFSLQN IKAVYRYVED IDLYTGALSE KPLKGSILGP TLTCLILDQF
     IRLKFGDRFW YENPQPPYSF SIEQLDEIRK TTLARVICDN ADYLDTIQPQ VMHGLTGKNE
     NIPCSNVSTP NWLLWKENLH YVGFPTQRMN VRLLTSG
//
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