ID   A6QUP4_AJECN            Unreviewed;      1324 AA.
AC   A6QUP4;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HCAG_01100 {ECO:0000313|EMBL:EDN03236.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN03236.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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DR   EMBL; CH476655; EDN03236.1; -; Genomic_DNA.
DR   STRING; 339724.A6QUP4; -.
DR   VEuPathDB; FungiDB:HCAG_01100; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd20612; CYP_LDS-like_C; 1.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo-like_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF13424; TPR_12; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT   BINDING         425
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   1324 AA;  149481 MW;  D08C396799163F35 CRC64;
     MQFLHISSLA EYPTAQIIMW HPLSKLELCM DRAPRSLDPD VKTENNKLLR TPKNGHVNGK
     LKDAPLPVAK RSKGRRVERQ EIEDTFAKYS EFSGDHSRMK KDGSSGKFQE VRWMGWKGVR
     TLLEVVKSKT SGKLVDDRDY LMERIIQLVA NLPPESSARE QLTKTFVKSL WVSLPHPPLA
     YLGDEYRYRA ADGSNNNPMF PRLGAANTPY ARSVRPITIQ PAALPDPGLI FDSLFARQEF
     KPHPTGVSST DPRNQHISQT SSYLDLSTLY GDNQDDQNQM RTFKDGKLKA DTFSDPRLLA
     LPPACSVILV LLNRFHNYVV EQLAQINENG RFTKPHANLP PDQSAKAWVK YDNDLFQTGR
     LITCGLYINI TLYDYVRTII NLTRSNTTWS LDPRIDTKKV AAPESAESGV GNQVSFEFNL
     AYRWHSCIGQ LDEKWINDIY HDLFGKSGED ISMPELMVGM GKWKQKLPED PSKRTFAKLK
     RQADGRFRDE DLARIITEAT EEVAGTFGPR NVPKALRAVE ILGIQQARKF GCGTLNEFRK
     FFGLKQYESF EEINSDPEIA GQLRNLYEHP DYVELYPGIV SEEPKIPMVP GAGICPTYTI
     SRAVLSDAVA LVRGDRFYTS DYNAKSLTNW GYTETHYDLS INQGVPDSIY AHYPMTIPSV
     NKEIFAKLGR QSHFSWDRPA LLSPRIDLTS YNGAKTILQN SKDFRVTWEA SLGSHLASQG
     FNESQAKVID ETFAQDSWRE EVKQFYQDIT QKLLKRNSVK IAGINQIDIT RDLGNLTHVH
     FAASTFNLPI KTKDNSKGVF TDHEMFMVML AAFTSVFSDV DPTKSFPLRQ VAREVGEQFG
     QVVESYVKSI KAFNPFSSII DRFQKDGNTL AKFGADATRR LLKAGLSVPQ VALSYILPII
     CTAVPSQAQA FTQIIDYYLS DEGKIHLPDI NSLAKEDSLE SDTKLLHYCM EGLRLNGPFS
     SYRDSNANIL INDGGREVSI NDGDTVFISS ARDPNIFPRP DEVVLDRPLE SYIHYTDGAF
     TCFGRDAQMV ALSSMLRVVG RLDNLRPAPG PQGQLARISR PDGHFAYMRE DWGGYSALPM
     TLKVHYDATE AQPIKIITNY LAVWLLSEQI MLTPSYDFIE LLYCCTWYLF ERGRFDISFS
     IAEKAVEFAK RSLKIKEQAV ADNALDKHHP QLANSYINIG VFIAGMNPRD AIRLHEKAIV
     IREGSPKYAD DQMQLLSLNY MNIGRCWWMV KGLDKATAAY EKSISIIKEL EEATGAPFAQ
     KSWAMSALAN VLIDKGKFDA AFDLFTQSVK VHQQVLGATH HKTVACYNKI AWFLRKQGEY
     GMAM
//