ID A0A167IA46_9HYPO Unreviewed; 1109 AA.
AC A0A167IA46;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:OAA48842.1};
GN ORFNames=BBO_01887 {ECO:0000313|EMBL:OAA48842.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA48842.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA48842.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA48842.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA48842.1}.
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DR EMBL; AZHA01000004; OAA48842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167IA46; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000076863; 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:UniProtKB-KW.
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 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 PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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:0000313|EMBL:OAA48842.1};
KW Peroxidase {ECO:0000313|EMBL:OAA48842.1}.
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418
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 1109 AA; 124228 MW; A049ACDA2945F43A CRC64;
MQKKTSSIAV DGHNGHATNG HTTGTNAQKR QPLPKYPKPS KSNSQGSQSH LSGILQLRAA
SRRPLPAEMG DGTYRFIKSR PSLLRDLRSM TWSDFKTIKA IVAAKLKRET QTDDKTMLME
KTIQLVAGLP DYSRRQELLT NDFIDKLWYS LDHPPLLYMG DQYRFRQPDG SNNNPLLPRL
GAAGTAYSRT CKPRGMGLGA LPAPDTIFES IMARNEFQKN PNNVSSILWY WATIIIHDLF
NSSSADGNIN NNSSYLDLSP LYGNSQAAQD SIRTFKDGRL KPDAFADKRM LGNPPGVCIL
LIMFNRFHNH IAENLAAINE GNRFPQPTPD LPPEQAAAAW KKYDEELFQT ARLVTSGLYI
NITLIDYVRN IVNLNRVDTT WTLDPRQEMG VAVGTQQGSH SGVGNSVSAE FNLCYRWHSC
ISQKDEEWMQ DFFAGLLGES DQELDFTALM TAMKKFEMTL PQDPGECTFG KFTRGADGRF
NDDELMEALT AAIEEPGGAF GARNVPRIMK PIEALGIIRG RKWHVASLNE FRKQFGLKAY
DTFEDINSDP YVADQLRHLY QHPDNVELYP GIVAEEAKAP MAPGVGIAPT YTISRVVLSD
AVSLVRGDRH YTTDYHTGAL TNWGFNEANY DLSVNHGCVF YKLFIRAFPN HFRENSVYAH
YPMVTPAENR KILANLGRAD WFNFDRPTYV PDKIDIVSHT AFKHVLGNDA TYHPDWRQGL
GYLMNERSLD TMLAGGPDLH AIQRSSVGAS LFGQEWKSAV KQFYNNMAET LMAQNSYQIA
GQTQVDIVRD VGNLVHTHFV ARVFNLPLKT KGHRKGVFSE QELFKFLTII YVCIFLDYDP
VKSFPLRRAA KAASAQLGAL IETNVKLGLL FGMRGLYVKK FKNDVLAQYG HQLVQALAKT
GLNAHEIAWS QILPTAGAMV PNQAQMFAQS VDWYLSEEGE PHRAEIERIA AQESTDASDA
LLLGYAMEGV RMAGTFTLYR NVAAPDTFND DAGRPYSVNH GDTVFVSVTP ATRDGGLPYP
ERVDPKRPLD SYVQHGLGPE LCLGREVAQT ALIALFRTVF RKKNLRRVPG LQGELKRLAK
PDGSHGFMTE DWGTIWPFPT SMKLMWDED
//
