ID K5VKM3_PHACS Unreviewed; 544 AA.
AC K5VKM3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKM51943.1};
GN ORFNames=PHACADRAFT_102576 {ECO:0000313|EMBL:EKM51943.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM51943.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM51943.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51943.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; JH930476; EKM51943.1; -; Genomic_DNA.
DR RefSeq; XP_007399735.1; XM_007399673.1.
DR AlphaFoldDB; K5VKM3; -.
DR GeneID; 18907231; -.
DR KEGG; pco:PHACADRAFT_102576; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR InParanoid; K5VKM3; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11061; CYP67-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305:SF29; BENZOATE-PARA-HYDROXYLASE; 1.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 544 AA; 60733 MW; EA3201F89353F8D0 CRC64;
MEQSHFILPQ LDLKLITAIL AASLLAAWII PFLVDKYRLR GYPGPLLAKF SGFWLASKAY
KGTTTSAVYA LHQKYEGPFV RISPKYVSIA DPEALQAIYG HTSGTLKTDF YDAFVTFRRN
IFTSRSRLEH SRKRKYTSHA MSMKGITEFE PNVREYQHML LKQLDTLCAV GAQGIDGVLG
SCPWTTRDGW VLFDCMPWLN FDTFDVIGDL AFGKPFGMLE AGKDAALVPV SEEQAMKSFG
RQDTDLKWAT IPAIKLLNET VPWTFFLGCL PPQARFLMSK LPSFNAGTSR KLFVKLAVAT
VSKRLASEAT RRDFLSHLVA ARNDEGKPLS AQELTAEALN LIVGGSDTTS SSIGVVIYHV
ARNRDVQERL QKELDDVLGV PNSTFSTDEV VAPFELVKNL TYLQDVINEG LRLHSTVGVG
LPREVPEGGM TVAGKALLPG THVSCPTYTL HRLKSIWGDD ADEFNPDRWT RGDRNMMLKY
FAPFSIGPRA CIGRNLAMME MTICIATIVH RYRLVLANPD QQLECSEGFV RKPKNVHVGM
QRRL
//
