ID B6HBN9_PENRW Unreviewed; 1118 AA.
AC B6HBN9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Pc18g00240 protein {ECO:0000313|EMBL:CAP94248.1};
GN ORFNames=Pc18g00240 {ECO:0000313|EMBL:CAP94248.1}, PCH_Pc18g00240
GN {ECO:0000313|EMBL:CAP94248.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP94248.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP94248.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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DR EMBL; AM920433; CAP94248.1; -; Genomic_DNA.
DR RefSeq; XP_002561871.1; XM_002561825.1.
DR AlphaFoldDB; B6HBN9; -.
DR STRING; 500485.B6HBN9; -.
DR GeneID; 8315811; -.
DR KEGG; pcs:Pc18g00240; -.
DR VEuPathDB; FungiDB:PCH_Pc18g00240; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OMA; RHYTIDY; -.
DR OrthoDB; 3322316at2759; -.
DR BioCyc; PCHR:PC18G00240-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c18.
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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 125562 MW; 972DD6B42212EBD8 CRC64;
MLKRFSTQFK RSKDSKDPKE SNGDAEPKST DKSSKRASKV SPSPKSTHKE ENHVVKRSEV
VAVFDKYAQA IHASQEPLPN QTSDGAYLKH DKSSGLINDI KALGFRDVGT VKDLIASKAS
GGIIDDKTYL MERIIQMVAD LPGNSKNRTD LTGLFLDDLW NSIPHPPLSY MGDDYKYRSA
DGSNNNPTLP WLGAANTPYC RTIAPLTIQP SGLPDAGLIF DTLYARQEFT PHPNKVSSVF
FDWASLIIHD IFQTDYSQQH LNQTSAYLDL SILYGDVKEQ QDKIRSHENG KLKPDCFSEG
RLQALPPACG VLLVMLNRFH NHIVTQLAAI NENGRFSAPR PGLSEEETKA AWAKRDEDLF
QTGRLITCGL YINITLYDYL RTIVNLNRTN STWCLDPRAQ AEKADATPSG LGNQCSVEFN
LAYRWHSTIS QGDEKWIEQI YYDLMGKPAE QVSMPELLMG MKKVKGMLEA DPAKRTFGHL
QRNADGYFDD GELVNILTRA TEDVASSFGP RNVPKAMRSI EILGIEASRR WNVGSLNEFR
KHFGLKPYET FEDVNSNPEI ANTLRHLYEH PDYIELYPGI VSEEAKEPMI PGVGIAPTYT
ISRAVLSDAV ALVRGDRHYT IDYNPRNLTN WGYNECRYDL NINQGCIFYK LATRAFPNHY
KPDSIYAHYP MTIPSENRNI MKDLGREQDY SWDKPAFMEP RVNLTSHQNA KLLLENQKDF
RPSWARSMSE LFGKGEFDTK QREAIGKALN TEEFPKLVKT FYEDITERLI AEKGGQLGKI
NQIDITRDVG NLAHVHFAST IFGVPLKTED NPRGLFTEHE MYMILSTIFS ALFFDVDAPR
SYALNRAASA VSNQLGQVVE ATVKADTNSG LFAGIMDNFR PHDNALREFG TEAIRRMKEA
GSSASDITWS AIVPTIVGLV PNQAQVFTQI IEFYTAPENK AHLAEINRFA KTDSAESDEK
LYRYCLEAVR LNGTFGAFRE AKETVTVEED GKTYTVQPGQ QVFASFDQAN HDPSVFPEPN
EVNLDRPLDS YINHGQGPTT GFGEQVTKIA LIAMLRVVGR LQGLRRAPGA QGQLKKIPQE
GGYQVYLRGD GTAYCPFPMS LKLHWDGPFE QKKKVTSS
//
