(data stored in ACNUC8465 zone)

SWISSPROT: B6HEB5_PENRW

ID   B6HEB5_PENRW            Unreviewed;       633 AA.
AC   B6HEB5;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Pc20g02270 protein {ECO:0000313|EMBL:CAP85556.1};
GN   ORFNames=Pc20g02270 {ECO:0000313|EMBL:CAP85556.1}, PCH_Pc20g02270
GN   {ECO:0000313|EMBL:CAP85556.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 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:CAP85556.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85556.1, 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.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
CC       oxidoreductase family. {ECO:0000256|SAAS:SAAS00677740}.
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DR   EMBL; AM920435; CAP85556.1; -; Genomic_DNA.
DR   RefSeq; XP_002562785.1; XM_002562739.1.
DR   EnsemblFungi; CAP85556; CAP85556; PCH_Pc20g02270.
DR   GeneID; 8307173; -.
DR   KEGG; pcs:Pc20g02270; -.
DR   eggNOG; ENOG410IEVN; Eukaryota.
DR   eggNOG; ENOG4112CFH; LUCA.
DR   HOGENOM; HOG000159116; -.
DR   OMA; NGALMNP; -.
DR   OrthoDB; 827142at2759; -.
DR   BioCyc; PCHR:PC20G02270-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HEB5.
DR   SWISS-2DPAGE; B6HEB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   FAD {ECO:0000256|SAAS:SAAS00677734};
KW   Flavoprotein {ECO:0000256|SAAS:SAAS00677742};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    633       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002843571.
FT   DOMAIN      169    348       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   633 AA;  68838 MW;  95EFFDC07B9CD398 CRC64;
     MSPCSFMTGI FIVALLLVTH GDARAGQVSS ASVAGAPLFD SEKFQLTDND IAKLSQQQSA
     LVKFGCDGTS KPTQPTRKCK VFPGDRQWPS QSVWSAFDDL LGGALIKTVP LAASCYSSWP
     QYDSDECERI SSQWTDSHLH AADPASAMWP LFEGRTCLPT TNASASCTLG GYSSYSVNVS
     NVAQIQLAVN FARNADIRLV VKNTGHDFNG KSTGAGALGI WTHNLKDIEY YENYRGSGYQ
     GPAVKMGAGV QAFEVYAKGQ ELGFTAVGGE GKTVGVTGGY VLGGGHSPMS SLYGLAADQV
     LALEVVLANG RFVTVTEESD PDHFWALRGG GGGTYGVVTS LISRVYPKVG VTVSTFNFST
     GKDVSVETFW AGVRSYLERF PTHADAGTYA YFWIMPTGPN AFTFLMNPFF AVNHTVDEFN
     ALVKPWYDDL HELGISFQPN TTYYDNFYDG WMAGFALETV ASSTMMTGSR LFPRANWDTP
     TSLNATLNAL RATITDGFAL LAFNMKAELH EGFTSNSANP AWRQTLMHAI TSTSWTNTTS
     DADIKVKMDD LTKAVGKWRA VCPDSGAYMS ESDIQEPHFQ QAFYGTNYDR LYKLKQRYDP
     TGLFYAPTGV GSEDWVVKSL DGLPDQNGRL CRV
//

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