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Database: UniProt
Entry: K1WP77_MARBU
LinkDB: K1WP77_MARBU
Original site: K1WP77_MARBU 
ID   K1WP77_MARBU            Unreviewed;      1038 AA.
AC   K1WP77;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   05-JUN-2019, entry version 29.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EKD14751.1};
GN   ORFNames=MBM_06962 {ECO:0000313|EMBL:EKD14751.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina
OS   leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD14751.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD14751.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD14751.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; JH921444; EKD14751.1; -; Genomic_DNA.
DR   RefSeq; XP_007294851.1; XM_007294789.1.
DR   EnsemblFungi; EKD14751; EKD14751; MBM_06962.
DR   GeneID; 18762897; -.
DR   KEGG; mbe:MBM_06962; -.
DR   InParanoid; K1WP77; -.
DR   KO; K19069; -.
DR   OrthoDB; 798314at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR038697; CHD_cytochrome_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006753};
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     42       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      529    552       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      695    709       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   REGION      414    433       Disordered. {ECO:0000256|MobiDB-lite:
FT                                K1WP77}.
FT   REGION      972   1020       Disordered. {ECO:0000256|MobiDB-lite:
FT                                K1WP77}.
FT   COMPBIAS    992   1020       Polar. {ECO:0000256|MobiDB-lite:K1WP77}.
SQ   SEQUENCE   1038 AA;  110574 MW;  B653CE7C12EA8D4F CRC64;
     MLTASQDDEC SCKGSSAACG IIITFALTPA TLVIGIALLL ILDRKHRTLI RIKSVRYIRS
     HGAQGFAGKD LPPMPVLSVM HNVRGSQLPE LTWPTRSRPW WLWPSGPATI FYVVSHLLPS
     SRTSRSGIRN QKAATRSMAI TAVINGGNDL ACAASGPIPS HLFEDQYPAN TNGRANEKAV
     IVKGSAARYR TTHARYCNLE LFSRVPTARK EFEHVPATEI SYRHYTCRRR IPAHSASDGS
     QISEGTYTFG IAMPATASSD FIGRISSQGN AGWAGISLGG PMRGSLMVVA RPNEGAVIGS
     LRLATGYANP GVYSGAATLE IIAEGTAYDT ESTNFTMTFL CKGCLQGDDS TFAAADATTN
     LGWATSSVDV TTPADASTVL GYHDTGFGLF AVDLAAAQSA SFAEWAALAS QSYSNSPATP
     TNPTAGGGAN GYGNNTAPAT PPTVSNTTYD YIVIGSGPSG LISSQRLTET GKSVLLIERG
     MATTFSSGGE RFVPWNNSLT YYDVPGVWGF MNEGTQGEAY CTDTAAIAGC ALGGGGAVNA
     MAFIRPANFD FDDKWPETWK SADLAPAAER LYSRNPGTTI PSNDGISYDN ATQAVLEPFF
     EQNGWSNTDY VNDPDSKDQV YGLPSLNVAN GLRSGPIHTY LPLAQAKPDF TLALHTKVIR
     ILRNASTITG VEVENASGRE IINLNPSGAV ILAAGSMSTP RLLFNSGIGP TEQINIVKSS
     PTGVTVPESD WISLPVGVGI KDHSTYALIF NVTGGITARS REEVMNPSEL DLSLYQTGSG
     VLAHSQQRLD VFRKINMTDG HTIGFQMHCM SVNVNDTITC QAFETHGLTS AGVLGIKPDQ
     ATYFTKEPWA NNDVDRKAWE MFIDEVFEMA RQPGSPLVYS GGAEMTAAEY LAASKVSNGY
     HVVGSTKMGS DDGRRNGTAV VDLDTKVYGT DNLFIVDASF HPDLPTGNTQ AQVMVAAERA
     IERIIALRGE TWSPTGGYSQ GTPPPTGYTP ATPPTGEKSN GSPEDTPPTG EKTNGYPQAT
     SPEYCCEFEF HILNWRAT
//
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