ID A0A1Z5SQD4_HORWE Unreviewed; 1365 AA.
AC A0A1Z5SQD4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=BTJ68_14303 {ECO:0000313|EMBL:OTA23042.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA23042.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA23042.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA23042.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:OTA23042.1}.
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DR EMBL; MUNK01000324; OTA23042.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5SQD4; -.
DR VEuPathDB; FungiDB:BTJ68_14303; -.
DR InParanoid; A0A1Z5SQD4; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000194280; Unassembled WGS sequence.
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; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1365
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012916092"
FT DOMAIN 347..370
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 517..531
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 224..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1365 AA; 144242 MW; 3F403B0CDCC537C8 CRC64;
MVKITNLAGA LALGASTASA QTFKTYTDDN GIEFWQSTFE TSVGDGGAQF GLALPAAAQS
GFEEEYIGHL VVPKGGDDGT WMGLSHMSGM TGSLLLLSWL DGDEIMTSFR YASGYTQPDI
YNGNATLSKI SQNINDTHFE LTYRCENCWS WDHEGAAGDQ IPATTSSAVQ IIGWAQATQA
PNSPSDADSD IKQHDDDGIF GAAVGSARNS AYTSWVSLAT ATSAPATATA TPTGSTNGTG
SAGPTATATP TAAACPSANT MANSTWDYII VGAGAGGIPL ADKLSEDGSS VLLIEKGPAS
SGRWGGTMRP EWLVGSNLTR FDVPGLDNQI WKDSEGIACE DYSVMAGCVL GGGTAVNAGL
WWKANPEDFD YNFPEGWKSS DMQSAVDRTF ERIPFTDHPS MDGIIYKPQG YNIVSGALAA
AGWENVTADE VPGKKNHTFS RPNHMFSNGE RGGPMATYLV SASERKNFQL ITNTTVPRVI
RDGSHITGVE TEAFLDGGMC GEINVTPGTG KVILSAGAFG TPKILFRSGI GPQDQLEIVQ
KAEGSAMVGS SDWINLPVGH NLDDHTNTDI VITHPNVSFY DFYAAYNNPI KSDAESYLND
RTGILAQSAP NLSVLFWEEI LGDDGIVRQM QYTARVEGGH GISSNQSMVI SQYLGRGKTS
RGRTVINGAL DMTVSQVPYL NNEHDISAVA AGIESLKAAL SKDPQIKIVF PAANTSTEDF
LADYATTTGS RSANHWMGSC KMGPDSGLDN GTSVVDTDTK VYGTDNLFVV DASIFPGMVS
TNPSALIVAV AEKASGLIAD AKVEGNPNQV SASAPFPLGN STSPQGTGMP SGTGLPYSTG
VSLAPSAISS PSSKCTSDVT ITRTRKASSQ TARVSTQAVE TAARPATSSA HSTFTMPADG
FQPSNGTLPS ATGTASTATG TAPVASGTAP TASSILPTAT GALVEPWAAA AARGIPAASS
VLMAGFARTL TRTTASASSQ AVPALDDTID LLHAMLYGAN IEMVSVEAIR KANAQGKSLD
GLVCVFVGGT GGIGESTARE LFIRATRPRA VIVGRSEQKA AQLIEDLKEI NPEGEAYFLQ
KDVSLLRNVD ELCDELKRRE PKINCLFVTA GYMTLRGRNE TVEGLDRKMC VNYYSRIRCM
VNLIPCLKAA SDQGEISRAI SVLAAGSEGD VAIDDLDLRH NFTLHACLAH CAVMTDFAVE
ELARRYPFTS FSHSYPGTVK TGIANELTGP VRLAVKVMYA VMTPWILNVK ESGERHFFQM
TNKCYPAAQG GVGIEPPDDV SIMRGSNGQV GSGAYLIDWD GKPTGDENVL KRYRDLGMPQ
KVWEHTMAMF EQAERLNRKA AKRPASREAE GAGRPIPDPV GWRPA
//
