ID N1QJA2_SPHMS Unreviewed; 1330 AA.
AC N1QJA2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:EMF11875.1};
GN ORFNames=SEPMUDRAFT_67241 {ECO:0000313|EMBL:EMF11875.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11875.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11875.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11875.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KB456265; EMF11875.1; -; Genomic_DNA.
DR RefSeq; XP_016759996.1; XM_016909782.1.
DR STRING; 692275.N1QJA2; -.
DR GeneID; 27906919; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_261362_0_0_1; -.
DR OMA; ITSQTWD; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000016931; 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 GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
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; 3.30.2130.10; VC0802-like; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR027795; CASTOR_ACT_dom.
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 PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF55021; ACT-like; 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 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:UP000016931};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004110380"
FT DOMAIN 358..381
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 524..538
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 217..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 141696 MW; 3C9590D3A5B24B40 CRC64;
MKLLSLIPVL AYTPYTLGQV FSSYVDDNGI VLWQNTWDSQ VGAGNAQWGL ALPPVNASEY
MNEYIGRVVA PIPETGTWLG ISHSSGMTGS LILLTWVNGD QVMTGFRYAS GYVEPSVYTG
NASLSVISSF VNTTHYGLTY RCQDCWSWEQ DGVSGSQVPK TTSAAAQLLG WAQATTAPMT
PEDTDTGIVQ HAADGIMAAT VASARNAAYT SWVSLGTPTG SPPPSSPSNV TTITPPTGTN
TTIPTGGSNS TATPTASSTP SSSPACASNS TITSQTWDYI VVGAGAGGIP LADKLSESGA
SVLLVEKGPP SSGRWGGTLK PDWLVGTNLS RFDVPGLDNE IWRDSDGIAC TDVSVMAGCV
LGGGTAVNAG LWWKANPTDF DYNFPVGWKG ADMTEAVERV FDRIPFTDVP SQDGRIYQGE
GYDVVGGALA AAGWKNVTAG DVPGEKNLTF SRPNHMFAHG ERGGPMATYL VSASERSNFR
LVTNTSVARV LRNGATMTGI EVEAFLDGGI CGTINASNII LSAGAFGTPK ILFRSGIGPQ
DQLETVSAAE GDKMIDSSNW INLPVGHNLD DHTSTDIVIT HPNVTVYDFY GAYTDPIDAD
MELYLQGRSG ILAQSAPNLL AGFWQEIDGS DGITRQLQYT ARAESSHDVS SNHSISITQY
LGRGSTGRGV ASITAALNMV VSKVPFASSA EDVAAIKSGI ESVLSALSLD PSIQVVYPLL
SSNSNSNSSS SNNNTTTTTT IDSWLANYPL TTSSRSANHW MGTAKMGLDS GLVANGTAVV
DTDTKVYGTQ NLFVVDASVF PGMVSTNPSA MIVAVAEHAS ERILARGRDD KKKKKARALR
SPPTSRRRGS CSRPRSSGHT LRTIREEIVA AAATVINGIS FTCGRCRSIP NVDDDSDSGR
ILLRNPMGQP ISESTTLLNA NIGFLRTHLA IIHIPTSAYS LFLQPILALL LHNNSRDQDG
AVVPPHRPWN YWLPFVNLSI TPNECSIVCP REEAEALFQP LIASLSADLQ KHVSISTEDY
SAITIGGEGL EAGQRVLDLT SPLALAGIPI FFITSYYSDF ILVPFSSRLK VINALEERGF
VFEADSEDGE AGHMTNPASP LSPSHARQGS CSSSSNGSGI YHQHYHYHHQ SLMTPTTPPT
PPPTTISDLQ LKTFQILARN HISPSVDPSL QLITCAGLKD STPGSSTSNF TQGKLDVGIA
KCLTTTHPFP PKFFSLTLTD SESASFTLEK RLLENFFLGG EEILLGTQAP EQIPITLDLH
MLPVESTGIV CGVSSRLIEG MKGRLGREMF NMSYLSTSRA GHVIVYEDEL EDAMDALRGA
EELQLGKEER
//
