ID A0A135SEX8_9PEZI Unreviewed; 956 AA.
AC A0A135SEX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KXH34456.1};
GN ORFNames=CSIM01_00367 {ECO:0000313|EMBL:KXH34456.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH34456.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH34456.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH34456.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) 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:KXH34456.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFBX01000586; KXH34456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135SEX8; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000070328; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR049326; Rhodopsin_dom_fungi.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-RELATED; 1.
DR Pfam; PF20684; Fung_rhodopsin; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 483..506
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 660..674
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 336..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 103136 MW; C5E036EF2A7B7495 CRC64;
MIGPGGDAPM ALAVLWGLTG LAFFFVLLRL YTRLFILQAY GVDDHFFNLA FFLFVAYDVM
LTISSFYGFG RNILELEMDN VPKAILYEAI GSTILVSAIV VSKASLALFL LRLVNTRLHQ
VLVIAPVVIL FLIALASLLV FWFSCTPINF LWDRLIPDGS CPIDPGPIST AAGAWSVVVD
FWYAVTPWAL LWNVQMPKRE KLLINLSMSL GVMLEWLEAN VHDSAGACGI LRALQLKNLS
SVNFTKDTVA LIIWHAAELA VTLVCIGIPV CRPLFKGWLS KWSSRNGSRP GPYTRDMTGS
NLGFGLKTIG GTDYTVRVGL KTPDLDLGSL AGRSGEGRFG SGTRSGGKGF GDNESVDSIL
GPDDRYGQGR NMDIERRYYV AEDDLVKVSS PLLVAGVHVD AKRSIPVKVR LCGGLAGSVI
SNRLLHNDPS LKILLVEAGP NVNGLESIAY PNTSTGAGSD IDWAYTSVPQ ANVDNRSIAA
PAGKALGGGT AINGAAWVRG HTVDYDLWAE EVGDDRWSYE GQLPYMKLTE KFFDASINPS
QHGENGSMII QGVTPMNRHF PMREKLAESL EALRVSALPQ LDANAGNPIG YGDLQENRVQ
GRRQLSSESF PLDGVTVITN TMVENILVSK SPNSTAITAK GIRLQNGTEY HSRKTILSAG
AYRTPQLLML SGIGPANVLT EHGIEVKLDQ PEVGQNMHDH ILMPTAWKVR NPSEGWAYES
DNPLFKEPQY GLGNKIDFLA TVTLPKEGLA AAIAEDEGVA PNPEHPLLRQ DRAHISHTLQ
YNGASTDGSA VLMLSIVLID TSRGSVGISS ANVTDPPVID PNYLSTAVDR YAVREALKFD
TRLLGSDLTP VGREILDGEL TADTPLTVDS PDEAFAARAR QVAGSCFHPS GTASMGKVVN
TDLSVKGVDG LFVADSSIFP VSISANLQVA MYAMALQAAE IIGEHGSKCR QVRATL
//