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Database: UniProt
Entry: U6L5E5_EIMTE
LinkDB: U6L5E5_EIMTE
Original site: U6L5E5_EIMTE 
ID   U6L5E5_EIMTE            Unreviewed;       169 AA.
AC   U6L5E5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase C-terminal domain-containing protein {ECO:0000259|Pfam:PF05199};
GN   ORFNames=ETH_00031410 {ECO:0000313|EMBL:CDJ42985.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42985.1};
RN   [1] {ECO:0000313|EMBL:CDJ42985.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ42985.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ42985.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ42985.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; HG675748; CDJ42985.1; -; Genomic_DNA.
DR   RefSeq; XP_013233735.1; XM_013378281.1.
DR   AlphaFoldDB; U6L5E5; -.
DR   EnsemblProtists; CDJ42985; CDJ42985; ETH_00031410.
DR   GeneID; 25255353; -.
DR   VEuPathDB; ToxoDB:ETH2_1578200; -.
DR   VEuPathDB; ToxoDB:ETH_00031410; -.
DR   OrthoDB; 3382025at2759; -.
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   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF227; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          96..141
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          16..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   169 AA;  17575 MW;  A43C16AEA1D1BCDA CRC64;
     MQLFTFTLYH PVGTCSMGQQ QQQQQQQQQQ QGRPTTANPT ATTNPTTTKT RSSNASSSSN
     ASSSSSSSSS SSSSSSSSSK SSSSSSSSSS SSSSWSSSAV VDGSLRVCGG LCVSNLIIAD
     ASVLPHLPSG NTHLPTLAAA HLAADTLRSS WQQQQQQQQQ QQQQQEARG
//
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