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Database: UniProt
Entry: E3QAW1_COLGM
LinkDB: E3QAW1_COLGM
Original site: E3QAW1_COLGM 
ID   E3QAW1_COLGM            Unreviewed;       661 AA.
AC   E3QAW1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EFQ27999.1};
GN   ORFNames=GLRG_03143 {ECO:0000313|EMBL:EFQ27999.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; GG697339; EFQ27999.1; -; Genomic_DNA.
DR   RefSeq; XP_008092019.1; XM_008093828.1.
DR   AlphaFoldDB; E3QAW1; -.
DR   STRING; 645133.E3QAW1; -.
DR   EnsemblFungi; EFQ27999; EFQ27999; GLRG_03143.
DR   GeneID; 24408508; -.
DR   VEuPathDB; FungiDB:GLRG_03143; -.
DR   eggNOG; ENOG502QUV4; Eukaryota.
DR   HOGENOM; CLU_018354_4_2_1; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878:SF176; FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..661
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003180357"
FT   DOMAIN          193..372
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   661 AA;  71895 MW;  CE4A137006F57CFE CRC64;
     MPLMRSLLTA VLLSVGRLAV AQTLKVDGRE VAANASTVAP AAAVADAPAA AAAAGLFTEE
     NVQLTDAVLA NLTALELSNI SLFSFEDSYS VAKRSLFGRC KTYPGDFLYP TDLIWNIFDL
     LLGGALTKTV PEASVCYNDF GNFDKAKCDF LTANWVNGSY IHTEDPTAIN AVLFEGLSCM
     PPTINVGETD CKVGGLPSYV VEATQVAHIQ LAVNFARNLN LRLVVKNTGH DFGAKSTGAG
     SLSIWTHKLN NIQYLESYQQ DSYSGPALKL GSGVRAFEVY EAANKYGVTA VGGEGQTVGI
     IGGYVLGGGH SPMSGLWGMA ADSVLSFEVV TADGRFLTAS ESQNPDLFWA LRGGGGSTYG
     VVTSAVVKVF PKINITTMTF AFSTGANVTN DQFWAALRAY FDGFIEYAVD NANYEYFRIQ
     NLGTSLAFDM GPWWAPNMTE AQLRELTAPL FAKWAEIGVK VEPVYTEYDN FHDAWLTSFP
     LEPWGSNAIR QGSRLFPKAN WEDETKLNAT FEAIKSVVED GGLIIAFNIM AAPKTGFPDN
     AVNPAWREAV MHCIAAVLWD PTAEESVRKA ASDKLTFDWV QSWRDVSPGA GAYMSESDYI
     EPNFTQAFWG TKYEKALDLK KKYDPNDVFY AQNAVGSENW EMSEMILGNL PSQNSKLCRK
     Q
//
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