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Database: UniProt
Entry: T0KZD1_COLGC
LinkDB: T0KZD1_COLGC
Original site: T0KZD1_COLGC 
ID   T0KZD1_COLGC            Unreviewed;       574 AA.
AC   T0KZD1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EQB57534.1};
GN   ORFNames=CGLO_02323 {ECO:0000313|EMBL:EQB57534.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB57534.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:EQB57534.1}.
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DR   EMBL; AMYD01000476; EQB57534.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KZD1; -.
DR   STRING; 1237896.T0KZD1; -.
DR   eggNOG; ENOG502R8I5; Eukaryota.
DR   HOGENOM; CLU_018354_4_2_1; -.
DR   OMA; NITADGH; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000015530; 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; -; 2.
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; GULONOLACTONE OXIDASE; 1.
DR   PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 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:UP000015530};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..574
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013334291"
FT   DOMAIN          112..292
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   574 AA;  61421 MW;  E1E7F150F2B6CE51 CRC64;
     MKIIILFLLA STALAATYPR PAACRYISGD PGWPSSSLWN RLNATVGGRL LATNPLAHSC
     HDPTYSDDTC TSLRQQWGQP NLQIPYPAEF LSPWFQNQSC VPFTPRSSAC ELGNSASYSI
     NVTGPSDIIS GLKFAQQNNV RLVIKNTGHD QNGKGTGKGA LSLWTHNLKD KKFIPSYKSS
     YYKGPAVKLG AGVQGGEAAT FAHQNGGYRV VAGSCPTVGL VGGYTQGGGH SSLSGIYGLG
     ADNVLEWEVI TATGQHLTAT PEKNIDLYWA LSGGGPGTYG VVVSMTTRVF PDAPTGAASY
     SFSIASTGNK EDAYWNAVTT FHAQLPPLLD QGVYVTYSVT NNTFYIIAII APSHNQTELN
     ALMQPMLTAL SQQNGLSAQS LGLNTFGTSN VYDILATNVW PVLQDASLVA AQGGRLITRA
     NLNANLTGVM SAMRSITTGG TFYLACTAIN TTTAQGVPPI AKNAVLPAWR DTSLNCLVGT
     AWAWGQSWDP VPGWQKELLD RVLPTIEAVT PNSGAYLNEA NFAQRDWQGQ FYGKNYQKLV
     AIKKKYDPQD LFYAVSAVGS EVWAADGEGR LCRT
//
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