ID M2SKS0_COCH5 Unreviewed; 511 AA.
AC M2SKS0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=COCHEDRAFT_1117319 {ECO:0000313|EMBL:EMD85895.1},
GN COCHEDRAFT_74431 {ECO:0000313|EMBL:EMD93866.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD85895.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD85895.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 {ECO:0000313|EMBL:EMD85895.1}, and C5 / ATCC 48332 / race O
RC {ECO:0000313|Proteomes:UP000016936};
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).
RN [2] {ECO:0000313|EMBL:EMD85895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C5 {ECO:0000313|EMBL:EMD85895.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Dhillon B.,
RA Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S., LaButti K., Han J.,
RA Copeland A., Lindquist E., Lucas S., Barry K., Schmutz J., Baker S.,
RA Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite and effector coding
RT capacity across Cochliobolus pathogens.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KB445586; EMD85895.1; -; Genomic_DNA.
DR EMBL; KB445573; EMD93866.1; -; Genomic_DNA.
DR AlphaFoldDB; M2SKS0; -.
DR STRING; 701091.M2SKS0; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_2_1; -.
DR OMA; STNCWLQ; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF27; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000016936}.
FT DOMAIN 81..253
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 511 AA; 55351 MW; AD494A1CA19F89EC CRC64;
MGVNGLQTRT TTAAGFASFG QQIGLSESTI KTLGEKFAQV SSPAEALAVA CQTARESLGE
AQVQATPVDQ TVVEVNWSET CYAFPSCVIQ PRNATDVSTA IQIVKFFQVK FSVRSGGHSP
NPGWSSIGSE GILLDLQRLD FVTLSGNGTV ASLGPGGRWS NAMTVLNAQG VSVQGGRLGQ
VGVGGLLLGG GYFYTSGQFG LAVDNVKNFE VVLSNGTIIN ASFSQNTDLF WALKGGGPNF
GIVTRFDLYT IPVLEIWGKV QIYSTDMAFK LLEAFDEWQQ NGASDTKSSV AFEIGLDYIT
LGLIYSEPTT SPTAFAAFED IEPLQVVVPP INTTFSNVYN ILSASYPNIT ARHDYRGASS
RINTEFTKEM YAFWRENAVA LRNKTGASQT FAMQHIGANL IQQGIDKGGN ALGIEAGAQQ
WWTTLVDWEN EGDDNLVRSV SINFTEQWKR RGQELGVYLP FEYMNDASRD QNPIGSYGSE
NVASLVKVSQ KYDAEQVFQT LQNSGFLLSK L
//
