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Database: UniProt
Entry: N1QMA9_SPHMS
LinkDB: N1QMA9_SPHMS
Original site: N1QMA9_SPHMS 
ID   N1QMA9_SPHMS            Unreviewed;       356 AA.
AC   N1QMA9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:EMF16509.1};
GN   ORFNames=SEPMUDRAFT_55912 {ECO:0000313|EMBL:EMF16509.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16509.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF16509.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF16509.1,
RC   ECO:0000313|Proteomes:UP000016931};
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).
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC       {ECO:0000256|ARBA:ARBA00010928}.
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DR   EMBL; KB456260; EMF16509.1; -; Genomic_DNA.
DR   RefSeq; XP_016764630.1; XM_016909380.1.
DR   AlphaFoldDB; N1QMA9; -.
DR   STRING; 692275.N1QMA9; -.
DR   GeneID; 27906517; -.
DR   eggNOG; KOG2741; Eukaryota.
DR   HOGENOM; CLU_023194_0_0_1; -.
DR   OMA; QVHAVNI; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42840:SF3; BINDING ROSSMANN FOLD OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G10240)-RELATED; 1.
DR   PANTHER; PTHR42840; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          6..120
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          142..341
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   356 AA;  39669 MW;  978940F6E596C8CD CRC64;
     MVRKLQVGVS GLGRMGARHA LHFLDRTPRA ELVAAFDPDE KALAWARQRL KPYGTKLYSD
     YEAFLQHPGL EAVVVAGITT QHAAQTIRAI EADKHVLCEK PLSTSVKICE DVERIARAKP
     HLKVLCGFSR RFDGSYRDAA HRIKRGDIGR PAILRSQTCD KHRDDDYFVQ YAKFSGGIFV
     DANIHDIDLA LWYFGADSII KSVTAVGINA RLTDLSQHQD VDNGVGIVEF HNGKIAYFYA
     SRMMAAGQID TTEIIGTHGK IVVNGNPQKN LVEVHEANGI RREVPQTYYD RFEEAFVTES
     NEFTECVLDG KELPFGLSGA ITAVKIGDAL QKSLRTGRKL EFNELGEEIV EDKARL
//
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