ID A0A0P7B366_9HYPO Unreviewed; 360 AA.
AC A0A0P7B366;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPM40499.1};
GN ORFNames=AK830_g6041 {ECO:0000313|EMBL:KPM40499.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM40499.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM40499.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM40499.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:KPM40499.1}.
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DR EMBL; LKCW01000082; KPM40499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B366; -.
DR STRING; 78410.A0A0P7B366; -.
DR OrthoDB; 6845at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05339; 17beta-HSDXI-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322; PKSB; 1.
DR PANTHER; PTHR24322:SF736; RETINOL DEHYDROGENASE 10; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424}.
SQ SEQUENCE 360 AA; 39093 MW; B46820E5DD7E3328 CRC64;
MSSLLYSPAI DGLARLVRIV LSPLWSGPLL LAVEYAPSTV RHVLASIASK LPAQVSPSSL
DLSVARTALQ VLVALGMVRQ LNKSLNTMAS NSWRLTAAKG WDWPAEIAVV TGGSSGIGRD
IVERLAALGV RVAVLDVQQL PKDMEANQRV RFYRCDVTST ESVAEAADAV RRELGHPSIL
VNNAGITQPT PILKMPESFL RRIFGVNCMA LWFTTQQFLP RMIQLDKGHV VTVASIASFV
ALATAADYSA TKAGALAFHE SLASELKHFY KARNVLTTVV HPNFVKTPLV DDFAHRLERS
GVRFLTSDQI ASEVVAQIQS RRGGQLIIPR SAAGISAIRG WPTWLQELVR DTVGRASVQQ
//