ID   A0A168AWU9_CORDF        Unreviewed;      1336 AA.
AC   A0A168AWU9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NAD(P)-binding domain protein {ECO:0000313|EMBL:OAA69296.1};
GN   ORFNames=LEL_10172 {ECO:0000313|EMBL:OAA69296.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA69296.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA69296.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA69296.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:OAA69296.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AZHF01000011; OAA69296.1; -; Genomic_DNA.
DR   STRING; 1081108.A0A168AWU9; -.
DR   OrthoDB; 2729442at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR024983; CHAT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR   PANTHER; PTHR43639:SF1; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   Pfam; PF12770; CHAT; 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:UP000076881}.
FT   DOMAIN          1034..1330
FT                   /note="CHAT"
FT                   /evidence="ECO:0000259|Pfam:PF12770"
SQ   SEQUENCE   1336 AA;  146458 MW;  54F1F71214744DCD CRC64;
     MPDTLSLQNK VAIVTGSGRE NGIGAGIALA LARNGASVVV HFASDTSKTR AAQVCETLRR
     AGGQAIAVQA SLDTVEGAKL LVRKTLEGFN TEHIDILVNN AGVAYFCPIT EELNLEQLSN
     VFQINVLGPF YMVHAVLPHM PRGGRIINIS STNSRRGNVN ISTYAASKAA LDSLTWTWAG
     ELGRSRGITV NSIAPGPVLT DLYPKGHEQA LMETEIALTR AENRAGTTAD IGDAVLLIVN
     EKSRWITGQY ISGVLSIEFS RTVAVATELN LFLEAEFHRG MHACIHFVYN SKDATNRPRN
     TELGSEDLDD YPLPLLRKDA AVRLTTVVRR LLQHSNPHAA LSIFNVLTGW YELDEVDSKV
     LLQEILDHGV RDTLLAARVY IQNATAIAHR ATFEISNILI TEAKNAVAFL GQSEYASELR
     LLEAKMAFIA LGGLDALSGP LSSAVVEGEY VAMVRDFMLA AHYNLAAKAV TEYMACIDYV
     RQPTKVNEII ALSDLLGATS GNNAYLWTTR LIALGSAPLQ SQIALGRQSV WCQTYLEEYS
     YTGAWEIARR YALYYSMYYH KIGDWTQQLY WSMAAEEFEG RISNDPHTRM SGMYHIFTVM
     ILRLQNLSGG YEEYDMEEVR QFGIDGFEAC EQAGFQDLAR KFLDKLSNIG IVPEELLGAS
     QENMSLAVAP LGEPKNLDAS ELLALYIEQR DLLDRLLDYE CVDQAFELHD QLNAYMEPIF
     KVLRHGTDLK LRSGDYASIQ NAMDLRVAEG VLHIQTATYA QRDRAFTIAK TAAARCGENG
     QLQTQRVALL VAAQCAFKMK EPNWGKVVVD LLHQADDCMD VSRKHVTATS RLDSLDQKQH
     LVASYGRSDV YVFGYMVMTA LKDSNDILAV MNPEDNISSE DIWAWMQRGK GRSVVDLIYA
     GESLEPAQTP YASLTVANNV AGTKPLAGEV DIGIALHDVQ SMAADYAMSK TGSSMIMVDW
     FLTSSHIDII IIDAAGQVHI EILDFTLEDA MKSLMRKPFT LRGTEDVKAW KEAYLAQSEF
     LGDLLTVDAL SELDWLVEPL EKHSKPGDLL VLCPSGVMHG LPLHALSVAG QLLIERNPIV
     YTSSLSLLFN CYKSASKRET AASSSAVFGV YGKAGRDSGA KSAEEQKVEA TLESVASRLD
     TKVDYGVSPE QFIAKCKDQH IIHYHGHAIL GKTKSCRFGQ SLVLASSSHE SDLLHWDDAI
     DDSLLLSGSD ELGPASPSAR LSARDMITQL KLSAPHVTLM ACNSASQEFS AGDEPQGMIP
     VLLLCGATSV LGTLWPILSA DGRAFSESFY TAFGEAGSVV NLARAVQQSV LSMRATRPEP
     IHWAGFVLHG AWFHKC
//