ID   A0A395NMY5_TRIAR        Unreviewed;       873 AA.
AC   A0A395NMY5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=S-hydroxymethylglutathione dehydrogenase alcohol dehydrogenase {ECO:0000313|EMBL:RFU77284.1};
GN   ORFNames=TARUN_4960 {ECO:0000313|EMBL:RFU77284.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU77284.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU77284.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU77284.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:RFU77284.1}.
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DR   EMBL; PXOA01000290; RFU77284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NMY5; -.
DR   STRING; 490622.A0A395NMY5; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 1.
DR   Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G03930)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        801..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        842..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..185
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
SQ   SEQUENCE   873 AA;  97433 MW;  1C4CB487E8148FB5 CRC64;
     MATSKAAYVA EKVIGHDDNA ITQQDVSGYQ QTGEAGTKMK ALVWKGKQKV EIVDVPKPNL
     LEDTDVILKV TGSTVCGSDL HLYHGAVVQL ADGDILGHEF CGIVEQVGSA INKVQVGKRY
     VASFQIACGD CFFCKQKLSS QCEKTNANTA AKSLYGGRTA GIFGYSHLTG GFAGGQAEYV
     RVPLADVNLL EIPEGVSDEK ALYLSDVLCT SYHAVKDTAV YQGDEVAIFG AGPIGQMAGV
     FALGEGASKV IFVDTEPRLT FIREHFPAEH SDKLFFIDYK KLSHGITSKE TVVSMLKDMC
     GGRGPDVAIE CAAGEYAKGW MHWLEIAVGA ETDTSEIVNE MIEGVRNYGR CGITGVYVAY
     TNHFNIGSLM QRGIRLIGNG QAPVHKYWEE LLAKIQKGEL NPLQMVSHRV RLEDLDKVYA
     KFDAKEDSMQ KVFVETKFSL PKESESPEIT SHRPILAPNT AMNQPEVVNY DVLEAALQER
     EKWQGIWPAV RVVDFCKGQT IDRAFELAAE LETFLKEKSQ AQLRLILLEI RQVTPSSKSH
     RQGEIISAAV NPAMLRCLRE HAGLFNTFIE ATCGIGHWYS AKHMCYDNGC DDHRGGRAKF
     EMFYEYIPQE RSHSCTQLST DFKSTTYFCL SLPGSVLARL MRDVAANAQL ATRPFYLETL
     IADEAMRTWQ RDIALKRTEL KSLDKIIDHS EVNNRSINEL HALARQWHIL ARNLSDYAAL
     MKFFKSASQR YPSIGVYRLE EMAILNGTLE YLDSSCQSLN RLISDYSGRT KTRIDLLYHL
     ANQAESQSTR ELAELARQDS AAMLTIAAVT LLFLPGTFIA SILSTTIFNF ADGEMQVYKK
     WWIFPVTVVP FTILVFIVWF AWLGRKRRSA ERR
//