ID F2SKN8_TRIRC Unreviewed; 375 AA.
AC F2SKN8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Alcohol dehydrogenase-like N-terminal domain-containing protein {ECO:0000259|Pfam:PF08240};
GN ORFNames=TERG_02757 {ECO:0000313|EMBL:EGD86496.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD86496.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; GG700650; EGD86496.1; -; Genomic_DNA.
DR RefSeq; XP_003235701.1; XM_003235653.1.
DR AlphaFoldDB; F2SKN8; -.
DR STRING; 559305.F2SKN8; -.
DR GeneID; 10373296; -.
DR VEuPathDB; FungiDB:TERG_02757; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; F2SKN8; -.
DR OMA; FARNEHK; -.
DR OrthoDB; 820313at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF18; NADP-DEPENDENT ALCOHOL DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_6G00510); 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 32..133
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 40736 MW; 9B528DF8881895C8 CRC64;
MTQEEGYEFT TFRGSDAGVV ASKTKRAPLT SNQVLISITH SGLCGTDQHY RKAGCVLGHE
GIGVVQALGP DVRTLRIGQR VGWGYVHGTC YKCRQCLEGY DQFCSARQVY GVTNLDQGSM
GYAAIWPESS LYAIPDKLSS LDAAPMMCAG ASIFGIYEQC GIKPNDRVGI IGLGGLGHMA
LIFGAKLGLE TVVFTHSVAK QVDAIVMGAT EFIPLEDLPR IISARRKRRD SDSGIDDQER
NSIDDGSEGD AGNIRPLDHL IVTTTENVDW PTFFELMAPR GTVHMLAGNI KDNLVVPSAA
LIDSGLRVFG SLVAPRSVMI RMLDFAARSR VKPIVQKFPL TADGVNTAFQ KLDEGTIRYR
GVLETPRDCL YKVSQ
//
