ID A0A9W8GJ52_9FUNG Unreviewed; 663 AA.
AC A0A9W8GJ52;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=DM2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IWW39_003379 {ECO:0000313|EMBL:KAJ2686792.1};
OS Coemansia spiralis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=417178 {ECO:0000313|EMBL:KAJ2686792.1, ECO:0000313|Proteomes:UP001151516};
RN [1] {ECO:0000313|EMBL:KAJ2686792.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 109367 {ECO:0000313|EMBL:KAJ2686792.1};
RA Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA Smith M.E.;
RT "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT fungi.";
RL Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
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:KAJ2686792.1}.
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DR EMBL; JANBTX010000094; KAJ2686792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W8GJ52; -.
DR OrthoDB; 191139at2759; -.
DR Proteomes; UP001151516; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR43157:SF31; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS F PROTEIN; 1.
DR PANTHER; PTHR43157; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS F PROTEIN-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF02201; SWIB; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP001151516}.
FT DOMAIN 309..364
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 461..538
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT REGION 411..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..640
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 72201 MW; 9AC47425FA666DB8 CRC64;
MGFSPVDSKP EWVPRERQEG RRFIVTGANR GIGLATATGL AALGAHVVMV GHEGSDAFNE
AMDRIVMETG CTRDHLGYMS LDLRSLDSVR QFAKSWAQRP EPERSIQGLI NNAGIAGMPG
LSPDGFEMCF QINYLSMFLL TRLLLPYLAP AAGDSMVPRI VCVSSSAHLF TLGLPTDEKY
LRTSGGGFFS LRYGESKLCV NSFVRQLQAR LPADKAHVFA VHPGSTASSF WQSFPAWAQR
CIASVAQDPS RGARTSLFCA TEPDLVSGGY YADCAQASAS FWLGRADAAD LLWQKSCAWT
GLSPKSLITM DVTTFAPRIR EILQNSDLST VSAKKVRRQL EHVMRVSLDA YKGDIDEIIK
QQFQQIHTET QQRQAQQHQY AQQYAQQQGQ MGGVFGVSQA LPGLHIPSAG GVAGAASGSA
SSPLPGEAPR KRGRPRKPEN EKKQQRKKRV VDPNKPKRST GLSKPMKLSP DLSSFLGQKY
EARTEVVKSL WKYIKERDLQ DPIDKRYILC DDKLLVLFHE SRLYMYTMNK LLNEHFIKPT
PEENAEAIAL LGLPPSQSAD GADVAAPTSV KAEGSTHSPA PSDGDTQHTG DEDEEDEEEE
EEDDDEHDVK EEAQPTSAST AVDSKPSLPK SLSPPAAISS GTSAPLVLPP MPSNINGAGS
SGI
//
