ID A0A316UEF2_9BASI Unreviewed; 670 AA.
AC A0A316UEF2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN ORFNames=BCV69DRAFT_279520 {ECO:0000313|EMBL:PWN23590.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN23590.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN23590.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN23590.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819321; PWN23590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UEF2; -.
DR STRING; 1684307.A0A316UEF2; -.
DR OrthoDB; 5488891at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245942}.
FT DOMAIN 49..663
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 72199 MW; A2A467F78E48EA0D CRC64;
MSQDDQQQQP QLSALESDPQ AHDQADGIEA VGQIVEASRS RPDARTQRYD RQLRLWASSG
QASLESANVL LIGATHLGAQ VLKNLILPGI GSFTVLDGQK VGEYDVGNNF FVDPASEGQS
RAEEVTRNLA ELNPSVISKA RMADPSQLLE QDPSWFTSFS LIIAANQPVD VLRPLADLVW
GQDRGTCVPL MSVRGAGMAG EVRIQIKEMG VIETHPASTV DLRLTSPWPE LSAYASAYDI
EDRDAMAHSH IPFVIILLRA LENWKSQHGG SLPSPSSDRK PFTDTINAMR DPSNLDLENF
DEAVAALGQN LWRPVSAGRS IAEDIQALLD DSRCDTVTAK STNFWLLVRA LRSFVAATTT
ATPSGGGGLL PLAGSLPDFK ATSSGYVEIQ RLYKEKARKD LSGLKGHLRA VLEEVGLPAS
AIGDEEVESF AKHAGFLKFV KGKSFKESLE QPARETIAMA FMDPINPSTI QHHAAFLAVD
AFYGKQHRFP GSSKAFSDSI VGSSSHVRHS SNGSSEAESS GGSRIRSAPP RGFSEPEKKR
QRSNSPYTTS RESTAQDDDG DSQMKESVKV NGGDGEEGTV DFAADEEACL KEAQAVMSHL
AIEDEDQIEA VEDAVKEMVR SGHGDIASTA SLLGGVAAQE AIKIITKQYI PLEGTAVYDG
IKQAIGAFRL
//
