ID A0A1E3QL13_9ASCO Unreviewed; 434 AA.
AC A0A1E3QL13;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN ORFNames=BABINDRAFT_163397 {ECO:0000313|EMBL:ODQ77687.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ77687.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV454439; ODQ77687.1; -; Genomic_DNA.
DR RefSeq; XP_018983015.1; XM_019129892.1.
DR AlphaFoldDB; A0A1E3QL13; -.
DR STRING; 984486.A0A1E3QL13; -.
DR GeneID; 30147745; -.
DR OrthoDB; 10004at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00755; YgdL_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF2; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE 1-RELATED; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..434
FT /note="THIF-type NAD/FAD binding fold domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009134291"
FT DOMAIN 56..334
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 434 AA; 48423 MW; DB10D3C2E300D923 CRC64;
MGCHKKLYLL TLAAVVVTAG CVEAVHAYLR SQKKKPTPTK TKQTVHDEEL IREQLARNYT
FLSEKGMEKV RNQRVVVVGA GGVGSWVTTM LVRAGVLALR IIDFDQVSLS SLNRHSVATL
ADVGVSKVEI LKAHSLQVAP WCEIDAVNSL WTLPDAEKLI YGGDFNPTYV VDCIDNIDTK
VDLLAFCYRN KIPVVSSGGA GCKSDPTRIN IGDISSTEED PLCRSVRRRL KKMGINGGIP
VVFSAEKPDP RKAALLPLEE AEFENGPVEE LSALKNFRVR ILPVLGTMPG MFGLTIATHI
LTTIAGYPIE PIEGKNRIKV YDGILQSLAG QQTRVGENDQ RVPISIHDVQ YLVEEVWRGK
SPISNYSTRL TLCRWDPKKE PSYQNIVLMT KEEQKMHEQR VLNGGEPVEA VYDTKVLANV
RRRFAEEEYY SQYR
//
