ID A1DEX0_NEOFI Unreviewed; 513 AA.
AC A1DEX0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=ThiF domain protein, putative {ECO:0000313|EMBL:EAW17927.1};
GN ORFNames=NFIA_078670 {ECO:0000313|EMBL:EAW17927.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW17927.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027696; EAW17927.1; -; Genomic_DNA.
DR RefSeq; XP_001259824.1; XM_001259823.1.
DR AlphaFoldDB; A1DEX0; -.
DR STRING; 331117.A1DEX0; -.
DR EnsemblFungi; EAW17927; EAW17927; NFIA_078670.
DR GeneID; 4586281; -.
DR KEGG; nfi:NFIA_078670; -.
DR VEuPathDB; FungiDB:NFIA_078670; -.
DR eggNOG; KOG2018; Eukaryota.
DR HOGENOM; CLU_013325_9_3_1; -.
DR OMA; SLNRHSC; -.
DR OrthoDB; 10004at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..364
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 513 AA; 56626 MW; 6F537327679FA18D CRC64;
MSSWLQRQVG QQQAQLAVTA VVSGAAVAGA IFGYQALRRK EAVQHLKASI PPIDERHHAE
KLTEYGTAAS STHLNKEDER SAALARRAQE GDYDDDLILE QLARNRVFLT DEGLAKLRSS
FIIVVGCGGV GSHAVASLAR SGVAKIRLID FDQVTLSSLN RHALATLADV GTPKVHCIKK
RLEQIVPWVK FDCRNELFGG SAAADLLAPW SWDDSDKGRK PDYVLDCIDN ITSKVELLHY
CHSNSIPVIS SMGAGCKSDP TRIMVGDISL STDDPLSRST RRRLKLLGVN SGIPVVFSTE
KPGPGKASLL PLAEEEFAKG QVGELGVLPD FRIRILPVLG TMPAVFGYTV ANHVICDISG
YPNDYNVGGK GREKLYDSII AFLQGLHERL ARAEAGQDLI GLRIPISKDD VGYLVEEIWR
GRSAISNLTN RLILVPWQRP ARGFLPDPEW EKEGQKFIPI DLKNLVCMTK EEGARHEREV
LRGGKDVTEV YDQKVLEKVK WHMAEVEVQE KFR
//
