ID F2TD03_AJEDA Unreviewed; 570 AA.
AC F2TD03;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN ORFNames=BDDG_04055 {ECO:0000313|EMBL:EGE81114.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE81114.1};
RN [1] {ECO:0000313|EMBL:EGE81114.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE81114.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
CC {ECO:0000256|PIRNR:PIRNR039099}.
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC ECO:0000256|PIRNR:PIRNR039099}.
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DR EMBL; GG749424; EGE81114.1; -; Genomic_DNA.
DR AlphaFoldDB; F2TD03; -.
DR HOGENOM; CLU_019618_1_0_1; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000007802; Unassembled WGS sequence.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01493; APPBP1_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR030667; APP-BP1.
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 PIRSF; PIRSF039099; APP-BP1; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 19..564
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 460..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63022 MW; EF53ACE7D702A37C CRC64;
MTESFPSSLA GLTSKERKYD RQLRLWAASG QKALENSKIL LINSDGPLDN EYPAVPGAVG
VETLKNLVLP GVGGFTIVDP AIVTESDLGV NFFLDEGSLG KSRAKETCKF LLELNPDVEG
DSLDKSIEEL LKEENFLKQY SLIVITAPMR RSMLKTISAA ARQRVIPLIY THSVGFYSGF
SLQLPTVYPI VETHPDPNSV QDLRLTNPFP ELVAATAKIA DLDSLDDHDH GHVPYLLLLL
HFLEKWKATH DGNLPLSYKD KSAFREMVRD GARTNNSTGG EENFDEAVAA VLKSINPWSL
KSNVREMFDM EQCNNLNPKS DNFWIIASAI KSFYTTHGVL PLPGSLPDMK AQSADYISLQ
NIYKSKALKD LEEVVGSVRA LEAQLRGESP QPPIPEKEIE TFCKHASSVK VIRGRDIPIL
DSNTDPTTLK AFRQAFQLPD SLMPIFLTLQ ILDTLVSEYR EKASEPQPEP PSSSSPPFLD
QADNWAAAQS KLFALLETDG YTLDDDVKLR IAKAVQETQR AGVGELHNIS SLTGGMVAQE
ALKVLTRQYV PLDNTCIFDG IGSRAEMFRL
//
