ID   A0A0L1JBE4_ASPNO        Unreviewed;       418 AA.
AC   A0A0L1JBE4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE            EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN   ORFNames=ANOM_002939 {ECO:0000313|EMBL:KNG89074.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89074.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG89074.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89074.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC       NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC         cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC         protein]-yl-L-cysteine.; EC=6.2.1.64;
CC         Evidence={ECO:0000256|ARBA:ARBA00024626,
CC         ECO:0000256|RuleBase:RU368009};
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC       {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC       subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC       ECO:0000256|RuleBase:RU368009}.
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:KNG89074.1}.
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DR   EMBL; JNOM01000039; KNG89074.1; -; Genomic_DNA.
DR   RefSeq; XP_015409997.1; XM_015548196.1.
DR   AlphaFoldDB; A0A0L1JBE4; -.
DR   STRING; 1509407.A0A0L1JBE4; -.
DR   GeneID; 26804743; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR   CDD; cd01488; Uba3_RUB; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR   Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR   InterPro; IPR014929; E2-binding.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR   InterPro; IPR030468; Uba3_N.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF08825; E2_bind; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM01181; E2_bind; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU368009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          335..418
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
SQ   SEQUENCE   418 AA;  46898 MW;  527DC5C1F384B13F CRC64;
     MASADSSLRW KHLHKVLTRP GPFSDEDWVP GPETIGALET SKILVIGAGG LGCEILKNLA
     LSGFKDIHVI DMGKSFPYHF FLFRQSDIGK PKAEVAAAFV ERRVKGVKIT PYVGKIQDKD
     EDYYMQFKIV VCGLDSIEAR RWINATLIGM VDPENPESLK PLIDGGTEGF KGQARVILPT
     LSSCIECQLD MHAPRPAVPL CTIATIPRQP QHCIEWAHQI AWQEKRKDDP FDSDDLDHIG
     WVYNAALERA KQFHIHGVTF QMTQGVVKNI IPAIASTNAV IAAATTSEAL KIATSCNPYL
     DNYMMYAGEE GVYTYTFEAE KKPDCPVCGN LARNMTVDPD MTLQEYIDTL GDLPEAQLKK
     PSMRTEEKTL YQRFPPQLEE QTRVNLNSKL RDLVEDGQEI AVSDPAYTID FRYRLLFK
//