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Database: UniProt
Entry: C1GK70_PARBD
LinkDB: C1GK70_PARBD
Original site: C1GK70_PARBD 
ID   C1GK70_PARBD            Unreviewed;       424 AA.
AC   C1GK70;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=PADG_07656 {ECO:0000313|EMBL:EEH42836.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH42836.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH42836.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH42836.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR   EMBL; KN275968; EEH42836.1; -; Genomic_DNA.
DR   RefSeq; XP_010763094.1; XM_010764792.1.
DR   AlphaFoldDB; C1GK70; -.
DR   STRING; 502780.C1GK70; -.
DR   GeneID; 22586112; -.
DR   KEGG; pbn:PADG_07656; -.
DR   VEuPathDB; FungiDB:PADG_07656; -.
DR   eggNOG; KOG2015; Eukaryota.
DR   HOGENOM; CLU_013325_13_1_1; -.
DR   InParanoid; C1GK70; -.
DR   OMA; ATSCNPY; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000001628; 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:UP000001628};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          341..424
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
SQ   SEQUENCE   424 AA;  47406 MW;  38A66F08DC0AA7A8 CRC64;
     MSTSVNPPNR EAQRWKYLYR ILTLAGPFSD EDWVPGPETI AGLESSKILG AGGLGCEILK
     NLALSGFKDI HVIDMDTIDI SNLNRQFLFR QDDVGKPKAE VAAAFVERRV KGVKITPYVG
     RIQDKDQDYY MQFRIVVCGL DSVEARRWIN STLAEMVDTS NLESLKPLID GGTEGFKGQV
     RVIVPKLSSC IECQLDMHAP RAAVPLCTIA SIPRQPQHCI EWAHQIAWGE QRQGEEFDGD
     DMEHVTWIYN TALERAEKFN IPGVTFSMAQ GVVKNIIPAI ASTNAVIAAA CTSEALKIVT
     TCNPYLDNYM MYAGEEGVYT YTFTAEQKKD CFVCGSSAKP IIVDPESTLE EFIMSLGELP
     EAQLKSPSLR SAAMMLYQRA PRQLEEYTRP NLTRKLKELV NDGDEVAVSD PAYTIDFRFR
     MTFK
//
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