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Database: UniProt
Entry: UBA3_DICDI
LinkDB: UBA3_DICDI
Original site: UBA3_DICDI 
ID   UBA3_DICDI              Reviewed;         442 AA.
AC   Q54QG9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=NEDD8-activating enzyme E1 catalytic subunit;
DE            EC=6.2.1.64;
DE   AltName: Full=NEDD8-activating enzyme E1C;
DE   AltName: Full=Ubiquitin-activating enzyme E1C;
DE   AltName: Full=Ubiquitin-like modifier-activating enzyme 3;
DE            Short=Ubiquitin-activating enzyme 3;
GN   Name=uba3; Synonyms=ube1c; ORFNames=DDB_G0283891;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 103-115; 141-152 AND 275-283, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RA   Bienvenut W.V., Veltman D.M., Insall R.H.;
RL   Submitted (JAN-2010) to UniProtKB.
CC   -!- FUNCTION: Regulatory subunit of the dimeric uba3-nae1 E1 enzyme. E1
CC       activates nedd8 by first adenylating its C-terminal glycine residue
CC       with ATP, thereafter linking this residue to the side chain of the
CC       catalytic cysteine, yielding a nedd8-uba3 thioester and free AMP. E1
CC       finally transfers nedd8 to the catalytic cysteine of ube2m (By
CC       similarity). {ECO:0000250}.
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   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of uba3 and nae1. The complex binds nedd8 and
CC       ube2m.
CC   -!- MISCELLANEOUS: Arg-192 acts as a selectivity gate, preventing
CC       misactivation of ubiquitin by this nedd8-specific E1 complex.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Nae1 and uba3 correspond to the N-terminal and the C-
CC       terminal part of yeast uba3. In yeast the two subunits form a single
CC       polypeptide chain.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000057; EAL65560.1; -; Genomic_DNA.
DR   RefSeq; XP_638902.1; XM_633810.1.
DR   AlphaFoldDB; Q54QG9; -.
DR   SMR; Q54QG9; -.
DR   STRING; 44689.Q54QG9; -.
DR   PaxDb; 44689-DDB0238040; -.
DR   EnsemblProtists; EAL65560; EAL65560; DDB_G0283891.
DR   GeneID; 8624299; -.
DR   KEGG; ddi:DDB_G0283891; -.
DR   dictyBase; DDB_G0283891; ube1c.
DR   eggNOG; KOG2015; Eukaryota.
DR   HOGENOM; CLU_013325_13_1_1; -.
DR   InParanoid; Q54QG9; -.
DR   OMA; ATSCNPY; -.
DR   PhylomeDB; Q54QG9; -.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q54QG9; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; ISS:dictyBase.
DR   GO; GO:0045116; P:protein neddylation; ISS:dictyBase.
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   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..442
FT                   /note="NEDD8-activating enzyme E1 catalytic subunit"
FT                   /id="PRO_0000330897"
FT   ACT_SITE        218
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Determines specificity for NEDD8"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  49301 MW;  FE6DB36C4D358E33 CRC64;
     METMDTSVDL PGRWIDIEKI IKRTGPFASP SFEPDTKASP NIMNGLQNDF KVLVIGAGGL
     GCEILKNLAL SGFRNIDVID MDTIDISNLN RQFLFRRKDV GKSKAEVAAA FINSRITGCN
     VTPHKCRIQD KDEDYYRQFK IVIAGLDSIE ARRWINGLLV NLVVVNDSGD IEPDTIIPLV
     DGGTEGFKGQ ARVILPKISS CFECSLDAFP PQVSYAICTI ANTPRVPEHC IQWALLFGLQ
     DATLEKPFDP KQFDNDNPDH MNWLFECAKK RAEKFNINGV TYKLTQGVAK NIIPAIASTN
     AIIAAACCNE VFKFCTDSSG YLNNYMMYNG LNGVYTFTFE YEIKEGCAVC GTNLVTFEID
     KSNTLSTFLE KITTDSRFQF KKPSLRSNGR NLYMQGLLHQ STVPNLEKTL SELNVQEDDE
     ITITDPALPG NLAVRMRIKY TS
//
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