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 03-AUG-2022, entry version 115.
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 (Slime mold).
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.DDB0238040; -.
DR PaxDb; Q54QG9; -.
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; LENYMMY; -.
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:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; ISS:dictyBase.
DR Gene3D; 1.10.10.520; -; 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.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF6; PTHR10953:SF6; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; SSF69572; 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
