UBA1_DICDI
ID UBA1_DICDI Reviewed; 1017 AA.
AC Q55C16;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P22515};
DE AltName: Full=Ubiquitin-activating enzyme E1;
GN Name=uba1; Synonyms=uae1; ORFNames=DDB_G0270272;
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).
CC -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC cellular proteins for degradation through the ubiquitin-proteasome
CC system. Activates ubiquitin by first adenylating its C-terminal glycine
CC residue with ATP, and thereafter linking this residue to the side chain
CC of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free
CC AMP. {ECO:0000250|UniProtKB:P22515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22515};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P22515}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000250|UniProtKB:P22515}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72486.1; -; Genomic_DNA.
DR RefSeq; XP_646665.1; XM_641573.1.
DR AlphaFoldDB; Q55C16; -.
DR SMR; Q55C16; -.
DR STRING; 44689.DDB0220497; -.
DR PaxDb; Q55C16; -.
DR EnsemblProtists; EAL72486; EAL72486; DDB_G0270272.
DR GeneID; 8617637; -.
DR KEGG; ddi:DDB_G0270272; -.
DR dictyBase; DDB_G0270272; uae1.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; Q55C16; -.
DR OMA; CIREKCN; -.
DR PhylomeDB; Q55C16; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DDI-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q55C16; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
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:0004839; F:ubiquitin activating enzyme activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..1017
FT /note="Ubiquitin-like modifier-activating enzyme 1"
FT /id="PRO_0000328363"
FT REPEAT 26..163
FT /note="1-1"
FT REPEAT 419..571
FT /note="1-2"
FT REGION 26..571
FT /note="2 approximate repeats"
FT /evidence="ECO:0000250"
FT REGION 765..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 592
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 536..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
SQ SEQUENCE 1017 AA; 113745 MW; 3C11B193828731E1 CRC64;
MSKPMDVEQE PKIDDALYSR QLYALSHETM KKITSTSVLV VGLQGLGIEI VKDLSLAGVK
SVTLYDKELV EIKDLSSQFY FSPEQVGKVG RADACFQKVV DLNNYVRIDV HNGELSDEFL
KKFNVVVLAN QPLALQLKVN EFCHANKIHF ISVETRGVFG QLFNDFGEQF TITDTNGENP
NAYMISSISQ DKEGIVTVVE EQKLQLLDGD LVTFKEVNGM SALNDLPPQK IKTISPLTFS
IGDTTNLPPY TSGGYVTEVK QPKVVDFKPL KNILESGENI FITDDFKFTQ PTNLLAGFQA
IHKFAEKNKH MPRPHNKEDA NAVIEIAKGL LKKPDDELDE KMITQLSFGA QGDIVPMQAI
LGGITAQEVL KACSGKFTPI HQLAFFDSVE CLPEDLETLP EEEFQPIGSR YDGQIITFGK
TLQNKIENLN YFLVGAGAIG CEMLKNFAMM GLGAGPKGLV HVTDMDTIEK SNLNRQFLFR
SSDIQQLKSQ TAANAVRVMN PDLNVKAYSL RVGPDTESHY NEEFFNSLDG VCNALDNVEA
RLYMDSQCVY YGKPLLESGT LGTKGNTQVV VPHLTESYSS SRDPPEKGIP VCTLHNFPNA
IEHTIQWARD TFEGLFKNNA DNVNSYLTNP AYVQSLKTQN PFVRLETLAS IKASLMDRPL
DFNQCIAWAR LKFEEYFNNN IEQLLYNFPK DMVTTTGTPF WSGPKRAPTP LKFDVENPLH
LEFIVAAANL RAFNYGIKAE TNIEVIQKQA ANVIVPDFTP KKVKIQTSEN EPAPSSNTQQ
AGGDAEDDQC DTILSQLPQP SEMAGYKINS IQFEKDDDTN HHIDFITATS NLRATNYAIS
PADKHKTKGI AGKIIPALVT TTAVVAGFVC IELIKVIQNK ALEKYKSTFM NLGIPFFGFV
EPIAAPKNKI REGWTWTLWD RFDVDGDITL KEFLDLFEKK HGLDISMLSC KVTLLYALFT
DKKTKEERLK MKISQLYETL SKKPLPKDKK YLLLEICCND TETGDDVDVP SVRYKYN
