UBA1_CANAW
ID UBA1_CANAW Reviewed; 1021 AA.
AC P52495; C4YP25;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ubiquitin-activating enzyme E1 1;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P22515};
GN Name=UBA1; ORFNames=CAWG_02960;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 817-1021.
RC STRAIN=WO-1;
RX PubMed=9489670; DOI=10.1046/j.1365-2958.1998.00704.x;
RA Raymond M., Dignard D., Alarco A.-M., Mainville N., Magee B.B.,
RA Thomas D.Y.;
RT "A Ste6p/P-glycoprotein homologue from the asexual yeast Candida albicans
RT transports the a-factor mating pheromone in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 27:587-598(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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; CM000310; EEQ44684.1; -; Genomic_DNA.
DR EMBL; U13193; AAC49911.1; -; Genomic_DNA.
DR PIR; T18215; T18215.
DR AlphaFoldDB; P52495; -.
DR SMR; P52495; -.
DR STRING; 5476.P52495; -.
DR PRIDE; P52495; -.
DR EnsemblFungi; EEQ44684; EEQ44684; CAWG_02960.
DR VEuPathDB; FungiDB:CAWG_02960; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OMA; GANLHAF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001429; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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; 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; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Nucleus;
KW Ubl conjugation pathway.
FT CHAIN 1..1021
FT /note="Ubiquitin-activating enzyme E1 1"
FT /id="PRO_0000194978"
FT ACT_SITE 598
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 542..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
SQ SEQUENCE 1021 AA; 114271 MW; F6C6CD1C01489D98 CRC64;
MSDNMQIDSP SPQEIDEGLY SRQLYVLGKE AMLKMQNANV LIIGLNGLGI EIAKNIALAG
VKSLSLYDPK PVSITDLSTQ FFLSESEIGQ PRDVASREKL AELNSYVPIN VVDNIDEETL
LKFKCIVSTN ISLEEQVKIN NITHANNIGY INADIKGLFG QIFVDFGDKF TVIDQTGEEP
LSGIVSDIEK NGTVTMLDDN RHGLQDGDYV KFAEVEGMPK LNEGNPHKVE VLGPYAFKIK
IDESYGEYVK GGLYTQVKVP KDLSFEPLTK QLAAPEYLIS DFAKFDKPAQ LHLGFQALHA
FQTKHQGELP APYNEQDATE AFRYAEELAT QNPSILGEDK LDEKYLKELF YQARGDIPGV
VAFYGGLIAQ EVLKNCSSKF TPIKQWLYFD SLESLPSETE YPRNEENNKP IGSRYDGQIA
VFGKAFQEKI ANLKVFLVGS GAIGCEMLKN WAMMGLGSGP EGKIFITDND SIEKSNLNRQ
FLFRPKDVGK NKSDVAALAV QQMNPDLKGK IDSKLDKVGP ETEDIFDDKF WTQLNIVVNA
LDNVEARTYV DRRCVFYKKP LLESGTLGTK GNTQVVIPNL TESYSSSQDP PEKSIPLCTL
RSFPNKIDHT IAWAKSLFQG YFAESPESVN LYLSQPNYVE QTLKQNPDIK GTLENISKYL
NNRPYTFEDC IKWARQEFET KFNHDIQQLL YNFPPDAKTS TGAPFWSGPK RAPKPLEFDI
NNKDHLDFII GGANLLAFIY GLKEPNATVD DFKKVLEQVI IEPFQPKSGV EIAATDAEAE
EQANNLSGSI DDEQIRKIAA SLPEPSTLAG YRLTPIEFEK DDDTNHHIEF ITAASNCRAL
NYGIEIADAH KTKFIAGKII PAIATTTALV TGLVCLELYK VVDGKDDIEQ YKNGFINLAL
PFIGFSEPIK SPEGKYNNKK FDQIWDRFEL NGDITLQELL DHFEKEEGLT ISMLSYGVSL
LYASFFPPKK VKDRLGLKLT SLIKEVSKKE VPSHVKNLIF EICCDDEEGE DVEVPYICVK
L
