ID   UBA2_YEAST              Reviewed;         636 AA.
AC   P52488; D6VT24;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 215.
DE   RecName: Full=Ubiquitin-activating enzyme E1-like;
DE   AltName: Full=Polymerase-interacting protein 2;
DE   AltName: Full=SMT3-activating enzyme subunit 2;
GN   Name=UBA2; Synonyms=PIP2, UAL1; OrderedLocusNames=YDR390C;
GN   ORFNames=D9509.10;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7629121; DOI=10.1074/jbc.270.30.18099;
RA   Dohmen R.J., Stappen R., McGrath J.P., Forrova H., Kolarov J., Goffeau A.,
RA   Varshavsky A.;
RT   "An essential yeast gene encoding a homolog of ubiquitin-activating
RT   enzyme.";
RL   J. Biol. Chem. 270:18099-18109(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kolarov J.;
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 200060 / W303;
RA   del Olmo M., Gross S., Moore C.L.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   FUNCTION.
RX   PubMed=9312010; DOI=10.1093/emboj/16.18.5509;
RA   Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.;
RT   "The ubiquitin-like protein Smt3p is activated for conjugation to other
RT   proteins by an Aos1p/Uba2p heterodimer.";
RL   EMBO J. 16:5509-5519(1997).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-
CC       dependent activation of SMT3 and formation of a thioester with a
CC       conserved cysteine residue on AOS1. {ECO:0000269|PubMed:9312010}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Heterodimer of UBA2 and AOS1. The complex binds SMT3.
CC   -!- INTERACTION:
CC       P52488; Q06624: AOS1; NbExp=4; IntAct=EBI-19710, EBI-15107;
CC       P52488; Q12306: SMT3; NbExp=2; IntAct=EBI-19710, EBI-17490;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Multiubiquitinated in vivo.
CC   -!- MISCELLANEOUS: Present with 18800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA82980.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z48725; CAA88617.1; -; Genomic_DNA.
DR   EMBL; Z30326; CAA82980.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U17263; AAB46626.1; -; Genomic_DNA.
DR   EMBL; U32274; AAB64832.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12234.1; -; Genomic_DNA.
DR   PIR; A57178; A57178.
DR   RefSeq; NP_010678.3; NM_001180698.3.
DR   PDB; 3ONG; X-ray; 2.30 A; A/C=439-563.
DR   PDB; 3ONH; X-ray; 1.60 A; A=439-563.
DR   AlphaFoldDB; P52488; -.
DR   SMR; P52488; -.
DR   BioGRID; 32451; 38.
DR   ComplexPortal; CPX-3238; SUMO activating enzyme complex.
DR   DIP; DIP-2296N; -.
DR   FunCoup; P52488; 2486.
DR   IntAct; P52488; 10.
DR   MINT; P52488; -.
DR   STRING; 4932.YDR390C; -.
DR   iPTMnet; P52488; -.
DR   PaxDb; 4932-YDR390C; -.
DR   PeptideAtlas; P52488; -.
DR   TopDownProteomics; P52488; -.
DR   EnsemblFungi; YDR390C_mRNA; YDR390C; YDR390C.
DR   GeneID; 851998; -.
DR   KEGG; sce:YDR390C; -.
DR   AGR; SGD:S000002798; -.
DR   SGD; S000002798; UBA2.
DR   VEuPathDB; FungiDB:YDR390C; -.
DR   eggNOG; KOG2013; Eukaryota.
DR   HOGENOM; CLU_013325_7_3_1; -.
DR   InParanoid; P52488; -.
DR   OMA; PGKTECF; -.
DR   OrthoDB; 10255449at2759; -.
DR   BioCyc; YEAST:G3O-29938-MONOMER; -.
DR   BRENDA; 6.2.1.45; 984.
DR   Reactome; R-SCE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-SCE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 851998; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P52488; -.
DR   PRO; PR:P52488; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P52488; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; IPI:ComplexPortal.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR   CDD; cd01489; Uba2_SUMO; 1.
DR   FunFam; 1.10.10.520:FF:000005; Ubiquitin-activating enzyme E1-like; 1.
DR   FunFam; 3.50.50.80:FF:000004; Ubiquitin-activating enzyme E1-like; 1.
DR   Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR   InterPro; IPR030661; Uba2.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PIRSF; PIRSF039133; SUMO_E1B; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
DR   PDBsum; 3ONG; -.
DR   PDBsum; 3ONH; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc.
FT   CHAIN           1..636
FT                   /note="Ubiquitin-activating enzyme E1-like"
FT                   /id="PRO_0000194979"
FT   REGION          581..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           619..622
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        586..595
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        177
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT   BINDING         28..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         177
FT                   /note="C->A,S: Loss of function."
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   HELIX           450..455
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   HELIX           458..469
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          473..479
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   TURN            480..483
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          484..488
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   TURN            493..496
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   TURN            499..503
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          509..515
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          518..522
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          525..531
FT                   /evidence="ECO:0007829|PDB:3ONH"
FT   STRAND          535..538
FT                   /evidence="ECO:0007829|PDB:3ONG"
FT   STRAND          549..551
FT                   /evidence="ECO:0007829|PDB:3ONH"
SQ   SEQUENCE   636 AA;  71259 MW;  DBF800E1458B3B10 CRC64;
     MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI VDLDTIDLSN
     LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM DISTFPLHWF EQFDIIFNAL
     DNLAARRYVN KISQFLSLPL IESGTAGFDG YMQPIIPGKT ECFECTKKET PKTFPVCTIR
     STPSQPIHCI VWAKNFLFNQ LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK
     IIISRDASRI PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV
     GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH IFNIPMKSVF
     DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT TKYTDLNMAF TAKASNLSQN
     RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS DCLNKMKLSD FVVLIREKYS YPQDISLLDA
     SNQRLLFDYD FEDLNDRTLS EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC
     SLPDVEVPLI KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI
     NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD
//