ID   UBA1_YEAST              Reviewed;        1024 AA.
AC   P22515; D6VWZ3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   18-APR-2012, entry version 130.
DE   RecName: Full=Ubiquitin-activating enzyme E1 1;
GN   Name=UBA1; OrderedLocusNames=YKL210W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=91114708; PubMed=1989885;
RA   McGrath J.P., Jentsch S., Varshavsky A.;
RT   "UBA 1: an essential yeast gene encoding ubiquitin-activating
RT   enzyme.";
RL   EMBO J. 10:227-236(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=94255012; PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
RA   Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
RA   Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
RA   Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 940-1024.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=89330565; PubMed=2569166; DOI=10.1038/340400a0;
RA   McGrath J.P., Varshavsky A.;
RT   "The yeast STE6 gene encodes a homologue of the mammalian multidrug
RT   resistance P-glycoprotein.";
RL   Nature 340:400-404(1989).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-914, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC       glycine residue with ATP, and thereafter linking this residue to
CC       the side chain of a cysteine residue in E1, yielding an ubiquitin-
CC       E1 thioester and free AMP.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P61864:UBI1 (xeno); NbExp=2; IntAct=EBI-19703, EBI-19797;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC       allowing it to accommodate two ubiquitin moieties at a time, with
CC       a new ubiquitin forming an adenylate intermediate as the previous
CC       one is transferred to the thiol site.
CC   -!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
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DR   EMBL; X55386; CAA39056.1; -; Genomic_DNA.
DR   EMBL; Z28210; CAA82055.1; -; Genomic_DNA.
DR   EMBL; X15428; CAA33468.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08959.1; -; Genomic_DNA.
DR   PIR; S38048; S38048.
DR   RefSeq; NP_012712.1; NM_001179775.1.
DR   PDB; 3CMM; X-ray; 2.70 A; A/C=10-1024.
DR   PDBsum; 3CMM; -.
DR   ProteinModelPortal; P22515; -.
DR   SMR; P22515; 11-1024.
DR   DIP; DIP-4853N; -.
DR   IntAct; P22515; 45.
DR   MINT; MINT-489454; -.
DR   STRING; P22515; -.
DR   PeptideAtlas; P22515; -.
DR   EnsemblFungi; YKL210W; YKL210W; YKL210W.
DR   GeneID; 853670; -.
DR   KEGG; sce:YKL210W; -.
DR   CYGD; YKL210w; -.
DR   SGD; S000001693; UBA1.
DR   eggNOG; COG0476; -.
DR   GeneTree; ENSGT00390000016689; -.
DR   HOGENOM; HBG356508; -.
DR   KO; K03178; -.
DR   OMA; GMEGLNG; -.
DR   OrthoDB; EOG4NKG3P; -.
DR   PhylomeDB; P22515; -.
DR   EvolutionaryTrace; P22515; -.
DR   NextBio; 974614; -.
DR   ArrayExpress; P22515; -.
DR   Genevestigator; P22515; -.
DR   GermOnline; YKL210W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 4.
DR   Gene3D; G3DSA:1.10.3240.10; Ub-like_act_enz_cat_cys_dom; 1.
DR   InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_e1_C.
DR   InterPro; IPR023280; Ub-like_act_enz_cat_cys_dom.
DR   InterPro; IPR000127; UBact_repeat.
DR   InterPro; IPR019572; Ubiquitin-activating_enzyme.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_AS.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF09358; UBA_e1_C; 1.
DR   Pfam; PF10585; UBA_e1_thiolCys; 1.
DR   Pfam; PF02134; UBACT; 2.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; MoeB; 2.
DR   TIGRFAMs; TIGR01408; Ube1; 1.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN         1   1024       Ubiquitin-activating enzyme E1 1.
FT                                /FTId=PRO_0000194977.
FT   REPEAT       27    164       1-1.
FT   REPEAT      425    579       1-2.
FT   NP_BIND     444    473       ATP (By similarity).
FT   REGION       27    579       2 approximate repeats.
FT   ACT_SITE    600    600       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     914    914       Phosphoserine.
FT   CONFLICT    526    526       E -> K (in Ref. 1; CAA39056).
FT   CONFLICT    736    736       S -> N (in Ref. 1; CAA39056).
FT   HELIX        16     25
FT   HELIX        29     34
FT   STRAND       38     42
FT   HELIX        50     57
FT   STRAND       62     65
FT   HELIX        73     77
FT   HELIX        84     86
FT   HELIX        96     99
FT   STRAND      108    110
FT   HELIX       120    122
FT   STRAND      124    128
FT   HELIX       134    146
FT   STRAND      150    154
FT   STRAND      163    166
FT   STRAND      171    174
FT   STRAND      186    189
FT   STRAND      195    198
FT   STRAND      210    217
FT   HELIX       220    223
FT   STRAND      237    239
FT   STRAND      254    257
FT   STRAND      262    264
FT   HELIX       269    274
FT   HELIX       283    287
FT   HELIX       288    293
FT   HELIX       297    305
FT   HELIX       316    332
FT   HELIX       345    353
FT   TURN        363    365
FT   HELIX       370    378
FT   STRAND      387    389
FT   HELIX       394    396
FT   TURN        400    402
FT   TURN        407    410
FT   HELIX       418    421
FT   HELIX       427    433
FT   STRAND      437    440
FT   HELIX       448    455
FT   STRAND      466    469
FT   HELIX       476    478
FT   TURN        479    481
FT   HELIX       487    489
FT   HELIX       494    505
FT   HELIX       507    509
FT   STRAND      513    516
FT   TURN        523    527
FT   HELIX       530    535
FT   STRAND      537    541
FT   STRAND      544    546
FT   HELIX       547    559
FT   STRAND      563    565
FT   STRAND      576    578
FT   TURN        580    582
FT   HELIX       586    588
FT   HELIX       599    603
FT   HELIX       609    620
FT   HELIX       626    636
FT   HELIX       640    645
FT   HELIX       655    663
FT   HELIX       669    684
FT   HELIX       686    694
FT   HELIX       725    732
FT   HELIX       736    741
FT   HELIX       755    762
FT   HELIX       799    802
FT   HELIX       808    811
FT   HELIX       830    844
FT   HELIX       852    858
FT   HELIX       867    873
FT   HELIX       877    885
FT   HELIX       891    893
FT   TURN        901    904
FT   TURN        926    928
FT   STRAND      930    933
FT   HELIX       939    948
FT   STRAND      953    958
FT   STRAND      963    966
FT   HELIX       971    977
FT   HELIX       982    989
FT   STRAND      990    992
FT   STRAND     1000   1008
FT   STRAND     1019   1023
SQ   SEQUENCE   1024 AA;  114266 MW;  8910804DF9156661 CRC64;
     MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE IAKNVVLAGV
     KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA ELNAYVPVNV LDSLDDVTQL
     SQFQVVVATD TVSLEDKVKI NEFCHSSGIR FISSETRGLF GNTFVDLGDE FTVLDPTGEE
     PRTGMVSDIE PDGTVTMLDD NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI
     GSVKEYGEYK KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH
     QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE LSYQARGDIP
     GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP KNFPRNEKTT QPVNSRYDNQ
     IAVFGLDFQK KIANSKVFLV GSGAIGCEML KNWALLGLGS GSDGYIVVTD NDSIEKSNLN
     RQFLFRPKDV GKNKSEVAAE AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT
     NALDNVDART YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC
     TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD VKGVLESISD
     SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK TSNGEPFWSG AKRAPTPLEF
     DIYNNDHFHF VVAGASLRAY NYGIKSDDSN SKPNVDEYKS VIDHMIIPEF TPNANLKIQV
     NDDDPDPNAN AANGSDEIDQ LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC
     RAQNYFIETA DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN
     LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE GLEITMLSYG
     VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST MILEICADDK EGEDVEVPFI
     TIHL
//