ID   UBC1_SCHPO              Reviewed;         217 AA.
AC   O74810;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 1;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase 1;
DE   AltName: Full=Ubiquitin carrier protein 1;
GN   Name=ubc1; ORFNames=SPBC2D10.20;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; CU329671; CAA21178.2; -; Genomic_DNA.
DR   PIR; T40123; T40123.
DR   RefSeq; NP_596239.1; -.
DR   HSSP; P21734; 1FZY.
DR   GeneID; 2540277; -.
DR   KEGG; spo:SPBC2D10.20; -.
DR   NMPDR; fig|4896.1.peg.2105; -.
DR   GeneDB_Spombe; SPBC2D10.20; -.
DR   OMA; O74810; LQSPEPN.
DR   BRENDA; 6.3.2.19; 653.
DR   ArrayExpress; O74810; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Nucleus; Ubl conjugation pathway.
FT   CHAIN         1    217       Ubiquitin-conjugating enzyme E2 1.
FT                                /FTId=PRO_0000310742.
FT   ACT_SITE     89     89       Glycyl thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   217 AA;  24507 MW;  4ACDEC0648676BE4 CRC64;
     MSDNRSRRIA KELADVQQDK QAGIQVWTIN DDISHLKGMF RGPEGTPYEG GYFVVDIEIP
     IDYPFRPPKM NFDTKIYHPN VSSQTGAICL DILKDQWSPV YTMKSALISL QSLLCTPEPS
     NPQDAQVAQV YLQNYQQFVR TAREWTSSYA AAPAGVDLDA ENTEFGGIDP NIITNLQQFG
     FSTELIVRVL QREHIKSQED LKDYPNGING ILDQLLH
//