ID   UBC11_SCHPO             Reviewed;         176 AA.
AC   O00103;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-20 kDa;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase;
DE   AltName: Full=Ubiquitin carrier protein;
GN   Name=ubc11; Synonyms=ubcp4; ORFNames=SPCC1259.15c;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=97299689; PubMed=9154838;
RA   Osaka F., Seino H., Seno T., Yamao F.;
RT   "A ubiquitin-conjugating enzyme in fission yeast that is essential for
RT   the onset of anaphase in mitosis.";
RL   Mol. Cell. Biol. 17:3388-3397(1997).
RN   [2]
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).
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; D85545; BAA20375.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB38416.1; -; Genomic_DNA.
DR   PIR; T40902; T40902.
DR   RefSeq; NP_588069.1; -.
DR   HSSP; Q95044; 2E2C.
DR   GeneID; 2539190; -.
DR   KEGG; spo:SPCC1259.15c; -.
DR   NMPDR; fig|4896.1.peg.407; -.
DR   GeneDB_Spombe; SPCC1259.15c; -.
DR   OMA; O00103; WANQEEF.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002391-MON; -.
DR   BRENDA; 6.3.2.19; 653.
DR   ArrayExpress; O00103; -.
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; TAS:GeneDB_SPombe.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IMP:GeneDB_SPombe.
DR   GO; GO:0008054; P:cyclin catabolic process; IGI:GeneDB_SPombe.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:GeneDB_SPombe.
DR   GO; GO:0007091; P:mitotic metaphase/anaphase transition; IMP:GeneDB_SPombe.
DR   GO; GO:0016567; P:protein ubiquitination; TAS:GeneDB_SPombe.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:GeneDB_SPombe.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR015582; Ubiquitin-conj_enz_E2_H10.
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   PANTHER; PTHR11621:SF26; UbcH10; 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; Cell cycle; Cell division; Complete proteome; Ligase;
KW   Mitosis; Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    176       Ubiquitin-conjugating enzyme E2-20 kDa.
FT                                /FTId=PRO_0000082566.
FT   ACT_SITE    113    113       Glycyl thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   176 AA;  19664 MW;  6C80769C37AD4950 CRC64;
     MDSDMQNQNP HTNSKNSSSA GMAVDGHSVT KRLRSELMSL MMSNTPGISA FPDSDSNLLH
     WAGTITGPSD TYYEGLKFKI SMSFPANYPY SPPTIIFTSP MWHPNVDMSG NICLDILKDK
     WSAVYNVQTI LLSLQSLLGE PNNASPLNAQ AAELWSKDPI EYKRLLMQRY KEIDEI
//