ID   MMS2_SCHPO              Reviewed;         139 AA.
AC   O74983;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Ubiquitin-conjugating enzyme spm2;
DE   AltName: Full=Ubiquitin-conjugating enzyme variant MMS2 homolog;
DE            Short=UEV MMS2;
GN   Name=spm2; ORFNames=SPCC338.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH UBC13.
RX   PubMed=12531016; DOI=10.1016/s1568-7864(02)00111-8;
RA   Brown M., Zhu Y., Hemmingsen S.M., Xiao W.;
RT   "Structural and functional conservation of error-free DNA postreplication
RT   repair in Schizosaccharomyces pombe.";
RL   DNA Repair 1:869-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Has a role in the DNA error-free postreplication repair (PRR)
CC       pathway. Lacks catalytic activity by itself. The ubc13/spm2 heterodimer
CC       catalyzes the synthesis of non-canonical poly-ubiquitin chains that are
CC       linked through 'Lys-63'. {ECO:0000269|PubMed:12531016}.
CC   -!- SUBUNIT: Heterodimer with ubc13.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AF470233; AAL79845.1; -; mRNA.
DR   EMBL; CU329672; CAA19336.1; -; Genomic_DNA.
DR   PIR; T41737; T41737.
DR   RefSeq; NP_588162.1; NM_001023151.2.
DR   AlphaFoldDB; O74983; -.
DR   SMR; O74983; -.
DR   BioGRID; 275304; 9.
DR   STRING; 4896.SPCC338.05c.1; -.
DR   MaxQB; O74983; -.
DR   PaxDb; O74983; -.
DR   EnsemblFungi; SPCC338.05c.1; SPCC338.05c.1:pep; SPCC338.05c.
DR   GeneID; 2538720; -.
DR   KEGG; spo:SPCC338.05c; -.
DR   PomBase; SPCC338.05c; -.
DR   VEuPathDB; FungiDB:SPCC338.05c; -.
DR   eggNOG; KOG0896; Eukaryota.
DR   HOGENOM; CLU_063065_4_0_1; -.
DR   InParanoid; O74983; -.
DR   OMA; NLPCVDQ; -.
DR   PhylomeDB; O74983; -.
DR   Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-SPO-9020702; Interleukin-1 signaling.
DR   Reactome; R-SPO-9646399; Aggrephagy.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O74983; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:PomBase.
DR   GO; GO:0006301; P:postreplication repair; IMP:PomBase.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:PomBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   Ligase; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..139
FT                   /note="Ubiquitin-conjugating enzyme spm2"
FT                   /id="PRO_0000082599"
FT   DOMAIN          5..139
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   139 AA;  15555 MW;  BB247264D23F9BB2 CRC64;
     MAKVPRNFKL LEELEKGEKG LGESSCSYGL TNADDITLSD WNATILGPAH SVHENRIYSL
     KIHCDANYPD APPIVTFVSR INLPGVDGET GKVNPHKIDC LRHWKREYSM ETVLLDLKKE
     MASSSNRKLP QPPEGSTFF