ID   MUG30_SCHPO             Reviewed;         807 AA.
AC   O94275;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase mug30;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT-type E3 ubiquitin transferase mug30;
DE   AltName: Full=Meiotically up-regulated gene 30 protein;
GN   Name=mug30; ORFNames=SPBP8B7.27;
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 [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).
RN   [2]
RP   FUNCTION IN MEIOSIS.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [3]
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 fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase. Has a role in meiosis.
CC       {ECO:0000269|PubMed:16303567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Localizes
CC       to the barrier septum and the cell tip.
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DR   EMBL; CU329671; CAA21812.1; -; Genomic_DNA.
DR   PIR; T40821; T40821.
DR   RefSeq; NP_596534.1; NM_001022455.2.
DR   AlphaFoldDB; O94275; -.
DR   SMR; O94275; -.
DR   BioGRID; 277890; 24.
DR   STRING; 4896.SPBP8B7.27.1; -.
DR   PaxDb; O94275; -.
DR   EnsemblFungi; SPBP8B7.27.1; SPBP8B7.27.1:pep; SPBP8B7.27.
DR   GeneID; 2541379; -.
DR   KEGG; spo:SPBP8B7.27; -.
DR   PomBase; SPBP8B7.27; mug30.
DR   VEuPathDB; FungiDB:SPBP8B7.27; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   HOGENOM; CLU_002173_5_1_1; -.
DR   InParanoid; O94275; -.
DR   OMA; WFSSWKS; -.
DR   PhylomeDB; O94275; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O94275; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   CDD; cd00078; HECTc; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Meiosis; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..807
FT                   /note="Probable E3 ubiquitin-protein ligase mug30"
FT                   /id="PRO_0000300502"
FT   DOMAIN          453..807
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   ACT_SITE        775
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   807 AA;  93415 MW;  7203EB2667E2D3AB CRC64;
     MSRPIEIANV SSGNRRTLPA LHGSSFSSRS ELDNNTNSKI SRRLRELVCQ RMGENPLRLR
     QSFHETISND SYGNSEKLVI RPCICCNSVL RYPAQAMCFR CSLCMTVNDV YFCLSGSQIK
     TKASTDGSQF ISVEHFVETI HQTRSALQLA KQRTGNVQAI VAAGLPLREL ISLVFGSPPI
     LNKLFSVKNG CSIQSSGLNY KLIYQLYHDI TNLDILITNE LLRAIESLLR RPMLYCHDPA
     DYQYLLILLE NPLLNSKSKN IVNKSSSILK RILGVLSNLN EKTHHFFISC FKKQPYNNPK
     FFRRKVDLIN KFIGQRLMET YSRNKRKHYY NNDWQIKSAA ITMALLYSAN SQMRLIDRSS
     FYCIMADFIN LYHDFELWEQ KINCFCFCQY PFLLSMGAKI SILQLDARRK MEIKAREAFF
     SSILSKMNVE PYLMIRVRRD RLLEDSLRQI NDRNKDFRKA LKVEFLGEEG IDAGGLKREW
     LLLLTRKVFS PEFGLFVNCE ESSNYLWFNY SHRSKEIDYY HMSGILMGIA IHNSINLDVQ
     MPRAFYKKLL QLPLSFNDLD DFQPSLYRGL KELLLFEGDV KNTYGLNFTI NLKAVEGFRT
     VELKEGGSEL SVDNENRKEY VLRYVDYLLN TTVKKQFSAF FDGFMKVCGG NAISLFQDNE
     ISKLIRGSEE VIDWELLKNV CVYDFYDQNA ISNSISESEP SMTASKYLCH SFVSKRKIIL
     WFWDLISHYS LKMQKLFLIF VTGSDRIPAT GAHNFQLRIS VLGPDSDQLP ISHTCFNHLC
     IWEYSSREKL KKKLDTALLE TNGFNIR