ID   UBC8_SCHPO              Reviewed;         184 AA.
AC   Q9P7R4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 8;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 8;
DE   AltName: Full=Ubiquitin carrier protein 8;
DE   AltName: Full=Ubiquitin-protein ligase 8;
GN   Name=ubc8; ORFNames=SPBC211.07c;
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).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28263}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CU329671; CAB75415.1; -; Genomic_DNA.
DR   PIR; T50342; T50342.
DR   RefSeq; NP_596617.1; NM_001022538.2.
DR   AlphaFoldDB; Q9P7R4; -.
DR   SMR; Q9P7R4; -.
DR   BioGRID; 277261; 6.
DR   STRING; 284812.Q9P7R4; -.
DR   iPTMnet; Q9P7R4; -.
DR   MaxQB; Q9P7R4; -.
DR   PaxDb; 4896-SPBC211-07c-1; -.
DR   EnsemblFungi; SPBC211.07c.1; SPBC211.07c.1:pep; SPBC211.07c.
DR   GeneID; 2540738; -.
DR   KEGG; spo:SPBC211.07c; -.
DR   PomBase; SPBC211.07c; ubc8.
DR   VEuPathDB; FungiDB:SPBC211.07c; -.
DR   eggNOG; KOG0416; Eukaryota.
DR   HOGENOM; CLU_030988_7_1_1; -.
DR   InParanoid; Q9P7R4; -.
DR   OMA; SPSIGFC; -.
DR   PhylomeDB; Q9P7R4; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9P7R4; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:PomBase.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:PomBase.
DR   GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF128; UBIQUITIN-CONJUGATING ENZYME E2 H; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..184
FT                   /note="Ubiquitin-conjugating enzyme E2 8"
FT                   /id="PRO_0000310743"
FT   DOMAIN          3..148
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          154..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   184 AA;  20990 MW;  A07A925FD586B7B5 CRC64;
     MSSPRRRIET DVMKLLMSDY EVTLVNDNMQ EFYVRFHGPS ETPYSGGIWK VHVELPSEYP
     WKSPSIGFVN RIFHPNIDEL SGSVCLDVIN QTWSPMFDMI NIFEVFLPQL LRYPNASDPL
     NGEAAALLLR EPNTYYAKVR DYIARYANKE DADITLNDSS DDDTMSSIDT ESGDEIAGPM
     DSDF
//