ID   UBC6_SCHPO              Reviewed;         227 AA.
AC   O42646; P78897; Q1L844;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 6;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 6;
DE   AltName: Full=Ubiquitin carrier protein 6;
DE   AltName: Full=Ubiquitin-protein ligase 6;
GN   Name=ubc6; ORFNames=SPAC10F6.05c;
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 [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-227.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Functions in degradation of misfolded or regulated proteins
CC       localized in the endoplasmic reticulum (ER) lumen or membrane via the
CC       ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the
CC       doa10 ubiquitin ligase complex, which is part of the ERAD-C pathway
CC       responsible for the rapid degradation of membrane proteins with
CC       misfolded cytoplasmic domains. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q5VVX9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CU329670; CAA15718.1; -; Genomic_DNA.
DR   EMBL; D89248; BAA13909.1; -; mRNA.
DR   PIR; T37499; T37499.
DR   PIR; T43159; T43159.
DR   RefSeq; NP_593256.1; NM_001018653.2.
DR   AlphaFoldDB; O42646; -.
DR   SMR; O42646; -.
DR   BioGRID; 278138; 51.
DR   STRING; 284812.O42646; -.
DR   MaxQB; O42646; -.
DR   PaxDb; 4896-SPAC10F6-05c-1; -.
DR   EnsemblFungi; SPAC10F6.05c.1; SPAC10F6.05c.1:pep; SPAC10F6.05c.
DR   GeneID; 2541642; -.
DR   KEGG; spo:SPAC10F6.05c; -.
DR   PomBase; SPAC10F6.05c; ubc6.
DR   VEuPathDB; FungiDB:SPAC10F6.05c; -.
DR   eggNOG; KOG0894; Eukaryota.
DR   HOGENOM; CLU_041481_1_0_1; -.
DR   InParanoid; O42646; -.
DR   OMA; AWNVSTI; -.
DR   PhylomeDB; O42646; -.
DR   Reactome; R-SPO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O42646; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; 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:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway.
FT   CHAIN           1..227
FT                   /note="Ubiquitin-conjugating enzyme E2 6"
FT                   /id="PRO_0000082551"
FT   TOPO_DOM        1..206
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..163
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        87
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   CONFLICT        22
FT                   /note="V -> F (in Ref. 2; BAA13909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   227 AA;  25659 MW;  58BE058326D843AC CRC64;
     MASKGAYKRL MKEYLALQKN PVELVDAKPA TENILEWHYI ITGPPDTPYE GGQYHGTLIF
     PPDYPFKPPA IRMITPSGRF QTNTRLCLSF SDFHPKSWNP SWMVSTILVG LVSFMTSDEI
     TTGGIVTSES TRRTYAKDTK RFNIMDNPKF LIMFPELIDK NREDIAKAAA EAALIEPQQI
     HSTPVSSNEC KKNEPFNSKQ SWVKSRWSIA VLVFFALALA RFFGADS
//