ID   UBC7_SCHPO              Reviewed;         166 AA.
AC   O00102; Q9HDP3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 7;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=ubc7; Synonyms=ubcp3; ORFNames=SPBP16F5.04;
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].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9154838; DOI=10.1128/mcb.17.6.3388;
RA   Osaka F., Seino H., Seno T., Yamao F.;
RT   "A ubiquitin-conjugating enzyme in fission yeast that is essential for the
RT   onset of anaphase in mitosis.";
RL   Mol. Cell. Biol. 17:3388-3397(1997).
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).
RN   [3]
RP   FUNCTION.
RX   PubMed=12456009; DOI=10.1128/ec.1.4.613-625.2002;
RA   Nielsen I.S., Nielsen O., Murray J.M., Thon G.;
RT   "The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6
RT   affect transcriptional silencing of the mating-type region.";
RL   Eukaryot. Cell 1:613-625(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=19520858; DOI=10.1074/jbc.m109.002436;
RA   Hughes B.T., Nwosu C.C., Espenshade P.J.;
RT   "Degradation of sterol regulatory element-binding protein precursor
RT   requires the endoplasmic reticulum-associated degradation components Ubc7
RT   and Hrd1 in fission yeast.";
RL   J. Biol. Chem. 284:20512-20521(2009).
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, and of the hrd1 ubiquitin ligase
CC       complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC       for the rapid degradation of soluble lumenal and membrane proteins with
CC       misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC       misfolded transmembrane domains (ERAD-M) (By similarity). Together with
CC       hrd1, required for the degradation of the transcription factor sre1
CC       precursor in the absence of its binding partner scp1. Has a role in the
CC       formation of chromatin structures that influence the localization of
CC       transcriptional silencing factors. {ECO:0000255|PROSITE-
CC       ProRule:PRU00388, ECO:0000269|PubMed:12456009,
CC       ECO:0000269|PubMed:19520858}.
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   -!- PTM: Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked
CC       polyubiquitination, which leads to proteasome-dependent protein
CC       degradation. {ECO:0000250|UniProtKB:Q02159}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; D85544; BAA20373.1; -; mRNA.
DR   EMBL; CU329671; CAC08543.1; -; Genomic_DNA.
DR   PIR; T43235; T43235.
DR   RefSeq; NP_595778.1; NM_001021678.2.
DR   PDB; 6OP8; X-ray; 1.70 A; A=1-166.
DR   PDBsum; 6OP8; -.
DR   AlphaFoldDB; O00102; -.
DR   SMR; O00102; -.
DR   BioGRID; 277766; 2.
DR   STRING; 284812.O00102; -.
DR   MaxQB; O00102; -.
DR   PaxDb; 4896-SPBP16F5-04-1; -.
DR   EnsemblFungi; SPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
DR   GeneID; 2541252; -.
DR   KEGG; spo:SPBP16F5.04; -.
DR   PomBase; SPBP16F5.04; ubc7.
DR   VEuPathDB; FungiDB:SPBP16F5.04; -.
DR   eggNOG; KOG0426; Eukaryota.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; O00102; -.
DR   OMA; NIDACKM; -.
DR   PhylomeDB; O00102; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O00102; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:PomBase.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:PomBase.
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; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW   Thioester bond; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..166
FT                   /note="Ubiquitin-conjugating enzyme E2-18 kDa"
FT                   /id="PRO_0000082553"
FT   DOMAIN          5..165
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        90
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   CROSSLNK        90
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q02159"
FT   CONFLICT        6
FT                   /note="A -> P (in Ref. 1; BAA20373)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..20
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   TURN            63..66
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   HELIX           139..147
FT                   /evidence="ECO:0007829|PDB:6OP8"
FT   HELIX           149..166
FT                   /evidence="ECO:0007829|PDB:6OP8"
SQ   SEQUENCE   166 AA;  18720 MW;  C376ACE52EF444EE CRC64;
     MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF EGGLYPATLK
     FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD PNMYESSSER WSPVQSVEKI
     LLSVMSMLAE PNDESGANID ACKMWREDRE EYCRVVRRLA RKTLGL
//