UBC2_ASPFU
ID UBC2_ASPFU Reviewed; 151 AA.
AC Q4WLA7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 2;
DE AltName: Full=Ubiquitin carrier protein ubc2;
DE AltName: Full=Ubiquitin-protein ligase ubc2;
GN Name=ubc2; ORFNames=AFUA_6G14210;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Plays a role in transcription regulation by catalyzing the
CC monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives
CC a specific tag for epigenetic transcriptional activation and is also a
CC prerequisite for H3K4me and H3K79me formation. Also involved in
CC postreplication repair of UV-damaged DNA, in N-end rule-dependent
CC protein degradation and in sporulation. {ECO:0000255|PROSITE-
CC 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, 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:Q5VVX9}. Nucleus
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; AAHF01000006; EAL89257.1; -; Genomic_DNA.
DR RefSeq; XP_751295.1; XM_746202.1.
DR AlphaFoldDB; Q4WLA7; -.
DR SMR; Q4WLA7; -.
DR STRING; 746128.CADAFUBP00000054; -.
DR EnsemblFungi; EAL89257; EAL89257; AFUA_6G14210.
DR GeneID; 3508612; -.
DR KEGG; afm:AFUA_6G14210; -.
DR VEuPathDB; FungiDB:Afu6g14210; -.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; Q4WLA7; -.
DR OMA; DHKSQYI; -.
DR OrthoDB; 1292821at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IEA:EnsemblFungi.
DR GO; GO:1990305; C:RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070628; F:proteasome binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0090089; P:regulation of dipeptide transport; IEA:EnsemblFungi.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:EnsemblFungi.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Nucleotide-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="Ubiquitin-conjugating enzyme E2 2"
FT /id="PRO_0000082527"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 151 AA; 17169 MW; 89345B6BA251A556 CRC64;
MSTSARRRLM RDFKRMQTDP PAGVSASPVA DNVMTWNAVI IGPADTPFED GTFRLVMHFE
EQYPNKPPGV KFISQMFHPN VYGTGELCLD ILQNRWSPTY DVAAILTSIQ SLLNDPNTSS
PANVEASNLY KDNRKEYIKR VRETVEKSWE D
