UBC9_DICDI
ID UBC9_DICDI Reviewed; 159 AA.
AC Q9NGP4; Q54JV2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Sumo-conjugating enzyme ubc9;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin carrier protein 9;
GN Name=ubc9; ORFNames=DDB_G0287693;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Franke J., Volino P.A., Kessin R.H.;
RT "The Dictyostelium homolog of ubc9.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Accepts the ubiquitin-like protein sumo from the E1 complex
CC and catalyzes its covalent attachment to other proteins with the help
CC of an E3 ligase.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF246690; AAF65153.1; -; Genomic_DNA.
DR EMBL; AAFI02000104; EAL63493.1; -; Genomic_DNA.
DR RefSeq; XP_637050.1; XM_631958.1.
DR AlphaFoldDB; Q9NGP4; -.
DR SMR; Q9NGP4; -.
DR STRING; 44689.DDB0191440; -.
DR PaxDb; Q9NGP4; -.
DR EnsemblProtists; EAL63493; EAL63493; DDB_G0287693.
DR GeneID; 8626304; -.
DR KEGG; ddi:DDB_G0287693; -.
DR dictyBase; DDB_G0287693; ubc9.
DR eggNOG; KOG0424; Eukaryota.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; Q9NGP4; -.
DR OMA; QEPAWRA; -.
DR PhylomeDB; Q9NGP4; -.
DR Reactome; R-DDI-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-DDI-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DDI-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-DDI-3232118; SUMOylation of transcription factors.
DR Reactome; R-DDI-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DDI-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DDI-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DDI-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DDI-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DDI-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q9NGP4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
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; Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..159
FT /note="Sumo-conjugating enzyme ubc9"
FT /id="PRO_0000327848"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 159 AA; 18127 MW; BC92A0B8F78527DD CRC64;
MAGISSARLS EERKNWRRDH PYGFFARPST NTDGSLNLYV WNCGIPGKTK TNWEGGVYPL
IMEFTEDYPS KPPKCRFPKD FFHPNVYPSG TVCLSILNEE ADWKPSVTIK TVLLGIQDLL
DNPNPKSPAQ QLPIHLFLTN KEEYDKKVKA QSKVYPPPQ