UBC39_ARATH
ID UBC39_ARATH Reviewed; 316 AA.
AC F4HPP7; Q9C917;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Putative ubiquitin-conjugating enzyme E2 39;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 39;
DE AltName: Full=Ubiquitin carrier protein 39;
GN Name=UBC39; OrderedLocusNames=At1g53023; ORFNames=F14G24.31, F8L10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000250|UniProtKB:P42743}.
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 -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC019018; AAG52279.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32877.1; -; Genomic_DNA.
DR RefSeq; NP_001185206.1; NM_001198277.1.
DR AlphaFoldDB; F4HPP7; -.
DR SMR; F4HPP7; -.
DR STRING; 3702.AT1G53023.1; -.
DR PaxDb; F4HPP7; -.
DR PRIDE; F4HPP7; -.
DR EnsemblPlants; AT1G53023.1; AT1G53023.1; AT1G53023.
DR GeneID; 10723074; -.
DR Gramene; AT1G53023.1; AT1G53023.1; AT1G53023.
DR KEGG; ath:AT1G53023; -.
DR Araport; AT1G53023; -.
DR TAIR; locus:6530298162; AT1G53023.
DR eggNOG; KOG0895; Eukaryota.
DR HOGENOM; CLU_025097_0_0_1; -.
DR InParanoid; F4HPP7; -.
DR OMA; NEVAVFM; -.
DR OrthoDB; 808738at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F4HPP7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HPP7; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..316
FT /note="Putative ubiquitin-conjugating enzyme E2 39"
FT /id="PRO_0000430143"
FT DOMAIN 57..217
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 143
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 316 AA; 36488 MW; 90860D2AA8AFFA7E CRC64;
MVEIKDSSNV RKLKEEFLRD FKRFDTVEDF SDHHYAAEGS PAKLSLWHLK FKGRPKNWVK
DIQKEWKILD KNLPETIFVR ACESRIDLLR AVIIGAEGTP YHDGLFFFDI QFPDTYPSVP
PKVHYHSGGL RINPNLYKCG KVCLSLISTW TGKKREKWLP KESTMLQLLV SIQALILNEK
PYYNEPGYEK SMGTPLGESY SKDYSENVFV FSLKTMHFEE FVRSHFFVRS HDIVKACNAY
KDGAPVGSID KGGVKKQTRQ RGSLKFRINV TSFMKTVVDE FVNLGAIREA NHRGEPNPTL
FSCFFFCYLE LIICSV
