UBC30_ARATH
ID UBC30_ARATH Reviewed; 148 AA.
AC Q9FKT3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 30;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 30;
DE AltName: Full=Ubiquitin carrier protein 30;
GN Name=UBC30; OrderedLocusNames=At5g56150; ORFNames=MDA7.21;
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 [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH RGLG3 AND RGLG4.
RX PubMed=27497447; DOI=10.1093/pcp/pcw122;
RA Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R., Staes A.,
RA Van Leene J., Rubio V., Gevaert K., De Jaeger G., Pauwels L., Goossens A.;
RT "The Arabidopsis iron-sulfur protein GRXS17 is a target of the ubiquitin E3
RT ligases RGLG3 and RGLG4.";
RL Plant Cell Physiol. 57:1801-1813(2016).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins.
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 -!- SUBUNIT: Interacts with RGLG3 and RGLG4. {ECO:0000269|PubMed:27497447}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels.
CC {ECO:0000269|PubMed:16339806}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; DQ027043; AAY44869.1; -; mRNA.
DR EMBL; AB011476; BAB09297.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96726.1; -; Genomic_DNA.
DR EMBL; AY059806; AAL24288.1; -; mRNA.
DR EMBL; AY081511; AAM10073.1; -; mRNA.
DR EMBL; AY084220; AAM60821.1; -; mRNA.
DR RefSeq; NP_851198.1; NM_180867.3.
DR AlphaFoldDB; Q9FKT3; -.
DR SMR; Q9FKT3; -.
DR BioGRID; 20958; 4.
DR STRING; 3702.AT5G56150.1; -.
DR PaxDb; Q9FKT3; -.
DR PRIDE; Q9FKT3; -.
DR ProteomicsDB; 243217; -.
DR EnsemblPlants; AT5G56150.1; AT5G56150.1; AT5G56150.
DR GeneID; 835714; -.
DR Gramene; AT5G56150.1; AT5G56150.1; AT5G56150.
DR KEGG; ath:AT5G56150; -.
DR Araport; AT5G56150; -.
DR TAIR; locus:2161850; AT5G56150.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q9FKT3; -.
DR OMA; RAKYENT; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; Q9FKT3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FKT3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKT3; baseline and differential.
DR Genevisible; Q9FKT3; AT.
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; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin-conjugating enzyme E2 30"
FT /id="PRO_0000345195"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 148 AA; 16480 MW; 3FAF79744E8821C7 CRC64;
MASKRINKEL RDLQRDPPVS CSAGPTGDDM FQWQATIMGP ADSPFAGGVF LVTIHFPPDY
PFKPPKVAFR TKVYHPNINS NGSICLDILK EQWSPALTVS KVLLSICSLL TDPNPDDPLV
PEIAHIYKTD RVKYESTAQS WTQKYAMG
