ID   UBC31_ARATH             Reviewed;         154 AA.
AC   Q9C8X7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 31;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 31;
DE   AltName: Full=Ubiquitin carrier protein 31;
GN   Name=UBC31; OrderedLocusNames=At1g36340; ORFNames=F7F23.6;
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], INDUCTION, 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).
RN   [2]
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   [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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- INDUCTION: By biotic stresses. {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; DQ027044; AAY44870.1; -; mRNA.
DR   EMBL; AC021199; AAG52201.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31861.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59827.1; -; Genomic_DNA.
DR   EMBL; BT015146; AAT85742.1; -; mRNA.
DR   EMBL; BT015658; AAU15157.1; -; mRNA.
DR   PIR; E86484; E86484.
DR   RefSeq; NP_001319154.1; NM_001333179.1.
DR   RefSeq; NP_564472.1; NM_103322.3.
DR   AlphaFoldDB; Q9C8X7; -.
DR   SMR; Q9C8X7; -.
DR   STRING; 3702.Q9C8X7; -.
DR   PaxDb; 3702-AT1G36340-1; -.
DR   ProteomicsDB; 243218; -.
DR   EnsemblPlants; AT1G36340.1; AT1G36340.1; AT1G36340.
DR   EnsemblPlants; AT1G36340.2; AT1G36340.2; AT1G36340.
DR   GeneID; 840541; -.
DR   Gramene; AT1G36340.1; AT1G36340.1; AT1G36340.
DR   Gramene; AT1G36340.2; AT1G36340.2; AT1G36340.
DR   KEGG; ath:AT1G36340; -.
DR   Araport; AT1G36340; -.
DR   TAIR; AT1G36340; UBC31.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; Q9C8X7; -.
DR   OMA; GVEKKFC; -.
DR   OrthoDB; 639280at2759; -.
DR   PhylomeDB; Q9C8X7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9C8X7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8X7; baseline and differential.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF370; UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q9C8X7; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..154
FT                   /note="Probable ubiquitin-conjugating enzyme E2 31"
FT                   /id="PRO_0000345196"
FT   DOMAIN          8..153
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        91
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   154 AA;  17833 MW;  2B6942F225E96486 CRC64;
     MFKKMDKKAA QRIAMEYRAM ISKESLFSIG QNSNNIYEWT AVIRGPDGTP YEGGMFNLSI
     KFPTDYPFKP PKFTFKTPIY HPNINDEGSI CMNILKDKWT PALMVEKVLL SILLLLEKPN
     PDDPLVPEIG QLFKNNRFQF DQRAREFTAR HANN
//