PUB33_ARATH
ID PUB33_ARATH Reviewed; 834 AA.
AC Q8GUH1; O80828;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=U-box domain-containing protein 33;
DE AltName: Full=Plant U-box protein 33;
DE Includes:
DE RecName: Full=E3 ubiquitin ligase;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000305};
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.-;
GN Name=PUB33; OrderedLocusNames=At2g45910; ORFNames=F4I18.11;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11495788; DOI=10.1016/s1360-1385(01)01960-4;
RA Azevedo C., Santos-Rosa M.J., Shirasu K.;
RT "The U-box protein family in plants.";
RL Trends Plant Sci. 6:354-358(2001).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004665; AAC28534.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10616.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61922.1; -; Genomic_DNA.
DR EMBL; BT002512; AAO00872.1; -; mRNA.
DR EMBL; AK227123; BAE99173.1; -; mRNA.
DR PIR; T02456; T02456.
DR RefSeq; NP_001324111.1; NM_001337160.1.
DR RefSeq; NP_182115.2; NM_130154.4.
DR AlphaFoldDB; Q8GUH1; -.
DR SMR; Q8GUH1; -.
DR BioGRID; 4535; 4.
DR STRING; 3702.AT2G45910.1; -.
DR iPTMnet; Q8GUH1; -.
DR PaxDb; Q8GUH1; -.
DR PRIDE; Q8GUH1; -.
DR ProteomicsDB; 226064; -.
DR EnsemblPlants; AT2G45910.1; AT2G45910.1; AT2G45910.
DR EnsemblPlants; AT2G45910.2; AT2G45910.2; AT2G45910.
DR GeneID; 819199; -.
DR Gramene; AT2G45910.1; AT2G45910.1; AT2G45910.
DR Gramene; AT2G45910.2; AT2G45910.2; AT2G45910.
DR KEGG; ath:AT2G45910; -.
DR Araport; AT2G45910; -.
DR TAIR; locus:2050669; AT2G45910.
DR eggNOG; ENOG502QQ1P; Eukaryota.
DR HOGENOM; CLU_000288_153_0_1; -.
DR InParanoid; Q8GUH1; -.
DR OMA; PVEYQQE; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8GUH1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GUH1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GUH1; baseline and differential.
DR Genevisible; Q8GUH1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
FT CHAIN 1..834
FT /note="U-box domain-containing protein 33"
FT /id="PRO_0000322140"
FT DOMAIN 481..744
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 762..834
FT /note="U-box"
FT REGION 232..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..462
FT /evidence="ECO:0000255"
FT COMPBIAS 232..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 603
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 487..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 640
FT /note="V -> I (in Ref. 3; AAO00872 and 4; BAE99173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 93030 MW; 3209BBFCEB271144 CRC64;
MALVSPIPAM GERAGSMRFH GIGSPGSRSS RSGIMDEPVS RLIDEKIFVA VDKHVAKSKS
TLIWALQNTG GKKICLIHVH QPSQMIPLMG AKFPVGAVKE EEVRVFREKE REKVHMILDD
YLRICQQRGV RAEKMFIEME SIENGIVQLI SELGIRKLVM GAAADRHYSR RMTDLKSRKA
IFVRREAPTL CQIWFTCKGY LIHTREATMD DTESEYASPR PSISASDLLQ TFSTPESEHQ
HISRVQSTDS VQQLVSNGSS TEQSGRVSDG SLNTDEEERE SDGSEVTGSA TVMSSGHSSP
SSFPDGVDDS FNVKIRKATS EAHSSKQEAF AETLRRQKAE KNALDAIRRA KQSESAYSEE
LKRRKDTEIA VAKEKERFIT IKNEQEVIME ELQSAMAQKA MLESQIAKSD GTMEKLNQKL
DIAVKLLQKL RDEREELQTE RDRALREAEE LRSHAETSTL QLPQYFTDFS FSEIEEATNH
FDSTLKIGEG GYGSIYVGLL RHTQVAIKML NPNSSQGPVE YQQEVDVLSK MRHPNIITLI
GACPEGWSLV YEYLPGGSLE DRLTCKDNSP PLSWQNRVRI ATEICAALVF LHSNKAHSLV
HGDLKPANIL LDSNLVSKLS DFGTCSLLHP NGSKSVRTDV TGTVAYLDPE ASSSGELTPK
SDVYSFGIIL LRLLTGRPAL RISNEVKYAL DNGTLNDLLD PLAGDWPFVQ AEQLARLALR
CCETVSENRP DLGTEVWRVL EPMRASSGGS SSFHLGRNEH RIAPPYFICP IFQEVMQDPH
VAADGFTYEA EAIRAWLDSE HDTSPMTNVK LSHTSLIANH ALRSAIQEWL QHHL
