PUB34_ARATH
ID PUB34_ARATH Reviewed; 801 AA.
AC Q8S8S7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=U-box domain-containing protein 34;
DE AltName: Full=Plant U-box protein 34;
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=PUB34; OrderedLocusNames=At2g19410; ORFNames=F27F23.21;
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 [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 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}.
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DR EMBL; AC003058; AAM14871.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06878.1; -; Genomic_DNA.
DR PIR; T01289; T01289.
DR RefSeq; NP_179531.1; NM_127499.2.
DR AlphaFoldDB; Q8S8S7; -.
DR SMR; Q8S8S7; -.
DR STRING; 3702.AT2G19410.1; -.
DR PaxDb; Q8S8S7; -.
DR PRIDE; Q8S8S7; -.
DR EnsemblPlants; AT2G19410.1; AT2G19410.1; AT2G19410.
DR GeneID; 816460; -.
DR Gramene; AT2G19410.1; AT2G19410.1; AT2G19410.
DR KEGG; ath:AT2G19410; -.
DR Araport; AT2G19410; -.
DR TAIR; locus:2047605; AT2G19410.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_3_1; -.
DR InParanoid; Q8S8S7; -.
DR PhylomeDB; Q8S8S7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8S8S7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8S7; baseline and differential.
DR Genevisible; Q8S8S7; AT.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
FT CHAIN 1..801
FT /note="U-box domain-containing protein 34"
FT /id="PRO_0000322141"
FT DOMAIN 442..705
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 724..797
FT /note="U-box"
FT REGION 205..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..395
FT /evidence="ECO:0000255"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 564
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 448..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 801 AA; 90914 MW; 0E41C37B13CCAC8D CRC64;
MVVMLTQEMS GGGGPKAEEG QLFVAVAVKG LIGDKLGGAG SRRAVRWAVD NLLPKADKFV
MIHVIPTITS IPTPNILILM FTRMWVVTAG DRLPVEEVEE SVVEMYVRDV KKEYETVFVP
FLKMCKSTRS TKRYFRSRRT KGTGVPLTVL RYAPETCEVY IVCKDRITTK SMDPLINREP
CTSPHAAATA HDFLRDWAAS FHTLRSPTLP DPRQSTEAGT RRSASARELR FEALSLTCNK
PKTPQSSKAS SATTPEIFRR RRGSDIPQLN YSDFDKTCTK PQSNVENIVS EHRDSDRSPP
ETSRKSKKVE IEEEVERLKN ELQSTVFKYK QACEELFSTQ NKVKMLSTEY LNESKRVNNA
VEKEELQRNT AALEKERYMK AVKEVETAKA LLAREFCQRQ IAEVNALRTY LEKKKVIDQL
LGTDHRYRKY TIEEIVTATE GFSPEKVIGE GGYGKVYQCS LDSTPAAVKV VRLDTPEKKQ
EFLKEVEVLS QLRHPHVVLL LGACPENGCL VYEYLENGSL EEYIFHRKNK PPLPWFIRFR
VIFEVACGLA FLHSSKPEPI VHRDLKPGNI LLNRNYVSKI ADVGLAKLVT DVAPDNVTMY
RNSVLAGTLH YIDPEYHRTG TIRPKSDLYA FGIIILQLLT ARNPSGIVPA VENAVKKGTL
TEMLDKSVTD WPLAETEELA RIGLKCAEFR CRDRPDLKSE VIPVLKRLVE TANSKVKKEG
SNLRAPSHYF CPILREIMEE PEIAADGFTY ERKAILAWLE KHNISPVTRQ KLDHFKLTPN
HTLRSAIRDW KSRVRFSNVV V
