PUB50_ARATH
ID PUB50_ARATH Reviewed; 765 AA.
AC Q9FGD7; F4KHZ7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative U-box domain-containing protein 50;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 50;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB50 {ECO:0000305};
GN Name=PUB50; OrderedLocusNames=At5g65500; ORFNames=K19O4.3;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FGD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FGD7-2; Sequence=VSP_042251, VSP_059309;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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; AB026638; BAB11278.1; -; Genomic_DNA.
DR EMBL; AB026639; BAB11278.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED98064.1; -; Genomic_DNA.
DR RefSeq; NP_201353.4; NM_125948.4. [Q9FGD7-2]
DR AlphaFoldDB; Q9FGD7; -.
DR SMR; Q9FGD7; -.
DR STRING; 3702.AT5G65500.1; -.
DR PRIDE; Q9FGD7; -.
DR EnsemblPlants; AT5G65500.1; AT5G65500.1; AT5G65500. [Q9FGD7-2]
DR GeneID; 836676; -.
DR Gramene; AT5G65500.1; AT5G65500.1; AT5G65500. [Q9FGD7-2]
DR KEGG; ath:AT5G65500; -.
DR Araport; AT5G65500; -.
DR eggNOG; ENOG502QST6; Eukaryota.
DR InParanoid; Q9FGD7; -.
DR OMA; VILHVTH; -.
DR PhylomeDB; Q9FGD7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FGD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGD7; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
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; SM00504; Ubox; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Coiled coil; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..765
FT /note="Putative U-box domain-containing protein 50"
FT /id="PRO_0000322143"
FT DOMAIN 422..765
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 688..762
FT /note="U-box"
FT COILED 198..391
FT /evidence="ECO:0000255"
FT BINDING 428..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 107..117
FT /note="CPLSVNFVLFG -> KAELLKVEKQHDSIQVLILDLISKLRITKLVMGITFM
FT RSSSSW (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042251"
FT VAR_SEQ 240..249
FT /note="DVAEKLEYVR -> VKIL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059309"
SQ SEQUENCE 765 AA; 87314 MW; 1DD2B3DD1297152B CRC64;
MEETKTHELE VEAESGSRME KVYIAVGNDV QEGYKTIHWA LKKWNNIPIS IVLLHLCNIS
QDFVYTPFGK LPASSVSEEK LQVLRKYEDQ KIDKLLSKYI TFCGKVCPLS VNFVLFGKSK
SAISGSFYVY QNKPEFCEFY IICGGKMVSL KNDVNNNNSN IRSWIGKMFH DPGRNLDRSS
GNNDDPTASG SSWDKNLQEI ENYFQQLLSL NLAEEETENV VEEEQEDDDD VALNVLQHMD
VAEKLEYVRR KVNEAKLMID EKSREVKVNA ERSNRAEWAI SLCNSRIGEF EAWIKEESER
REKLQATLDS DKECIEEAKN YVEKGKTKLH SLAELQEVLS SKVKTMMEAK SQAEVELERV
VLQRGEMITE IEKLRSQRDV FNRRIEFCKE REVIGSVSKE EVKCGYREYV AEDIRLATET
YSDRLRLKSG GNWTNVYRGR IKHTTVAVKV IGDSLSDEAF GAKVKLLNEI RHPNLVAIAG
FCSQRPKCLL FEYMHNGNLR DNLFTSQRKS RRSKILKWHD RIRIAHQVCS GLGFLHSVKP
KPIVHGRLTP SKILLDRNLV PKITGFGLIM HSDQSDTKPD VMAFGVLLLH LLTGRNWHGL
LKAMSMNQTS ILRDLDQTAG KWPLELAKEF GALAVKCSSV NRGGNMDFST KEIMEELGKI
REKADEFKTK GGYEEATNSN MDEGDPNDIP SVFMCPILQE VMKNPHVAAD GFSYELEAIQ
EWLSMGHDTS PMTNLRLDYQ MLTPNHTLRS LIQDWHSKRA AQASS
