PUB53_ARATH
ID PUB53_ARATH Reviewed; 819 AA.
AC Q9LU47;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative U-box domain-containing protein 53;
DE AltName: Full=Plant U-box protein 53;
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=PUB53; OrderedLocusNames=At5g51270; ORFNames=MWD22.22;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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=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; AB023044; BAA97390.1; -; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9LU47; -.
DR SMR; Q9LU47; -.
DR STRING; 3702.AT5G51270.1; -.
DR PaxDb; Q9LU47; -.
DR PRIDE; Q9LU47; -.
DR Araport; AT5G51270; -.
DR TAIR; locus:2176177; AT5G51270.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_1_1; -.
DR InParanoid; Q9LU47; -.
DR PhylomeDB; Q9LU47; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LU47; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LU47; baseline and differential.
DR Genevisible; Q9LU47; 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 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 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..819
FT /note="Putative U-box domain-containing protein 53"
FT /id="PRO_0000322146"
FT DOMAIN 460..728
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 748..819
FT /note="U-box"
FT REGION 208..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..437
FT /evidence="ECO:0000255"
FT COMPBIAS 220..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 582
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 466..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 819 AA; 91821 MW; A4F3FCB29AAA9578 CRC64;
MDSFFKNSYL DPKAVRAQLP KRADLAAPSE PMTVALAISG SIKSKNVIKW ALNKFGSDKN
VTFKLIHIHP KITTLPTASG NIVSISEELE EVAAAYRQKV MQETKETLLK PFKKMCERKK
LKIDETRFES SLTKVAVELQ VLESNSVAVA ITKEVNQHLI SNLIIGRSSQ AASSRNYDIT
ASISASVSNL CTVYVVSNGG VHILAKDTSD TERNDTSIES GFERTSSSCS SGSGANSDVM
SNALKSNPHT LSNKRMQNLP TIVRGVSVPM ETSSTESDET KKRSSDAAEE ASKRSSPETS
RSVSWNPQFR DFDERKDAMS SMSSNFEYGN VVTPLGHYFT DNQDTLNEIS KLRAELRHAH
EMYAVAQVET LDASRKLNEL KFEELTLLEH ETKGIAKKET EKFEQKRREE REAAQRREAE
MKATHEAKEK EKLEESSLVA PKLQYQEFTW EEIINATSSF SEDLKIGMGA YGDVYKCNLH
HTIAAVKVLH SAESSLSKQF DQELEILSKI RHPHLVLLLG ACPDHGALVY EYMENGSLED
RLFQVNDSQP IPWFVRLRIA WEVASALVFL HKSKPTPIIH RDLKPANILL NHNFVSKVGD
VGLSTMIQAA DPLSTKFTMY KQTSPVGTLC YIDPEYQRTG RISPKSDVYA FGMIILQLLT
GQQAMALTYT VETAMENNND DELIQILDEK AGNWPIEETR QLAALALQCT ELRSKDRPDL
EDQILPVLES LKKVADKARN SLSAAPSQPP SHFFCPLLKD VMKEPCIAAD GYTYDRRAIE
EWMENHRTSP VTNSPLQNVN LLPNHTLYAA IVEWRNRNQ
