ID D7MGJ0_ARALL Unreviewed; 832 AA.
AC D7MGJ0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ARALYDRAFT_492318 {ECO:0000313|EMBL:EFH43881.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GL348719; EFH43881.1; -; Genomic_DNA.
DR RefSeq; XP_002867622.1; XM_002867576.1.
DR AlphaFoldDB; D7MGJ0; -.
DR STRING; 81972.D7MGJ0; -.
DR EnsemblPlants; fgenesh2_kg.7__1751__AT4G25160.1; fgenesh2_kg.7__1751__AT4G25160.1; fgenesh2_kg.7__1751__AT4G25160.1.
DR Gramene; fgenesh2_kg.7__1751__AT4G25160.1; fgenesh2_kg.7__1751__AT4G25160.1; fgenesh2_kg.7__1751__AT4G25160.1.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_1_1; -.
DR OrthoDB; 1118232at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; STK_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR006016; UspA.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF15; U-BOX DOMAIN-CONTAINING PROTEIN 35; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00582; Usp; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFH43881.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 477..742
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 762..832
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 832 AA; 93416 MW; 5FB74FD6E38E721C CRC64;
MSRSPDNLAL PPPPPPPPSR TVVVALSGSS KSKYVVTWAL EKFAPEGNVG FKLLHIHPMI
TSVPTPMGNA IPISEVRDDV VTAFRQEILW QSEEMLKPFT KLFVRKKVAV EVLVIESDNL
AAAIAEEVTR DSIDRIVIGG SSRSFFSRKA DMCSAISALM PNFCTVYVVS KGKLSCVRPS
DSDGNATIRD DGSERTNSSS GSSGPTSDVM SSVHDSQSRA LSLPVRRMQN FPTIARQASV
PMETSSVGSD ETRCMSLDAE EARDVSSINR SSTDTTSRWT PRLRDYEERK EAMSSSSSNR
EYGNIGSRFS WTGMGVDNTH SRASQQASNM SDALSEQSYT DSQVNLNFEV EKLRAELRHV
QEMYAMAQTE TFDASRKLGE LNQRRLEEAI KLEELKLKEY EARELAEREK QNVEKARRDA
ESMRERAERE IAQRREVERK SARDTKEREK LKGTLGSPQL QYQHFAWEEI MAATSSFSEE
LKIGMGAYGA VYKCNLHHTT AAVKVLHSAE SRLSKQFQQE LEILSKIRHP HLVLLLGACP
EQGALVYEYM ENGSLEDRLF QVNNSPPLPW FERFRIAWEV AAALVFLHKS KPKPIIHRDL
KPANILLDQN FVSKVGDVGL STMVQVDLLS TKFTIYKQTS PVGTLCYIDP EYQRTGMISS
KSDVYSFGMI VLQLLTAKPA IALTHFVESA MDSNDEFLKI LDQKAGNWPI EETRELTALA
LCCTELRGKD RPDLKNQILP ALENLKKVAE MARNSLSGVS TQPPTHFICP LLKDVMNEPC
VAADGYTYDR RAIEEWLEEH DTSPMTDSPL HSKNLLPNYT LYTAIMEWRS TR
//
