ID F4K964_ARATH Unreviewed; 789 AA.
AC F4K964;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN OrderedLocusNames=At5g57035 {ECO:0000313|Araport:AT5G57035,
GN ECO:0000313|EMBL:AED96837.1};
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 {ECO:0000313|EMBL:AED96837.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AED96837.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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.
CC {ECO:0000256|ARBA:ARBA00003861}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; CP002688; AED96837.1; -; Genomic_DNA.
DR RefSeq; NP_680448.2; NM_148143.4.
DR AlphaFoldDB; F4K964; -.
DR SMR; F4K964; -.
DR IntAct; F4K964; 1.
DR iPTMnet; F4K964; -.
DR PaxDb; 3702-AT5G57035-1; -.
DR ProteomicsDB; 219803; -.
DR EnsemblPlants; AT5G57035.1; AT5G57035.1; AT5G57035.
DR GeneID; 835807; -.
DR Gramene; AT5G57035.1; AT5G57035.1; AT5G57035.
DR KEGG; ath:AT5G57035; -.
DR Araport; AT5G57035; -.
DR TAIR; AT5G57035; -.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_1_1; -.
DR InParanoid; F4K964; -.
DR OMA; KCTALRC; -.
DR OrthoDB; 1118232at2759; -.
DR PhylomeDB; F4K964; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K964; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF137; U-BOX DOMAIN-CONTAINING PROTEIN KINASE FAMILY PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AED96837.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4K964,
KW ECO:0007829|ProteomicsDB:F4K964};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 425..714
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 707..781
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 206..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 344..397
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 206..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 789 AA; 88875 MW; 0B08D2F6CFE3F25B CRC64;
MVVMTNKFFE LIGGAPSYSS VSVAVKGSVG DAVGGTASRR ALRWTIENFL PKIDRLVLVH
VMPTVTTIPS PSGSKIPIEE LDESVVSMYK RDLRKEFEQV FVPFKRICKS NKVETLLLEH
HDPAKALLKY MSDTDVECLV IGSCSSNFLT RKKGQEMPLT VLGEAPETCE IYVVCKDRIL
TKSTNQFTAD SSSSFRIPEG AEAYTESFSR TRSDKTGLSA SSITSSGRMR IGRPGSLPHS
HPTSRVYSDA QSSSTDIVLV DDEHCRSILR HSTVSTSKIQ MDPRPHLKTP KSGVRAEVEQ
LRKEVQTTLS MYKQACEELV HKQTQVQSLS SECIKETERV ITALEKEEMR RKAAAEEKEK
HLKAVKEVEE AKSMLAKEFC ERQLAELDAL KQSIEKQKVI EQLFLRDGRY RKYTKEEIAA
ATDNFSSRKI IGEGGYGKVY KCSLDHTPVA LKVLKPDSVE KKEEFLKEIS VLSQLRHPHV
VLLLGACPEN GCLVYEYMEN GSLDCHISPK KGKPSLSWFI RFRIIYETAC GLAFLHNSKP
EPIVHRDLKP GNILLDRNFV SKIGDVGLAK LMSDEAPDSV TVYRNSIIAG TLYYMDPEYQ
RTGTIRPKSD LYAFGIIILQ LLTARHPNGL LFCVEDAVKR GCFEDMLDGS VKDWPIAEAK
ELARIAIRCS QLKCRDRPDL STQVLPALKR ILESANSRLK TEQANARAPT HYYCPILKEI
MEDPQIAADG FTYERKAIKE WIQKHQDVSP VTKHRLKHSD LTPNHTLRSA IREWRSRSRL
DLSTTLGSY
//
