ID A0A0L9U2U7_PHAAN Unreviewed; 879 AA.
AC A0A0L9U2U7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=LR48_Vigan03g049100 {ECO:0000313|EMBL:KOM37110.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM37110.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003373; KOM37110.1; -; Genomic_DNA.
DR RefSeq; XP_017418919.1; XM_017563430.1.
DR AlphaFoldDB; A0A0L9U2U7; -.
DR EnsemblPlants; KOM37110; KOM37110; LR48_Vigan03g049100.
DR GeneID; 108329284; -.
DR Gramene; KOM37110; KOM37110; LR48_Vigan03g049100.
DR OMA; STQYFTH; -.
DR OrthoDB; 37517at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053144; Chromosome 3.
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:SF100; U-BOX DOMAIN-CONTAINING PROTEIN 33; 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 4: Predicted;
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 521..789
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 808..879
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..493
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 879 AA; 98045 MW; 4DDD231C1E28B4F0 CRC64;
MAVVSPVLAT SQRMGSVRSP SDASGEILEE PNPGVVDQPI YVAVAKEVKE SRSNLIWAIQ
HYGGKRICIL YVHVRATMIP LLGGKFPTSA LKEEQVQAYW EEEKQDMHRT LDEYLQICER
MGVRAEKLHI EMDNIEKGII ELVSQHGIRK LVMGAASDKY YNRRMMDLRS KKAIYVCKQA
PASCHIQFIC KGHLIHTRDH SLNEGNVEVA SPLVQQVPNS VRTFRSQSVT LGQGRRGNLT
NDARRVRSAS DGHLASFPAV SSPEETVGFS TPRDRMGTEV SSDESERLSM MSPSGLSISS
DSAVDLALTP GLITESSENA LELTMSQLVI EDLHHSSPPS TLDGGIDDTI YDQLQQAMTE
AEDASLTAYK ETVRRRNAEK EAFEAIRKAK ASESLYTEEL NLRKLAEEEL RKEKEELENA
KRLRDKVREE LHLALDQKAS LESQIASSEL IIKELEQKIV SAVDLLQSYK NEREELQIQR
DNALREAEEL RKKQGETSSS HVPQLFSEFS FSEIKEATDN FNPSLKVGEG GYGSIFKGVL
SYTEVAIKRL HSDSMQGPLE FQQEVDVLSK LRHPNLITLI GACPDAWALV YEYLPNGSLE
DRLACKDNTP PLSWQTRIRV ATELCSALIF LHSSKPHSIV HGDLKPSNIL LDANLISKLS
DFGICRILSN CESSSSNSTE FWKTDPKGTF VYMDPEFLAS GELTPKSDVY SFGIILLRLL
TGRPALGITK EVKYALDTGK LKSLLDPVAG DWPFVQAEQL ARLALRCCDM NRKSRPDLYS
DVWRILDAMR VSSGGTNSFG LSSEGLSQPP SYFICPIFQE VMRDPHVAAD GFTYEAEAIR
GWLDGGNDNS PMTNGKLAHH NLVPNRALRS AIHDWLQNH
//
