ID A0A8X7QT06_BRACI Unreviewed; 824 AA.
AC A0A8X7QT06;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Bca52824_058176 {ECO:0000313|EMBL:KAG2275621.1};
OS Brassica carinata (Ethiopian mustard) (Abyssinian cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=52824 {ECO:0000313|EMBL:KAG2275621.1, ECO:0000313|Proteomes:UP000886595};
RN [1] {ECO:0000313|EMBL:KAG2275621.1, ECO:0000313|Proteomes:UP000886595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2275621.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2275621.1};
RA Ma Q., Huang Y., Song X., Pei D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2275621.1}.
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DR EMBL; JAAMPC010000012; KAG2275621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8X7QT06; -.
DR OrthoDB; 1073015at2759; -.
DR Proteomes; UP000886595; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; USP_STK_Ubox_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR051348; U-box_ubiquitin_ligases.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF95; U-BOX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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:UP000886595};
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 478..759
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 753..824
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..386
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 824 AA; 92622 MW; 03EC7B69283DB568 CRC64;
MIRRQLRRPQ LRSAIRQRRG GDDLSLRQIV VELSPCRENY SDDDSDDYHG VEEANGVLDQ
LPTKAGSDVA CPSQSMTIAI AISGSSKSKN IVKWAVKKFS SEKNVVFKLI HVHLKITSVP
TPSGKLVSIS EAPEDVAATY RRQVMDETKE TLLKPYKKMC ERKKVAVELQ VLESNSVAVA
ITREVSKHLI SRLVVGRSSH VGLYGNRDVT AKISAYVSSL CTIYVVSKGV YIISKKSSSD
VQMNETITDS GSERTDTSSC SSGSGHISDA MSNALKSKSL ALSDKRLQHL PTIVRGVSVR
METSSVDSYG TTSMFSDAGE EVSKRSSPET SCIVSWNPPR SYMSSNDNVT QSEDYFTDNQ
DTFQEIRKLR DELKRAQGMY ELAQVEALDA SRKLNELHEF EELTLKEHVT KGLEEKETRT
FEQMRREARD VAHRREAEMK ATSEAKEKEK LKESSLVGPK LQYQEFTWEE IKTATSSFSK
DLKIGMGAYG DVYKCNLHHT IAAVKVLHSP ESNLSKQFDQ ELEILGKIRH PHLVLLLGAC
PEQGALVYEY MENGSLEDRL FRVNNSQPIP WFIRFRIAWE VASALVFLHK SKPKPIIHRD
LKPANILLDH NFVSKVGDVG ISTMIQVDPL LTQFTTYKQT SPVGTLCYID PEYQRTGRLS
PKTDVYAFGM IILQLLTALP AIALTYKLIK ILDKKAGDWP MEETRKLAAL ALYCTEIRAK
DGPDLENRIL PTLESLNKVA ENARTLISSE PKQPPSHFLC PLLKDVMNEP CVAADGYTYD
RRAIEEWMAD HRTSPVTNLP LQNINLLPSH TLYAAIVEWR RSNQ
//
