ID A0AAE1VJN3_9SOLA Unreviewed; 804 AA.
AC A0AAE1VJN3;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=RND71_018730 {ECO:0000313|EMBL:KAK4363489.1};
OS Anisodus tanguticus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Anisodus.
OX NCBI_TaxID=243964 {ECO:0000313|EMBL:KAK4363489.1, ECO:0000313|Proteomes:UP001291623};
RN [1] {ECO:0000313|EMBL:KAK4363489.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KB-2021 {ECO:0000313|EMBL:KAK4363489.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAK4363489.1};
RA Wang Y.-J.;
RT "Genome assembly of Anisodus tanguticus.";
RL Submitted (DEC-2023) 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:KAK4363489.1}.
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; JAVYJV010000009; KAK4363489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE1VJN3; -.
DR Proteomes; UP001291623; 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: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; 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:SF128; U-BOX DOMAIN-CONTAINING PROTEIN 35-LIKE; 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:UP001291623};
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 454..708
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 728..801
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 205..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 375..431
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 804 AA; 89775 MW; 587F25D834B30E8B CRC64;
MEEKNGVVTK VEGLSALPPL NTSTIAVAIN GKKKSEYVVK WALDKFVPEG KVCFKLLHVR
PRITGVPTAM GSFIPISQVR DDVVAAFRKD VEWQTSENLL PYKMLCTKRK VQVEVLQLES
DDIVKAIAQE VTKLNIIKLV IGASSRSIFS RGQSLSSRIS DSTPSFCTIY AVSKGKLLSV
RPSNSAINGS SSAEDSYTSC SISSSTGHTS SSLTERSEPD SSSSYSHFRS PSLPMQRFQA
LSHINQNFPH RRASSNESVH HKNYSLDFGD GEDDVSSCPQ GTYTADLASS FRSLVTDNYV
TADDQASISG ALTDSSSGYE VDINFELEKL RTELRHTRGM YAVAQTEVID ASRKINELHK
RRLDEDIKLR EICLKEEEVK ELARKENEMY EAVKREAEYV KDCAEREAAQ RKEAEKLALR
ELKEKDKLEN ALTGQAHQYQ EFTWEEIISS TSSFAENLKI GKGAYGTVYK CSLHHTTVAV
KVLHSEGSHL KSSISKSHPH LLILLGVCPD RGCLVYEFME NGCLEERLLR KHDTPPIPWF
DRYRIAWEVA SALAFLHNSK PDPIIHRDLK PANILLDRNF VSKIGDVGLS TMINSDAVLS
TTYKDTGPVG TLCYIDPEYQ RTGMVSPTSD IYAFGMVLLQ LLTAKTAMGL PHIVETAINK
DNLATVLDSE AGKWPLKETK KLAILALKCT EICRRDRPEL KDEILPALEK LKEVADKARD
SASTTQPPPP NYYLCPLLKD IMEEPCVAAD GYTYDRKAIE TWLKENDISP MTNLPLAHKN
LLPNYALLSA ILDWKYLGCL DRYV
//
