ID A0AAD6KKI1_9ROSI Unreviewed; 408 AA.
AC A0AAD6KKI1;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=U-box domain-containing protein {ECO:0000256|RuleBase:RU369093, ECO:0000259|PROSITE:PS51698};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369093};
DE AltName: Full=RING-type E3 ubiquitin transferase PUB {ECO:0000256|RuleBase:RU369093};
GN ORFNames=OIU84_025832 {ECO:0000313|EMBL:KAJ6425136.1};
OS Salix udensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix.
OX NCBI_TaxID=889485 {ECO:0000313|EMBL:KAJ6425136.1, ECO:0000313|Proteomes:UP001162972};
RN [1] {ECO:0000313|EMBL:KAJ6425136.1, ECO:0000313|Proteomes:UP001162972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Shoot tip {ECO:0000313|EMBL:KAJ6425136.1};
RX PubMed=36769224; DOI=10.3390/ijms24032904;
RA Hyden B., Feng K., Yates T.B., Jawdy S., Cereghino C., Smart L.B.,
RA Muchero W.;
RT "De Novo Assembly and Annotation of 11 Diverse Shrub Willow (Salix) Genomes
RT Reveals Novel Gene Organization in Sex-Linked Regions.";
RL Int. J. Mol. Sci. 24:2904-2904(2023).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|RuleBase:RU369093}.
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 ECO:0000256|RuleBase:RU369093};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369093}.
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:KAJ6425136.1}.
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DR EMBL; JAPFFJ010000006; KAJ6425136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD6KKI1; -.
DR Proteomes; UP001162972; Chromosome 16.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR058678; ARM_PUB.
DR InterPro; IPR045185; PUB22/23/24-like.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22849:SF128; U-BOX DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22849; WDSAM1 PROTEIN; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP001162972};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369093};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369093}.
FT DOMAIN 5..82
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
SQ SEQUENCE 408 AA; 46321 MW; 6994BFB889688D02 CRC64;
MDDIEIPEYF LCPISLQPLQ DPVTTITGIT YERESIEQWL KTARGNPTCP VTKQPLPRDS
ILTPNHTLKR LIQSWCVLNS VNGIDGIPMP KSPIKKSHVL RLVKDLDLPD HSCTKALMKL
EALAAENERN RACMVEAGLE KSMVLFIIKC FKEGKTAGLE ESLRILHLIW NPSQEIKILV
RENQEFIDSL TWILRCKIDN HVAVKTHAML VLQKTIDVVC QKQPERLNVD FFKDIITRVL
RKRISKLAIK SALLVLTQVC LWGRNRVKIV EANAVYELIE LELEKPERNI TELIFNLLAQ
LCSCAAGREQ FLKHAGSIAM LSKRILRVST ATDDRALHIL DSISKFSARD DAVLEMLRVG
AVTKLCMVIQ ADCAPYLKKK AGEILRLHSN TWNNSPCIAV YLLTRYAR
//
