ID   A0AAE0EI49_9ROSI        Unreviewed;      1029 AA.
AC   A0AAE0EI49;
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=Dsin_000805 {ECO:0000313|EMBL:KAK3228924.1};
OS   Dipteronia sinensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Sapindaceae; Hippocastanoideae; Acereae;
OC   Dipteronia.
OX   NCBI_TaxID=43782 {ECO:0000313|EMBL:KAK3228924.1, ECO:0000313|Proteomes:UP001281410};
RN   [1] {ECO:0000313|EMBL:KAK3228924.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBL {ECO:0000313|EMBL:KAK3228924.1};
RX   PubMed=37797086;
RA   Feng Y., Comes H.P., Chen J., Zhu S., Lu R., Zhang X., Li P., Qiu J.,
RA   Olsen K.M., Qiu Y.;
RT   "Genome sequences and population genomics provide insights into the
RT   demographic history, inbreeding, and mutation load of two 'living fossil'
RT   tree species of Dipteronia.";
RL   Plant J. 0:0-0(2023).
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:KAK3228924.1}.
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; JANJYJ010000001; KAK3228924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAE0EI49; -.
DR   Proteomes; UP001281410; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR052608; U-box_domain_protein.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   PANTHER; PTHR45958:SF11; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00185; ARM; 5.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP001281410};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          259..333
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   DOMAIN          266..304
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REPEAT          455..485
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   COILED          202..232
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1029 AA;  114067 MW;  E8BE6CA7B4D91614 CRC64;
     MSSMDFNIGI EDVGVAVLQE LWNRVAFQTV DLVSETRDAV LGKNSFQEFS RSINELHTLL
     QALDVRKIGA AKGSEFTKAR LEALDSQLRK AREIIKDYKS GSRLRLLLHS NSMLSQMQDL
     AREIATTISS FHLVNLDMAL NLKTMTNQII NSLESMEFQS AAATETIASE IENSISQNSR
     DREHSLNLLE KIAEALGASS NATLVQNELA LLKQEKEEME AAKKQAEALQ LSQLIQLLYS
     TEIITRPQNE GTATYYPQYP IEALICPLCN ELLTDPVAIS CGHSFERKAI LEHFKGGEKN
     CPTCGEELSS LDLTPNISLR SSIQEWKQID MELTFQAAIT EINSGDHSRQ NKALEHVQSL
     IHISKYADKA AEEGLIPKLV EFLKDKRLNI KATLKCLYCL AEYSDEYKDA ISEAGAVRQV
     VKQIYKGETE SDAIAVLLEL SKIETIGEKI GKTKDCIPVL VSLLRNDNPN VSQKAHNVLQ
     NLSSNTHFAV KMAEAGYFPP FVACFNQGAQ ETRALMAAAF TKMELKENSI KDLKDRQFIH
     NMIQMLSSNY PACKSTCLKC IKKLIAYPKM VKRLLSDPVS IPNLLGLISL MKSESHFKQE
     AAEVLALMVE ACQYPQFLLY QGLQELQSEH SISLFLQLVA SSEPQIKIQF LHLLVELSYK
     CEKARNLIQS NNEAVTHLFS SLESDHQAVR RWAMKLIHCI SEGYPDGVPL PPSPGKEAAV
     NTLATILTCS LDTDERSIAA AIISQLPKED NVVDEVLRKS ETLKAIHEVI CCTDGEFLGM
     KTPASQSNSL LENALAALLR FTEPTKPELQ RQVGKLELYP SLIRVLSTGS STAKQRTAIA
     LAQLSQSTSI SVSKTTTMSK QTNSMPMLQI MKLLPNMFWC CSASPENLFC SVHGSACSPR
     ETFCLVKADA VKPLVQTLSD KESGVAEAAL MALETLLMDH NTLSHAIAVI VDSQGVIAIL
     QVLEKGSLSA KTKALDLLQK ILKHTQISDF LSLRSETILI QLLDEDTLRK KVALVLRQMG
     IIPEQSSYF
//