ID   A0A7J0EKG1_9ERIC        Unreviewed;       731 AA.
AC   A0A7J0EKG1;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 14.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=Acr_05g0000480 {ECO:0000313|EMBL:GFY86409.1};
OS   Actinidia rufa.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=165716 {ECO:0000313|EMBL:GFY86409.1, ECO:0000313|Proteomes:UP000585474};
RN   [1] {ECO:0000313|EMBL:GFY86409.1, ECO:0000313|Proteomes:UP000585474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuchu {ECO:0000313|Proteomes:UP000585474};
RA   Sugita-Konishi S., Sato K., Mori E., Abe Y., Kisaki G., Hamano K.,
RA   Suezawa K., Otani M., Fukuda T., Manabe T., Gomi K., Tabuchi M.,
RA   Akimitsu K., Kataoka I.;
RT   "De Novo Assembly of kiwifruit Actinidia rufa.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:GFY86409.1}.
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DR   EMBL; BJWL01000005; GFY86409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J0EKG1; -.
DR   OrthoDB; 10064100at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000585474; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   FunFam; 3.30.40.10:FF:000114; RING-type E3 ubiquitin transferase; 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; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23315:SF240; U-BOX DOMAIN-CONTAINING PROTEIN 5; 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:UP000585474};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          243..317
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          680..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..703
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  81278 MW;  849BDB137EC87EFC CRC64;
     MCTKLIKLLD RILKVFPEIE ASRPRCSSGI QTLCLLNGGI DKAKSLLWYC SESSKLYLAI
     TADAILSRCN KSCKLLEQSL IQIQSNVPVM LAAEISLIIH DLRGASFSLD SSEKEAGKLL
     RAFIQQYASS GDSVDISAVE TIRFAALRLR ITSQKDVLIE KRSIKKLIDK VGDTDPAKKQ
     ILWFFMDLLK KYGKFIVGQQ TENDYLQHKE SFSFPSSYDE SVQAESHAEH GPEATNGVLC
     GRIPLEEFKC PISLRLMYDP VVIASGQTFE RMWIQKWFDE GHDTCPKTKE KLVHLSLTPN
     VSLKDLISKW CAENGVTIPD PCVQSAACRS LETSSTSIDS LSSMIDLHLP VDFSNVSLGS
     LDSNNSDSLR VKITDGSNSV PMHTNNESQK FQYCANTHEK KPSLNKLDKL PWESQCEMVK
     DVKSHLDLNN QTCHLLSYEN FIEPLIRFLK SAQYLHDVKA QRSGTQLLLA FLRIYGSVPN
     LHEEAYSLLA SFIDSEVTEE ALAIIELLSC HRCCGPKIVA SGAPYSILKI LETQSRKFVE
     PAIIILYNLS SSSDISSVIV PSEIIPKLVP FFEDVDFARY CISILKNLCD DEGCRVSVAE
     TNGCIASIAK LLESDSHEVQ EHAVTVLLSL CSQRVQYCWL VMEEGVIPSL ISISINGNDK
     GKAIAMELLR VLKDIDYSGA QESSGSDFDL SRDSSNHSKE KKSSSKASGF FGVRSRSIFS
     KPSSLATRKK K
//