ID A0A498HZJ4_MALDO Unreviewed; 1047 AA.
AC A0A498HZJ4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DVH24_030123 {ECO:0000313|EMBL:RXH75402.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH75402.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH75402.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH75402.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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:RXH75402.1}.
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DR EMBL; RDQH01000341; RXH75402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HZJ4; -.
DR STRING; 3750.A0A498HZJ4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000290289; Chromosome 15.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; IPR000225; Armadillo.
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:SF7; U-BOX DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 248..322
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 606..648
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 688..730
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 729..770
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 336..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..219
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 351..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 110124 MW; 12F41F9BBAF34302 CRC64;
MGLILGRINS WGVMEISLFK ALLNNISSFF HLSSHDNINF DPVLKYYKRA EEILKLLKIV
LDAIADSEIA SYELLNKPFE ELGQYVDELR EQIEDWQPLF SKVNLVLQVE SLISKIWASG
LDIFQLLKTS PQHLPDEMGS ASLEQCIQKL EHMGYEQMST VIKDAISDQV EGVGPSSEIL
VKIAEGLSLK SNQEILIEAV ALEKLKENAE QSEKIEEAEY IEQMISLVTR MHERLITIKQ
AESCSPVPIP ADFCCPLSLE LMTDPVIVAS GQTYERTFIK NWIGLGLTVC PKTRQTLAHT
NLIPNYTVKA LIANWCESNN VKLPDPIKSV GLNKSAHLGH AEPGTPKDSP IFSHSRVNQS
MSPESTRSTG LPSKNMFSSG PLHQERISPL HPRSTSEGSL PGIVGNGQAL DIERISLANS
EDRSANLEER STDLDSQHSL SPSRDELPNS IEDEQPSQSH NRTASASSVL FNANGTQGTS
VNANGVLQVS TNLSGYSSDA SGELKSQAQT VAPLAPQQRE TESPTRMAES RPRNQMWRRP
SSLIPRIVSS PPIETRPDLS ELEAQVRNLV DDLKSTSLDT QREATFQLRL LAKHNMDNRI
VIANCGAIGL LVDLLRSTDT RVQENAVTAL LNLSINDNNK TAIATANAIE PLIHVLETGS
AEAKENSAAT LFSLSVIEDN KVRIGRSGAI GPLVDLLGNG SPRGRKDAAT ALFNLSIFHE
NKGRIVQAGA VKYLVELMDP AAGMVDKAVA VLANLSTIPE GRTAIGQEGG IPVLVEVVEL
GSPRGKENAA AALLQLCTNV NRYCSQVLQE GAVPPLVVLS QSGTPRAKEK AQTLLSYFRN
HRQAAVEGSG DEASGDEASG PSGAGGLAIS GVGAAAGDLC FGFLLLLLLG VGAAAGDSCF
GFLLGAGAGT SGVVGGSAAG AGAAAGGDLA GGELTGALAG GELSGVGNGG ETVAVGGVAT
GVGAAAGLGG ADAGVGEDLG VATGDGDLGL GAAAGVVAGG VAAGVAGELV GADDGACPPT
PATRRQMSAM VKMLFRSISL RLSSRRF
//
