ID A0A498HUL5_MALDO Unreviewed; 563 AA.
AC A0A498HUL5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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_012257 {ECO:0000313|EMBL:RXH72573.1};
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:RXH72573.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH72573.1, 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:RXH72573.1};
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 -!- 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:RXH72573.1}.
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DR EMBL; RDQH01000341; RXH72573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HUL5; -.
DR Proteomes; UP000290289; Chromosome 15.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF136; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 506..547
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 60352 MW; F4015C9F9824CB49 CRC64;
MDEFSGKRAE NGLISKKGSG LGLRETANRD RNAQLCSRLG CSGRLNSVKS AQVEKAKPSR
PAFRSSSSGK EIIGSSSRSC VGVGNTRNSI AEPYKKLSFN LDTDSSETSS VQDDPEVSEI
APPPGKIQGG LHLESKNSVS SEITLMEVGS SRVESNTRSR RSFNQRSGLR SQDSIVGSSV
STGPKGTIQT RASTARNGLR SLRCSSVSDV VPSSCSSSDS SLGRRETIKK RTSEGESSSA
AKGKKMNGSS SAQNSNSSHG ISISDSRRAR NMPSNRDSNG VASVRTRRTV TGHSRGRLLP
NQGSGNNSTS NGFSAVGPHT SQPEMSINSN ASSSSQQLSA EVPLIRQNSY SRPGSSSGTL
HGILRAGASD VGFSRSLMNQ DGLRRYNMDG IAEVLLALER IEHDEELSFE QILVLETNLF
LNGLNIYDHH RDMRLDIDNM TYEGASEPFV MISASELLAL EERMGTVSTA LPEEALSDCL
KKSIYQSAPQ EDASVSCDGK KEDVKCSICQ EEYVAGDEVG RLRCEHSFHI VCVNQWLRLK
NWCPICKAAA APAPAPSPSL PST
//
