ID A0A498KMP5_MALDO Unreviewed; 1342 AA.
AC A0A498KMP5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-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_034036 {ECO:0000313|EMBL:RXI09419.1};
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:RXI09419.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI09419.1, 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:RXI09419.1};
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:RXI09419.1}.
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DR EMBL; RDQH01000327; RXI09419.1; -; Genomic_DNA.
DR STRING; 3750.A0A498KMP5; -.
DR Proteomes; UP000290289; Chromosome 1.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16541; RING-HC_RNF123; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045737; RKP_N.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR Pfam; PF19322; RKP_N; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 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 75..268
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 1290..1328
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1342 AA; 151256 MW; 5305797FF2005148 CRC64;
MAEDGLRLGG LSSGLAVLLN GEGSKENSLK THLVSNCDDF GHRSVERSLE YVLGLPNKYV
SLLASPVDCN LVRCIIRNEF PKLHANSSVF RNRDGVCISG DGCTPHIIGL DESSIRGDIR
VIKPPSLIES LAMFSSARAN AFVWKGKWMY EIILETSGIQ QLGWATVSCP FTDHKGVGDA
DDSYAFDGRR VRKWNKEAEP YGQSWVVGDA IGCCIDLDCN EILFYRNGVS LGPAFHGIRK
MGPGSGYYPA VSLSQGERCE LNFGARPFRF PIESYLPLQA LPSLVPFATR LLHCLSRLLG
LHSVEQAKHS SVQKLRRLKR FVTHEELFYP VSRGVCEEIF SVLEADVWST GYIAWGPFLS
FMMEVFGLQI PHDYSSLDRV LDVFLEFEGS HLLFEHFINA LACGCKTALL VLEDCPCSGS
YPYLAVAIHI LRRQELMVLW WKSPDFEFLF EGFLSRKNPN KHDLESMIPS VSWPGSSEDV
SYESSMLLTT RALSEAVSKI EEKHRDLCHL VIQFIPPVTP PQFPGSVFRT VLQNLLLKNR
GADRNLPPPG VSSNSVLVSL YTVILHFLSE GFGMGDICGQ LKSSENGPDV GFLHRGGHRS
FPVGLFLRND PHRNDSSRLG GSFSHLSKSN RVYDEETELI RWEEGCMDDE ETRVTHSSIK
KPCCCSCYND DFTKISKYPI RYTAKGSRVH CSSIPERSAH VATECSTGSL NDEIEDKPSS
SYQSESEFSY RSVQHMRFVP RESNMSSATL SEEELLDVLL LLYHIGLAPN FKQASYYMSH
QSQSISLMEE ADKQIREKAC SEQLKRLKEA RNGYREEVID CVRQCAWYRI SLFSRWKQRG
MYATCMWTVQ LLLVLTKVDL LFLYIPEYYL EALVDCFHVL RKSDPPFVPS SIFIKQGLAS
FVTFVVTHFN DPRISSADLR DLLLQSISVL VQYKEYLSVF ESNEAATQRM PKALLSAFDN
RSWIPVTNIL LRLCKGSGFG SSKQGESSSS SVVFQRLLGE TCINDQELFS AFLNRLFNTL
SWTMTEFSVS VREMQKKSYP GLPLYAGSGR GECRLTLPPF MERLLPSLEP ETYRSWAKAL
AIVLEFQQKK CGVIFDLSCN LTKLLEFCTH AIPQAFLSGA ETNLRRLMEL VVFILNHITS
AEDAEFFDLS LRRLGQSIEK INRGMILAPL VGIILNLLNA SEHMECREHN DVVSIFASMG
CLDSFHCRFQ YLVDYNWVSS SLSLSLKSKF FLKLKLLLRS EFKCNDGTCR GDAYLVKIAQ
LENFLSLLSQ SQSQENAICR GEKDGDDGMC CICYAREADA QFSPCSHRSC YGCITRHLLN
CHRCFFCNAT VVDVVLISEK TG
//
