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Database: UniProt
Entry: A0A498JJX7_MALDO
LinkDB: A0A498JJX7_MALDO
Original site: A0A498JJX7_MALDO 
ID   A0A498JJX7_MALDO        Unreviewed;      1001 AA.
AC   A0A498JJX7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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_024891 {ECO:0000313|EMBL:RXH95207.1};
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:RXH95207.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH95207.1, 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:RXH95207.1};
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   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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:RXH95207.1}.
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DR   EMBL; RDQH01000333; RXH95207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498JJX7; -.
DR   STRING; 3750.A0A498JJX7; -.
DR   EnsemblPlants; mRNA:MD07G0240600; mRNA:MD07G0240600; MD07G0240600.
DR   Gramene; mRNA:MD07G0240600; mRNA:MD07G0240600; MD07G0240600.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000290289; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   CDD; cd16571; RING-HC_SIAHs; 1.
DR   CDD; cd03829; Sina; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48102:SF6; CLP PROTEASE REGULATORY SUBUNIT CLPX1, MITOCHONDRIAL; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF03145; Sina_TRAF; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          662..698
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          715..775
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          79..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  111285 MW;  D5798B88CAE765CC CRC64;
     MAAALRSKPS RDTASSAASQ FRYFVFNYMH SGRVASSHYA HRTKSDDLFM NTPYHFTSFK
     PVLLGGNFVE KGSQIFDHPR ASRRASKNSD KNWGRKLSSS RCNGVMSSQG DPPEVWSGDG
     IVVRAAPGSN LVRGGGGGGG PNPGSGGGFD SNSKDENWGG SNLGRNFPTP KEICQGLDKF
     VIGQEKAKKV LSVAVYNHYK RIYHESLQKW SAGDSSNGKV DAMDDDRVEL EKSNILLMGP
     TGSGKTLLAK TLARFVNVPF VIADATTLTQ AGYVGEDVES ILYKLLTVAD YNVTAAQQGI
     VYIDEVDKIT KKAESLNISR DVSGEGVQQA LLKMLEGTVV NVPEKGARKH PRGENIQIDT
     KDILFICGGA FIDLEKTISE RRQDSSIGFG APVRANMRTG GVTDAAVTSS LLEIVESSDL
     IRYGLIPEFV GRFPILVSLS ALTENQLVEV LTEPKNALGK QYKKMFRMNG VKLHFTESAL
     RLIARKAISK NTGARGLRAI LENILMDAMY EIPDVRTGDD IIDAVVIDEE AVGLDGKGCG
     AKILYGKGAL DHYLSQNKPK DVEIAAKEGS DGEPEAETEL SSVVASMGRA MDLESIECVS
     SSDGLDEDEI HPHHNTTLHP HSHPHPHHHE FSKPRSNVTT NATIAGPTSI APATSVHELL
     ECPVCTNSMY PPIHQCHNGH TLCSTCKSRV HNRCPTCRQE LGDIRCLALE KVAESLELPC
     KYYSLGCPEI FPYYSKLKHE SVCNFRPYNC PYAGSECSVV GDIPFLVTHL RDDHKVDMHT
     GCTFNHRYVK SNPREVENAT WMLTVFHCFG QYFCLHFEAF QLGMAPVYMA FLRFMGDENE
     ARNYSYSLEV GANGRKLIWE GTPRSVRDSH RKVRDSHDGL IIQRNMALFF SGGDRKELKL
     RVTGRIWKEQ QNQDSGLSTF KRIPAQLHRH FWILSRLNFR LLHYVPPDQS VQLHSRQPHL
     HFLWPLQTLS RVLYSRTTWM EVRRRQQLLH FSLLLLLPPA P
//
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