ID A0A8J5HPJ3_ZINOF Unreviewed; 849 AA.
AC A0A8J5HPJ3;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, 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=ZIOFF_017908 {ECO:0000313|EMBL:KAG6520847.1};
OS Zingiber officinale (Ginger) (Amomum zingiber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC Zingiber.
OX NCBI_TaxID=94328 {ECO:0000313|EMBL:KAG6520847.1, ECO:0000313|Proteomes:UP000734854};
RN [1] {ECO:0000313|EMBL:KAG6520847.1, ECO:0000313|Proteomes:UP000734854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Rhizome {ECO:0000313|EMBL:KAG6520847.1};
RA Zhang R.-G.;
RT "Plant Genome Project.";
RL Submitted (AUG-2020) 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:KAG6520847.1}.
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DR EMBL; JACMSC010000005; KAG6520847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J5HPJ3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000734854; 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; 1.25.10.10:FF:000082; RING-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000562; 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; 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; PF25598; ARM_PUB; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000734854};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 171..245
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 448..490
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 530..572
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 92166 MW; 80094E6B88F43267 CRC64;
MAFNPFHDNG NDDTSNNGHF TVDYPNHRII TIVEEEDYKE PYEAAPIYDE YDEEGFADGN
QCDKIYSSTH EICQLVTSAL PSPVDSMAVK CIKELQCTDE KQISIVIEKA IRDQSDNGSS
SSEYLDMISN SLSLLSNEEL LIEVVTLKKL KVKFACSYTK IHQLHSINGV SVPADFCCPL
SLDLMSDPVI VASGQTYERA FIRKWLDQGI NVCPRTHQTL GHSNLIPNYT AKALIANWCK
SNDIKLPDPL NLTRAPESYG KANSHKDAHS SNGLTSQETC VSEKNGSPQH SSSSNVATLQ
MANGLEAHHS GVSLATTETN NEFSVELRNA RSGSQIVSQS EQDLTDDSLE QPGDANLVSW
VSSDLTHYSS DASGELAQDS QASSAPQREP KFPLGFVEAR SRSVESEIRK LIEGLKSDSV
DIQRNATGEL RLLARHNMDN RIVIANCGAI SLLVGLLYST DPQTQENAVT TLLSLSINDN
NKIAVGNANS IDPLIYVLET GNAEAKENAA ATLCSLSVIE ENKVRIGRSG AIAPLVELLA
NGTPRGKKDV ATALFNFSIF HENKARIVQA GAVRYLVELM DPAAGMVDKA VAVLSNLATT
PEIRIQSLLC KSLKTTYQLC MISINIISKH FATTVHAKRV ESLDLKHTDR GLLVDHGHTL
RSEVAGHLDV LLSETALLVE GPQIRRVIEN DLVATGSLGV IPKEPDHPLP QVPAAEGGID
DDVLDVADLP STAEELPLHE DAAGGDYSSA GPVLRDDDEV VVTEGGEFGE ASAEISVRQR
RSGGAELGEK IHEALGVIGD LKTAEREDKI VFLAIALHRS LVHFAGLRRE ETLDEPQQIN
RGFHLGDIT
//
