ID A0A444XG17_ARAHY Unreviewed; 344 AA.
AC A0A444XG17;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Ahy_B09g095750 {ECO:0000313|EMBL:RYQ88718.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ88718.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ88718.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ88718.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYQ88718.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SDMP01000019; RYQ88718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444XG17; -.
DR Proteomes; UP000289738; Chromosome b09.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd23145; RING-HC_SPL2-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022170; MUL1-like.
DR InterPro; IPR044247; SPL2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47355; E3 UBIQUITIN-PROTEIN LIGASE SPL2; 1.
DR PANTHER; PTHR47355:SF1; E3 UBIQUITIN-PROTEIN LIGASE SPL2; 1.
DR Pfam; PF12483; GIDE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 292..332
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 344 AA; 38554 MW; 65F12D774CF46FF4 CRC64;
MSSHDQVLAS LLSQIVLSFD GAVLGLALAY AAIRSIRNFT TNSASLRKLR RAPSVSVSDL
RSLLSDSDGN SDDGGIVVVR GTVEPKAAVD GSWKSLRPSL LVSRESGDKA VVLQITQTCI
YNEWKGLFGW TSDLRAIFAR SWRQPESKFL RKVPFVLVDV GRQPSTEYVV VNLDGSRHPL
PLTTVYHKLQ PINASPYTFL QALFGHEYPV GLLEEEKILP VGKDITAVGL CSVRNGIPEI
KSCKDLPYFL NWNKWMQWKE QRQRQQQRQA VIDEVDPQVD EQNEDIADGQ LCVICLMRRR
RSVFVPCGHL VCCQGCAISV EREVAPKCPV CRQEIRQSVR IFES
//
