ID A0AAD8VAL7_LOLMU Unreviewed; 330 AA.
AC A0AAD8VAL7;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=QYE76_016900 {ECO:0000313|EMBL:KAK1598101.1};
OS Lolium multiflorum (Italian ryegrass) (Lolium perenne subsp. multiflorum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type);
OC Loliodinae; Loliinae; Lolium.
OX NCBI_TaxID=4521 {ECO:0000313|EMBL:KAK1598101.1, ECO:0000313|Proteomes:UP001231189};
RN [1] {ECO:0000313|EMBL:KAK1598101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=02402/16 {ECO:0000313|EMBL:KAK1598101.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAK1598101.1};
RA Chen Y., Copetti D., Kolliker R., Studer B.;
RT "A chromosome-level genome assembly of Lolium multiflorum.";
RL Submitted (JUL-2023) 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:KAK1598101.1}.
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DR EMBL; JAUUTY010000620; KAK1598101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD8VAL7; -.
DR Proteomes; UP001231189; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR CDD; cd16667; RING-H2_RNF126-like; 1.
DR FunFam; 3.30.40.10:FF:000022; E3 ubiquitin-protein ligase RING1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF208; E3 UBIQUITIN-PROTEIN LIGASE RING1-LIKE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; Zn_ribbon_19; 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:UP001231189};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 204..245
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 255..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 34014 MW; 2B229C5A10DC615A CRC64;
MSSSSSPPPP PPPPQRYYCH QCDCAVPIPA PASPDDDVFC PLCAGGFVEE LLDENPSSPP
PPQSPFFPLS SFLDLRHPSD LAGVLGPPSP SAPRASASPS AAQFDVTDFL HGHLGGILSG
GATIQIVLEG SSFPAGAVFG GGGAGGLNLG DYFMGSGLEQ LIQQLAENDP NRYGTPPTAK
AAVAALPDVA VSADMMAADG GAQCAVCMDD FELGAAAKQL PCNHVFHKDC ILPWLELHSS
CPVCRHELPT DDPGYDNRQA SAAPAAAAPA SPGAPSPRVM ERRFRISLPW PLRAAFGGHA
AESGDPGSQD AADGSGDNNN DAHRSYDDLD
//
