ID A0A1E5VYD3_9POAL Unreviewed; 752 AA.
AC A0A1E5VYD3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BAE44_0008857 {ECO:0000313|EMBL:OEL30125.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL30125.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL30125.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL30125.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) 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:OEL30125.1}.
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DR EMBL; LWDX02026275; OEL30125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5VYD3; -.
DR OrthoDB; 7537227at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095767; 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:000627; RING-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
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:SF237; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 6.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000095767};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 147..221
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 480..522
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 521..563
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 562..604
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 603..644
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 242..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..386
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 81943 MW; 553C6A980DD3DDAB CRC64;
MILANYYMKV TQVESLITEM QKYVFEVCQI VNSLMLPSET NCISVYLEKA KQFHFEKMTA
VIGEASRDLA GKVMPKSETL TNIQVLLSLS TNQELLMEAV ALSKIKMRVS SEDSADLDGI
NDLSKLVNYM LDKHVEEKQM HSINGVPIPA DFCCPLSLEL MSDPVIVASG QTYERVFIRK
WLDLGYNVCP KTRQTLGHTN LIPNYTVKQL IENWSEIHGI MLPDPVELLS LSFPVSLNLT
NDSTSDKSRL SDNSPRSNKS GSPEHKVSSD DSHHHNLRHD DSDSDDQISK ASSFEDTDDS
ESDALRLPLA ATEANKSTCN KTIDGYEAIK QLRKYGLHVS DVEQHLPSSG SSSDIGTGTS
SSSNHLEAVA KHEEEQFSSN SSASESTRND QMVTSSKVEP NGMPRFGGVR SRSQLVWRQL
SDKAVPADSR SESPDVDVKV RRLIEDLKNE STELQRAATG ELLVLSRHSM ENRIAIANHG
AIPFLVSLLY SADPSLQESV VTVLLNLSIN DNNKIAIASA NAIEALIHVL ETGSPEAKAN
SAATLFSLSV NEENKAEIGR SGAIKPLVDL LQEGNAQGKK DAATALFNLS IFHENKARII
EAGAVKPLVE LMDPAAGMVD KAVSVLAILA TVQEGRNGIA QAGGIPMLVE VVELGSARAK
ENAAAALLQL CTNNSRFCSL VLQEGAMPPL VALSQSGTAR AREKVLLHLQ SLSCWHKLTL
SVLHRFSLAF FATSAKLARS LDGKFRSCRA LV
//
