ID A0A0D9VKM7_9ORYZ Unreviewed; 560 AA.
AC A0A0D9VKM7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G25650.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G25650.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G25650.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G25650.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0D9VKM7; -.
DR EnsemblPlants; LPERR02G25650.2; LPERR02G25650.2; LPERR02G25650.
DR Gramene; LPERR02G25650.2; LPERR02G25650.2; LPERR02G25650.
DR HOGENOM; CLU_006348_0_1_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000032180; Chromosome 2.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; 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:SF52; U-BOX DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF00514; Arm; 2.
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; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 184..258
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 319..361
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 402..444
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 156..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61186 MW; 03BA85975239BA8E CRC64;
MNQGNDAAIV GAGQVAPQDV ICNNVAIQFK FVTWQLQTVL ASLPQSRFQI SDEVQEEVDL
VRAQLRREME KKGEIDVNIF SKMHDILALP VSTIGSQSEQ SHGQPDTAQM ESLCNDHLEL
QNIITLVSEI SGVPKSDTKR ITSHLIEGLE NMRVTDSKRS VNVSQPSDET KGSPQTHKKS
DAVAIPEDFR CPISLELMRD PVIVSTGQTY ERAFIQRWID CGNRTCPKTQ QKLQNLTLTP
NYVLRSLILQ WCEEKGIEPP TRSKNDGSYL EVGGERVVIE TLVRNLSSSS LDERKSAAAE
IRSLAKKSTD NRILLAESGA IPALVKLLSS KDLKTQEHAV TSLLNLSIYD QNKELIVVAG
AIVPIIQVLR KGGMEARENA AAAIFSLSLI DDNKITIGST PGAIEALVEL LQSGSPRGRK
DAATALFNLC IYQANKVRAV RAGILAPLIQ MLQDSSRNGA IDEALTILSV LVSHHECKTA
IAKAHAIPFL IDLLRSSQAR NKENAAAILL ALCKKDAENL ACIGRLGAQI PLTELSKTGT
DRAKRKATSL LEHLSKLQVL
//