ID A0A0D3FA18_9ORYZ Unreviewed; 303 AA.
AC A0A0D3FA18;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G31170.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART02G31170.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G31170.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART02G31170.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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; A0A0D3FA18; -.
DR STRING; 65489.A0A0D3FA18; -.
DR PaxDb; 65489-OBART02G31170-1; -.
DR EnsemblPlants; OBART02G31170.1; OBART02G31170.1; OBART02G31170.
DR Gramene; OBART02G31170.1; OBART02G31170.1; OBART02G31170.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_919418_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000026960; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF9; RING-H2 FINGER PROTEIN ATL56; 1.
DR Pfam; PF13639; zf-RING_2; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 99..141
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 234..276
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 303 AA; 32669 MW; 7CCE1591568E9852 CRC64;
MAAGATLSVL LLVAGVVLML VLHVVVVFWA LRRGVFLRGA FRVEERRDQR AAGLTPDEIA
VLPCHERKEA AHDVARGGLS AEQVGELPCH VVKEGGGECA VCLEAFQAGD RCRVLPRCEH
GFHARCVDSW LRQSRVCPIC RAEVEVSGYA GKPAAAVAEA RDNSNVFLVA GLSLVVVVHV
LVLLWALWWG YGRSRLALAR ARVVGQHDVA RGGLSAEQVG ELPCHVVKEG AGECAVCLEA
FRAGDRRRVL PRCEHGFHAQ CVDSWLRVSR LCPICRAEVA ASRGKEGDAP VAEAASLEIV
AER
//
