ID A0A0D9WG50_9ORYZ Unreviewed; 1625 AA.
AC A0A0D9WG50;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:LPERR05G12110.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR05G12110.1, 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:LPERR05G12110.1, 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:LPERR05G12110.1}
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 EnsemblPlants; LPERR05G12110.1; LPERR05G12110.1; LPERR05G12110.
DR Gramene; LPERR05G12110.1; LPERR05G12110.1; LPERR05G12110.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000032180; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd23140; RING-HC_KEG-like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR044584; KEG.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46960; E3 UBIQUITIN-PROTEIN LIGASE KEG; 1.
DR PANTHER; PTHR46960:SF1; E3 UBIQUITIN-PROTEIN LIGASE KEG; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18346; SH3_15; 7.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 6..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 139..434
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 514..546
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 582..614
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 728..760
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 761..793
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 76..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1625 AA; 177737 MW; 0FD04F1AD403EE26 CRC64;
MRVPCCSLCH VRYDEEERTP LLLHCGHGFC RACLARMLAN ATGAVLPCPR CRHPTAVGNS
VTALRKNFPI LSLLSSSPSS PSFLHSESGS SSDGSDDDDD DFFGRPTRRS SSAAAAPSSS
SLQPAAGCAS FDLASHPDLK LARRIGSGPP GPAGQEVWAG TLSRGGGGGG TKRCKHPVAV
KRVPVPAGDG LEGVQEEVER LRRAATWCRN VSTFHGAVRV GGHLCFVMDR YVGSVQTEMR
QNGGRLTLEQ ILRYGADIAR GVAELHAAGI VCMSIKPSNI LLDTNGHAVV SDYGLSAILK
NLTSRRVSDD SNMVGMDATL LSPNYTAPEA WGPLKKSLNL FWDSANGILP ESDAWSFGCA
LVEMCTGAVP WAGLSAEEIF KSVVKEKKPP PQYSRVVGVG LPGELWKMIG DCLQFKPSRR
PSFQDMLKTF LRYLLDIPRS PPASPENDFT NASLPNGIDA PPTSILDMVH DNPNALHHLV
CEGDAAGVRN LLAEAASDRN GCLIRSLLEA QNADGHSALH LACRRGSAEI VEAIVAYQEN
VDILDKNEDP PIIFAMAAGS PQCVRALVRR SSDINSRLRE GLGPTLAHVC AHHGQPECMR
ELLMAGADPN AVDGEGESIL HIAVAKRYTD CAIVILENGG CRSMAIPNSL NKTPLHLCIE
TWNADVVRRW VEVASIEEIA EAIDVPSPVG TALCMAAALK KEHEKEGREL VRILLAAGAD
PTAQDDPHCR TALHTAAMIN DAELVKIILD AGVDVNIRNA QNTTPLLVAL NRGANSCVGL
LLAAGANCNL QDDDGDNAFH IAADAAKMIR ENLSWIVQIG WTLRDFLERL PREWISEELM
ETLEDKDVHL SPTIYEVADW VKFRRTVTEP AFGWQGAGPR SIGFVQSVVD HDQLVVSFCS
GEARVLTSEV IKVIQLNRGQ HVQLKPDVLE PRFGWRGQSR DSIGTVLCVD DDGILRVGFP
GASRGWRADP AEIVRVEEYK VGNWVRIRPS LTVAVHGMES ITPGSVGIVY SIRPDSSLLL
GLCYLSSPWL CEPEEVEHVD PFKIGDQVCV KRSVAEPRYA WGGETHHSVG KIIDIESDGL
LIIDIPNRAQ SWQADPSDME KIENLKVGDW VRVKATVPSP KYGWEDVNRS SIGVVHSLEE
DGDMGVAFCF RSKPFSCSVA DVEKAQPFEV GEKIHVLPSI SQPRLGWSNE TAATIGAISR
IDMDGTLNVK VSGRNSLWKV APGDAERLSA FEVGDWVRFK SSIGSRPTYD WNLVGKTSIA
VVHSIQDSGY LELAGCFRKG KWLTHNTDID KVEPLKVGYH VQFRAGITEP RWGWRDAKPD
SRGIIAGVHA DGEVRVAFFG VPGLWKGDPA DLEIEQVYEV GEWVRLRNNA DDWKSLKPGS
IGVVHGIGYE DDIWDGTIHV AFCGEQERWI GPSSHLEGVT KFVVGQRVRV RLSVRQPRFG
WSNHNHSSIG TISSIDADGK LRIHTPAGAR AWLIDPAEVE KVEEEEEVCV GDWVKVKDCV
TTPTYQWGDV NHNSIGVVHR AEDGELWVAF CFCERLWLCK RWEVEKVRPF RLGDRVRIRP
GLVTPRWGWG VETYESKGEV VGVDANGKLR IKFRWRDGVW IGDPADIILD DIPSLTEEAS
NGFCS
//
