ID A0A6G1CT64_9ORYZ Unreviewed; 804 AA.
AC A0A6G1CT64;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=E2562_026556 {ECO:0000313|EMBL:KAF0903269.1};
OS Oryza meyeriana var. granulata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza meyeriana.
OX NCBI_TaxID=110450 {ECO:0000313|EMBL:KAF0903269.1, ECO:0000313|Proteomes:UP000479710};
RN [1] {ECO:0000313|EMBL:KAF0903269.1, ECO:0000313|Proteomes:UP000479710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Menghai {ECO:0000313|Proteomes:UP000479710};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF0903269.1};
RA Li W.;
RT "Whole genome sequence of Oryza granulata.";
RL Submitted (NOV-2019) 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:KAF0903269.1}.
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DR EMBL; SPHZ02000008; KAF0903269.1; -; Genomic_DNA.
DR EMBL; SPHZ02000008; KAF0903270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1CT64; -.
DR OrthoDB; 10064100at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000479710; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; USP_STK_Ubox_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR051348; U-box_ubiquitin_ligases.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR006016; UspA.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF15; U-BOX DOMAIN-CONTAINING PROTEIN 35; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00582; Usp; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000479710};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 451..714
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 734..804
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 185..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 804 AA; 89846 MW; CE8F2FF3FD6A27CD CRC64;
MEIEEAAAAG DGELEMEAPS VSTVAIAVNG SKNSRHALKW ALDKFVPEGR VLFRILHVRP
TIKMVPTPMG NFIPITQVRE DVATAYRKEV EWQANNMLLP YKKMCAQRKV EAEAVLLESD
DVPTTISEEI RKFSVCKLVL GSSSSIFRRK LKGSRTATKI CECIPSFCTA YVVSKGKLSS
VHSATSDAVE TPESISSSTV SSPSSRSFSS SAPSEWGDTY GSANVSFHQP SLSSQRDQAL
ANMNRSSDRT ASPSGSGGSE ISYHDDTVLT SSHSVNSEAQ FSSSSSGNSI YKSFPRDHSF
GNSDQTSVSD IATNLKHSHD QDYLKLEIER LRVKLRHLQK LNELAQNESF DANQKLHKLG
IQNIEDEIRL KETELTEEKV RRLIRKKERE EQEVATREDQ FKNDNAEREA KQSNDNQEDD
KNKTGERIFG RCFDEYNRYT WEEIQASTSS LSDDLMIGKG SYGTVYKAKF HHTVAAVKVL
NSPEGCGTQQ LQQELEVLGK IRHPHLLLML GACPEHGCLV YEYMENGSLD DMLQRRNNTP
PLTWFDRFRI AWEVAAALMF LHSSKPEPII HRDLKPANIL IDRNLVSKIG DVGLSTLLPS
MDQYLSTMIK DTAPVGTFCY IDPEYQRSGV VSMKSDVYAL GIVILQLLTA KSPMGIAHVV
ETALEEGDFV DILDEAAGQW PLKEAQELAV LALKCAEMRR RDRPDLSDHV LPALERLKDV
ATKAKETALH GQTAPPSHFI CPILQEVMVD PYVASDGYTY DRKAVELWLS MNDKSPMTNL
RLPHKSLIPN HSLRSAIMDW RSKS
//
