ID A0A059BJ50_EUCGR Unreviewed; 1125 AA.
AC A0A059BJ50;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EUGRSUZ_G032192 {ECO:0000313|EMBL:KCW65896.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW65896.1};
RN [1] {ECO:0000313|EMBL:KCW65896.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW65896.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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}.
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DR EMBL; KK198759; KCW65896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BJ50; -.
DR STRING; 71139.A0A059BJ50; -.
DR EnsemblPlants; KCW65896; KCW65896; EUGRSUZ_G032192.
DR Gramene; KCW65896; KCW65896; EUGRSUZ_G032192.
DR eggNOG; KOG0198; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR InParanoid; A0A059BJ50; -.
DR OMA; IVRVEEY; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR040847; SH3_15.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF18346; SH3_15; 6.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..115
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 198..231
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 232..264
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 267..299
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 412..444
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 445..477
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 123..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 123615 MW; 237365CBB5449DA9 CRC64;
MDCTMLSPQY AAPEAWEPVK KSLKFWDDAI GISGESDAWS FGCTLVEMCT GSAPWAGLSA
EEIYRAVVKG GRLPPQYASV VGVGIPRDLW KMIGDCLQFK ASRRPSFNSM LAIFLRHLQE
IPRSPPASPE NDFTRSSGSS LTEPLRGSVS DLVQDNTGRL HKLVSEGNVN GVRDLLAKAA
SGKINNSMSS LLKAQNPDGQ TALHLACRRG SAELVEAILE HHEAYVDVLD KDGDPPLVFA
LAAGSPECVH ALIRRGANVR SRLRDGFGPS VAHVCAYHGQ PDCMRELLLA GADPNAVDDE
GESVLHQAVA KKYTDCAVVI LECGGCPSMS IVNSKNLTPL HLCVATHNVT VVRRWVEVAS
TEDVENAIDI PSPVGTAVCM AAALKKDREL EGRELVRLLL AAGADPTAQD AHGRTILHTA
AMADDVELVK AILDAGVDVN IRDMHNMIPL HTALSRGAKS CVGLLLYAGA NYNLQDDDGD
NAFHIAAESA KMIRENLQWL IIMLRSPDAA VEARNHSGKT LRDFLEALPR EWISEDLMEA
LANRGVYLSS TMYEVGDWVK FKRSVKNPTY GWQGANHKSV GFVQGVPDKE KLIVSFCSGE
AHVLASEVVK VIPLDRGQHV KLKADVEEPR FGWRGQSRDS IGTVLCVDDD GILRVGFPGA
SRGWKADPAE MERVEEFKVG DWVRIRPGLT TAKHGLGAVT PGSVGIVYCI RPDSSLFLEL
SYLGTRWHCE PEEVEHVVPF RIGDRVCVKR SVAEPRYAWG RETHHSVGRI CEIENDGLLL
IEIPNRNMPW RADPSDMEKL EDFKVGDWVR VKASVPFPKY GWEDITRDSI GIVHSLEEDG
DMGVAFCFRS KSFSCSVTDM EKVPPFEVGQ EIRMKPSVTQ PRLGWSNETP ATVGKVVRID
MDGALNVKVA GRHSLWKVSP GDAEQLAGFE VGDWVRSKPS LGTRPSYDWN SIGKESLALV
HSVQETGYLE LACCFRKGRW ITHYTDVEKV PSFKVGQHVR FRAGLSEPRW GWRGAQPDSQ
GVITSVHADG ELRVAINGLP GFWRGDPADF EIVQTFEVGE WVRLKEKANS WKSIGPGSIG
VVQGLGYNGD EWDGSTIISF CGEQERWVGS TSHLERVEKL MVGRR
//
