ID A0A067L7R5_JATCU Unreviewed; 1617 AA.
AC A0A067L7R5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=JCGZ_24549 {ECO:0000313|EMBL:KDP40550.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP40550.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP40550.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP40550.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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; KK914327; KDP40550.1; -; Genomic_DNA.
DR RefSeq; XP_012068697.1; XM_012213307.1.
DR STRING; 180498.A0A067L7R5; -.
DR GeneID; 105631247; -.
DR KEGG; jcu:105631247; -.
DR OrthoDB; 645118at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
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; 2.
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; 8.
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; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
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:UP000027138};
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 130..420
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 504..537
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 538..570
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 573..605
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 719..751
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 752..784
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1617 AA; 177807 MW; 298FE167C8EDE146 CRC64;
MKVPCCSVCQ TRYNEEERVP LLLQCGHGFC KDCLSRMFSA SLDTTLVCPR CRHVSVVGNS
VNALRKNYAV LALLHSPAAV SAPNFDCDYT DDEEDEDNVE EEEERCSRGS HASSSGGCGP
VIEVGVHPEV KLVRKIGEGR RAGVETWAAV IGGGIHGKCK HRVAIKRVEV GEDMEVEWVQ
GQLENLRRAS MWCRNVCTFH GMVKMDGCLG LVMDRFCGSV QSEMQRNEGR LTLEQILRYG
ADIARGVAEL HAAGVVCMNI KPSNLLLDPS GRAVVSDYGL AAILKKPACR KARSECESAK
IHSCMDCTML SPHYTAPEAW EPVKKSLNLF WDDAIGISAE SDAWSFGCTL VEMCTGSIPW
AGLSAGEIYR AVVKARKLPP QYASVVGVGM PRELWKMIGE CLQFKASKRP SFNAMLAIFL
RHLQELPRSP PASPDNSSFA KYAGSNVTEP SPASDLEVLQ DNPSHLHRLV SEGDVRGVRD
LLAKAASGNG GGSLSILLEA QNADGQTALH LACRRGSSEL VGAILEHRQA NVDVLDKDGD
PPLVFALAAG SPECVRALIE RGANVGSRLR DGFGPSVAHV CAYHGQPDCM RELLLAGADP
NAVDDEGETV LHRAVAKKYT DCALVILENG GCRSMAVRNS KNLTPLHLCV ATWNVAVVKR
WMEVASLEEI AGTIDIPSPV GTALCMAAAV KKDHENEGRE LVRILLAAGA DPTAQDAQHG
RTALHTAAMA NDVELVNIIL KAGVDVNIRN MHNTIPLHVA LARGAKSCVG LLLSAGASCN
LQDDEGDNAF HIAADAAKMI RENLEWLIIM LKNPGAAVEV RNHSGKTLRD FLEALPREWI
SEDLLEALMN RGVHLSPTIF EVGDWVKFKR SVTTPTYGWQ GAKHKSIGFV QSVVDKDNLI
VSFCTGEARV LASEVVKVIP LDRGQHVKLK PDVKEPRFGW RGQSRDSIGT VLCVDDDGIL
RVGFPGASRG WKADPAEMER VEEFKVGDWV RIRPALTTAK HGLGLVTPGS IGIVYCIRPD
SSLLLELSYL PNPWHCEPEE VEPVAPFRIG DRVCVKRSVA EPRYAWGGET HHSVGRISEI
ENDGLLIIEI PNRPIPWQAD PSDMEKVEDF KVGDWVRVKA SVSSPKYGWE DITRNSIGII
HSLEEDGDMG VAFCFRSKPF CCSVTDVEKV PPFEVGQEIH VMPSVTQPRL GWSNESPATV
GKIVRIDMDG ALNARVAGRH SLWKVSPGDA ERLSGFEVGD WVRSKPSLGT RPSYDWNSIG
KESLAVVHSV QETGYLELAC CFRKGRWITH YTDVEKVPCF KIGQHVRFRS GLVEPRWGWR
DAQPDSRGII TSVHADGEVR VAFFGLPGLW RGDPADLEIE QMFEVGEWVR LKEDAGNWKS
VGPGCIGVVQ GMGYDRDEWD GSTYVGFCGE QERWVGSTSH LEKVMRLMIG QKVRVKLSVK
QPRFGWSGHS HASVGTIAAI DADGKLRIYT PVGSKTWMLD PSEVELVEEE ELHIGDWVKV
RASVSTPTHQ WGEVNHSSIG VVHRMEDGEL WVAFCFTERL WLCKAWEMER IRPFKVGDKV
RIREGLVTPR WGWGMETHAS KGRVVGVDAN GKLRIKFQWR EGRPWIGDPA DIVLDES
//
