ID A0A445KZQ9_GLYSO Unreviewed; 1644 AA.
AC A0A445KZQ9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=D0Y65_009615 {ECO:0000313|EMBL:RZC16419.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZC16419.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZC16419.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC16419.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) 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:RZC16419.1}.
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DR EMBL; QZWG01000004; RZC16419.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000289340; Chromosome 4.
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; 4.
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; 1.
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:UP000289340};
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 152..448
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 531..564
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 600..632
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 746..778
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 779..811
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 80..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1644 AA; 180663 MW; BAEA964DA88694BF CRC64;
MKIPCCSVCQ TRYNEEERVP LLLHCGHGFC RECLSRMFSA SSDATLACPR CRHVSTVGNS
VQALRKNYAV LALLQSAAAA ANGGGGGRSN FDCDYTDDEE DGDGGREDED EEDDEKRRRN
SRESQASSSG GGCAPVIELG GGGGGGGAHN DLKLVRRIGE GRRAGVEMWM AVIGGGGGGE
GGGRQRCRHN VAVKKVAVAE GIDLDWVQGK LEDLRRASMW CRNVCTFHGT MRVEDSLCLV
MDRCYGSVQS EMQRNEGRLT LEQVLRYGAD IARGVVELHA AGVVCMNLKP SNLLLDANGH
AVVSDYGLAT ILKKPSCWKA RPECDSAKIH SCMECIMLSP HYTAPEAWEP VKKSLNLFWD
DGIGISSESD AWSFGCTLVE MCTGAIPWAG LSAEEIYRAV VKAKKLPPQY ASVVGGGIPR
ELWKMIGECL QFKPSKRPTF SAMLAVFLRH LQEIPRSPPA SPDNGLDKGS VSNVMEPSPV
PEMEVPQQNP NHLHRLVSEG DTAGVRDLLA KAASENGSNY LSSLLEAQNA DGQTALHLAC
RRGSAELVET ILECSEANVD VLDKDGDPPL VFALAAGSPE CVCILINRNA NVRSRLRDGF
GPSVAHVCAY HGQPDCMREL LLAGADPNAV DDEGESVLHR AIAKKYTDCA LVILENGGCR
SMAILNSKNL TPLHHCVAIW NVAVVKRWVE VATSDEIAEA IDIPSPIGTA LCMAAASKKD
HENEGRELVR ILLAAGADPS AQDSQNGRTA LHTAAMTNDV DLVKVILGAG VDVNIRNVHN
SIPLHLALAR GAKACVGLLL DAGADYNLKD DDGDNAFHIA AETAKMIREN LDWLIVMLMK
PDADIEVRNH SGKTLRDILE ALPREWLSED LMEALVNKGV HLFPTIFKVG DWVKFKRSVT
TPTHGWQGAK PKSVGFVQSV PDRDNLIVSF CSGEVHVLAN EVIKVVPLDR GQHVHLKEDV
KEPRFGWRGQ SRDSIGTVLC VDDDGILRVG FPGASRGWKA DPAEMERVEE FKVGDWVRIR
PTLTSAKHGL GSVTPGSIGI VYCIRPDSSL LIELSYLPNP WHCEPEEVEH VAPFRIGDQV
CVKRSVAEPR YAWGGETHHS VGRISEIEND GLLIIEIPNR PIPWQADPSD MEKVEDFKVG
DWVRVKASVS SPKYGWEDVT RTSIGVIHSL EEDGDMGVAF CFRSKPFSCS VTDMEKVPPF
EVGQEIHVMP SVTQPRLGWS NESPATVGKI LKIDMDGALN VRVTGRQNLW KVSPGDAERV
PGFEVGDWVR SKPSLGTRPS YDWNSVGRES LAVVHSVQDS GYLELACCFR KGKWITHYTD
VEKVPSFKVG QYVRFRTGLV EPRWGWRGAE PESHGVITSI HADGEVRFAF FGLPGLWRGD
PSDLEIEQMF EVGEWVRLNY NANNWKSIGP GSVGVVQGIG YEGDELDRSI FVGFCGEQEK
WVGPSSHLER FDKLFVGQKV RVKQYVKQPR FGWSGHTHAS IGTIQAIDAD GKLRIYTPAG
SKTWVLDPSE VEVVEEKELC IGDWVRVKAS ISTPTHHWGE VSHSSIGVVH RMEDEDLWVS
FCFTERLWLC KAWEMEWVRP FKVGDKVRIR DGLVTPRWGW GMETHASKGQ VVGVDANGKL
RIKFRWREGR PWIGDPADLA LDED
//
