ID A0A0S3QX37_PHAAN Unreviewed; 972 AA.
AC A0A0S3QX37;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-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 Name=Vigan.01G027800 {ECO:0000313|EMBL:BAT72836.1};
GN ORFNames=VIGAN_01027800 {ECO:0000313|EMBL:BAT72836.1};
OS Vigna angularis var. angularis.
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; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT72836.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT72836.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015034; BAT72836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3QX37; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291084; Chromosome 1.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47446; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR47446:SF2; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 30..105
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 729..762
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 938..972
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 107777 MW; 03A26B8DC9BF1076 CRC64;
MQTIFKQSSG SPDYPMADFD NPLHEIGKHA PPKDFVCPIT SHIFDDPVTL ETGQTYERKA
IEEWFNRGNL TCPITRQKLQ NTQLPKTNYV LKRLIASWKD RNPHLVQPPY ESPYEDTEAV
VQSTTASTSP NSVITQATVD GMMSELRCAI NNLYMSEVLK ESEMAVLQVE KFWRGVNIGV
DIHRMLVKPA VINGFMEILF NSVEPQVLQA AVFLLAEMGS RDNAVIETLT RVKTDVECIM
ALFKNGLTEA VVLLHLLNPP ITSLAEMAIV ESLITVLNTK EEESVTMCLK PKTAAVLLLA
RITRSSEEII ASSVVNTLFS ENAIGTIASS FGADLAKERI AAVEILLRCM EEDGTCRKNI
ADKAELSPLM ETLIGADDGE RFKIIQFFAE LVKLNRRTFT EQILHIIKEE GPFSTMHTLL
IYLQAAPHDH CPVMAGLLLQ LDLLDEPRKM SVYREEAMDT LIACLRNTDF PVTQLAAADT
IMSLQGSFDF FGNPLCREVL LKRAGIDKSS RNLVLVGHQI SNSSPEIDIT PEDEKAADDS
ERRIAYVLVS HEFGTIFEAL ADGMKGRNPE LRSACFISAT WLTYMLSILP DTGIQVPARA
CLLKQFIAKF NSARDVEDRI LSMVALNSFL QFPEGLGDLT SYTKDILRGL RELKRSCPLA
SKMLKSLVEE NESKADIWIH KELIKEDCSE NGEVVSVTCF KDKIFSGHTD GTIKVWTLKN
NLFHLLQEIQ EHTKAVTNLV ISESGDRLYS GSLDRTSKVW SIGKAAIHCV QVYDMKDQIH
NLVVTNSLAC FVPQGAGVKV QTLNGESKVL NSSKYVKCLT HVDGKLYCGC HDSSVQEIHL
ATGTVNTIQS GYKRLLAKAN PIHAIQIHGE FIYAAGSSMD GSSIKIWNSS SYSMVGSLQT
GSEVRTMAVS SGLIYLGCKG GTVEIWDKKK SSKVDTLQMG TNCRVNCMAL DRNEEVLVTG
TSDGQIQAWE MN
//