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Database: UniProt
Entry: A0A0S3QX37_PHAAN
LinkDB: A0A0S3QX37_PHAAN
Original site: A0A0S3QX37_PHAAN 
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
//
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