ID A0A0L9UQV9_PHAAN Unreviewed; 596 AA.
AC A0A0L9UQV9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=HKW66_Vig0159370 {ECO:0000313|EMBL:KAG2375909.1},
GN LR48_Vigan06g025300 {ECO:0000313|EMBL:KOM44947.1};
OS Phaseolus angularis (Azuki bean) (Vigna 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=3914 {ECO:0000313|EMBL:KOM44947.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM44947.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM44947.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2375909.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2375909.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000256|ARBA:ARBA00007930}.
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DR EMBL; JABFOF010000010; KAG2375909.1; -; Genomic_DNA.
DR EMBL; CM003376; KOM44947.1; -; Genomic_DNA.
DR RefSeq; XP_017427841.1; XM_017572352.1.
DR AlphaFoldDB; A0A0L9UQV9; -.
DR STRING; 3914.A0A0L9UQV9; -.
DR EnsemblPlants; KOM44947; KOM44947; LR48_Vigan06g025300.
DR GeneID; 108336052; -.
DR Gramene; KOM44947; KOM44947; LR48_Vigan06g025300.
DR KEGG; var:108336052; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 7846at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053144; Chromosome 6.
DR Proteomes; UP000743370; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd01923; cyclophilin_RING; 1.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF1; RING-TYPE E3 UBIQUITIN-PROTEIN LIGASE PPIL2; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KAG2375909.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 35..108
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 354..501
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 506..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 65101 MW; 25018AD69A00EFA2 CRC64;
MGKKQHSKDR MFITKTEWAT EWGGAKSKDS RTPFKRLPFY CCALTFTPFE EPVCTAEGSV
FDIMNITPYI IKYGKHPVTG TPLKLPDLIP LTFHKNSEGE YHCPVLNKVF TEFTHIVAVK
TTGNVFCYEA VKELNIKTKN WKELLTDEPF TRNDLITIQN PNALDDRVLL DFDHVKNDLK
VDDEELQKMS SDPTYNINMS GDIKQMLQEL GTDKGKETAM HGGGGGKAQK ERAAALAAII
AARSRVDEDS KSNANKDAKA PQAFSIVDAA SAAVHGRSAA AAKASSGDKT AARIAMHMSG
DRAPVNAKMV KSRFTTGAAS RSFTSTSFDP VTKNEFEYVK VEKNPKKKGY VQLHTTHGDL
NIELHCDITP RTCENFITLC ERGFYNGVAF HRSIRNFMIQ GGDPTGTGRG GESIWGKPFK
DELNSKLVHS GRGVVSMANS GPHTNGSQFF ILYKSANHLN FKHTVFGVVV GGLTTLAAME
KVPVDDNDRP LEEIKITSVT IFVNPYTEPD EGEEHDNATE KNVEDEDNGK VGSWFSNPGA
GTSESGSTGV GGGVGKYLKA RNAQATSANL DTSTAVVGKK RKVGVASSDF KDFSAW
//
