ID A0A8J4V2L8_9MYCE Unreviewed; 680 AA.
AC A0A8J4V2L8;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=CYY_009784 {ECO:0000313|EMBL:KAF2068894.1};
OS Polysphondylium violaceum.
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Polysphondylium.
OX NCBI_TaxID=133409 {ECO:0000313|EMBL:KAF2068894.1, ECO:0000313|Proteomes:UP000695562};
RN [1] {ECO:0000313|EMBL:KAF2068894.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=QSvi11 {ECO:0000313|EMBL:KAF2068894.1};
RA Narita B., Kawabe Y., Kin K., Saito T., Gibbs R., Kuspa A., Muzny D.,
RA Queller D., Richards S., Strassman J., Sucgang R., Worley K., Schaap P.;
RT "Development of genomics and gene disruption for Polysphondylium violaceum
RT indicates a role for the polyketide synthase stlB in stalk morphogenesis.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:KAF2068894.1}.
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DR EMBL; AJWJ01000805; KAF2068894.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000695562; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000695562};
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 283..492
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 287..334
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..60
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..87
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..137
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 77797 MW; 4112DEFDB628915D CRC64;
MFYKLKKILS PNGKKKKSSS SSASSNVVKN SNENSSYNSY DDIDNKNYKS QTSSSSLDAS
SEVENENETK INPIITTTTT TTTTTTTNSL NDDEKKPPTT ITITPSSSFL RTVSSQLLNI
KKNISSNNNS SKIDNNSPKT TIKVNGDEDD QDDACNQSKD DNQDDETNES FIDNDEEYSD
NDDDDDDEFI GFQDIEKESD KNFNCLSPEE LKLQQQKEIK EIAELLSIPM SSAITLLKHF
NWKKEILILK YIESPKEISK ELGIEYNSNN NNNNGNNNNN NDTIISCSIC GDENNLQEFT
KIKCNHYFCN DCWGGYLVLK ITEGEATIRC PSHKCNSVVQ DTIIQRLVAP VLYEKYQSFA
TKKFIQQNQK HIRYCPTPGC DNTITLRNDT VSSTTSVQCS CGFKFCFQCH RQSHLPATCE
QMALWETKCQ DESETSHWKT ANCKECPKCK VAVEKSGGCN HMVCKHCQYE WCWNCLSVWK
GHNDFYVCKK TLSSKATKKN QDALKEIEKS KLELSRYLQY YERYQFHEKA RHQEKSIREQ
AQTKMRELER SSTWAEVQFI EKGIDQLLDC RNVLKFTWIY SFYSFPNSNI SISTPTPSTT
NTTTSTSTSQ DDNAKYLFEF LQNDLEKSTE KLSDLMEDIL KKSNTLDQPL RLEIMNQISL
LKSKKDGLLD AVSKDSLFEF
//
