ID A0A835WV17_9CHLO Unreviewed; 542 AA.
AC A0A835WV17;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, 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=HYH02_001978 {ECO:0000313|EMBL:KAG2453768.1};
OS Chlamydomonas schloesseri.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=2026947 {ECO:0000313|EMBL:KAG2453768.1, ECO:0000313|Proteomes:UP000613740};
RN [1] {ECO:0000313|EMBL:KAG2453768.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCAP 11/173 {ECO:0000313|EMBL:KAG2453768.1};
RA Craig R.J., Hasan A.R., Ness R.W., Keightley P.D.;
RT "Comparative genomics of Chlamydomonas.";
RL bioRxiv 0:0-0(2020).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
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 -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:KAG2453768.1}.
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DR EMBL; JAEHOD010000003; KAG2453768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A835WV17; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000613740; 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; cd22583; Rcat_RBR_ARI7-like; 1.
DR CDD; cd23141; RING-HC_ARI6-like; 1.
DR FunFam; 1.20.120.1750:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 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 Pfam; PF13923; zf-C3HC4_2; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000613740};
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 127..344
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 131..177
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 62020 MW; 3D86BE45CED36808 CRC64;
MSDSDEEFRS GSEDEEMSDY GASDADMDVE DDDDDYGFAG AEEVSAVPKV PYKVLPKEEL
TKQREKALRE VQDVLGVDED TAMRLLRKYK WDASRVQEEW FSKYDQVRDS LGLIDEPGPS
GRPAAETEER CYICFDSYPV RDMRAAACKH YFCKDCWRGY ITQALSSGPA CLDLRCPSTE
CKKKVCVPSS LVMELASGEE QSKYSTYLVR SFVEDNSAMC WCTGKNCENA IQCLVDRGPN
EAMDVICSCS ATFCFNCKEE AHRPVSCETV TKWLTKNSAE SENMNWILAN TKPCPKCSRP
IEKNQGCMHM TCSQCRFEFC WLCQGDWKEH GERTGGFYAC NRFETAKKKG EYDDESRRRE
NAKASLERYM HYFERFDAHS KAREKARLDA SKVSKDWLEQ LADITKTPTS QLKFINEAWN
QIVECRRMLK WTYAYGYYAF EDADRNTEVA RHKGFFEFLQ GDAERSLERL HEAAEKDLGA
HVTKARNLAD GGFDVDAFQT FRKNLIGLTD VTAGFFDKLV KQLEKGFGSM EADYAGEKQV
KQ
//
