ID A0A8T2VRN0_9CHLO Unreviewed; 1084 AA.
AC A0A8T2VRN0;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 02-APR-2025, entry version 9.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=NADE_007067 {ECO:0000313|EMBL:KAH7617282.1};
OS Chlorella desiccata (nom. nud.).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=1650286 {ECO:0000313|EMBL:KAH7617282.1, ECO:0000313|Proteomes:UP000693320};
RN [1] {ECO:0000313|EMBL:KAH7617282.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UTEX 2526 {ECO:0000313|EMBL:KAH7617282.1};
RA Biondi T.C., Eng W.L., Sanders C.K., Hovde B.T., Dale T.;
RT "High-quality genome assembly and phylogenetic analyses support the
RT reclassification of the oleaginous marine species Nannochloris desiccata
RT (Trebouxiophyceae, Chlorophyta), formerly Chlorella desiccata.";
RL Submitted (OCT-2021) to the EMBL/GenBank/DDBJ databases.
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:KAH7617282.1}.
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DR EMBL; JAGTXX020000014; KAH7617282.1; -; Genomic_DNA.
DR OrthoDB; 514333at2759; -.
DR Proteomes; UP000693320; 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; cd20336; Rcat_RBR; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
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:UP000693320};
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 468..704
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 472..530
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 268..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..283
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..325
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..741
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..833
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 115810 MW; D8B4A118DBC8580E CRC64;
MESIREGKEG VSTISVMPGT GAGAEAAVTR AVVTRALLPA DPLHIYTDDG HSTILHYICT
GQPVGALSRI LLGWPGGIRP SPASRERAAL LSSLLALYPE LLQLVCLQNT NKSLTPVHCC
VNTASVDVLR VLVTTAQKYL GRKNAALLLS VPDSLGRTAL CIAIASQQWE AVQLLLDTAA
LSHPGIQASY RIHQALGAEN DGDGFGSRKI RRRKTTGGST ISSLSFVAAG SGAGAVITGA
VGGVLNKIWD SWGGNAAEVD SIEKHRTELR EGSGSGSGGG GRGNTSNKTF ITKSKEDPLC
SSPSASSSPS TFSTTTITTS TVGTSQSSTP LAVKLPCVSV LGDLSAVQRR QRHQIDRVAG
LLNISISEAM EVLMKYNWDE AVALTVSIPS LQGEEKENGE DDEVRGAARK VPKPSFILGK
TANTTQEERS DAKQDRTNDG FHSAEEEDED ENKQGTENKE KERPQLKSRR TCMVCFEDVI
ESSTANNTKT NLSKVSTRYL PCFKDHFTCD TCWRGILDSN PQSACCPLCR LPLPLKAAEM
LLPKAKYQRV LQLVAEKYVQ TAHDLRWCPA AGCTMCLQLP GGESGKVAEM AAASGKGIDA
YCSYCTHSSC WSCGEGSHEP ASCTQASEWS AELANLRAMA PVSDQRWLAQ HAKRCPGCNA
FIQRTGGCNH MTCGCGKHWC WECGRDWSEH NADTGGFYFC SLVENEEGNA FDEEESEQES
GGRQQGSNNN SSNNNSTSSS SGWLRDIWRS VHNVAGEATL HRCLQMQLRH ECDEAAVRAV
AAYLQDICSK MRSSETFSEN HSSGVGTNDN DKKKIAGAGP PPSVGGSSSS SSSVIASGGS
TILLGPEQVG VSKREAAEMR APEWATVVAT ACCSAAEDGI FHPKNVLKSI LKISTTSAIK
TNRNDTIIST NPALNINFPA IASVIIEAHM TLKNSAAPLR ALPGGARRRY LVELCEETER
YLALVEPVLM DAPYQTEAIE VGRGLLSPTS SGAGAQPPQP PHLQQQQRGF RGALSSFIQN
IKGVPGLNYE CRIPGVDAHV IVEQAHYVAA VQRQATELNI GEHVAALQKG INGLKDAGRK
GLFA
//
