ID A0A383VB24_TETOB Unreviewed; 665 AA.
AC A0A383VB24;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=BQ4739_LOCUS2667 {ECO:0000313|EMBL:SZX62140.1};
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX62140.1, ECO:0000313|Proteomes:UP000256970};
RN [1] {ECO:0000313|EMBL:SZX62140.1, ECO:0000313|Proteomes:UP000256970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cai Z.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNXT01000204; SZX62140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383VB24; -.
DR STRING; 3088.A0A383VB24; -.
DR Proteomes; UP000256970; 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; cd22586; Rcat_RBR_ARI1-like; 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; 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; 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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000256970};
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}.
FT DOMAIN 273..486
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
SQ SEQUENCE 665 AA; 74278 MW; D766A1D8C3D78339 CRC64;
MAAVLGSRRQ AFASSTRSSS CAAPRIAAVR TPSRRTSHKV RAIELDFSDP DTQLSMAGLA
LGLLFGIGAP AWYINRTERD EERLEELRAM NRATYKETGE YMTDEEIAQV RKPKWTDRRS
SFGTSVLLHR CLPGNSGAAS MGPGSVHMAD AEGSEISQDY SDLSSEYSYS SNDETDLGLA
EATTTKERPP YRIIDADMLK KVQAEAVSDL ETIWSCKKSV AKALLMYYRW DKERLLTDLA
EKGPELVYKT AGVAEQANNR AEPGAGSSSS QQEQVTCDVC MCENSCSECS SNGCGHTFCN
TCWRGHLAVQ IADGQARHIS CMAYKCGVVC DDELVLHVMK GEPELLSKYK QSHLESYMED
NERVAFCPSV PWCGHAVEVD SDPFVEPECP CGIAFCFKCG KAPHSPCTCD MWLLWDEKIN
GDSETRNWLA ANTKPCPKCS KPVEKNGGCN LVMCKCGQAF CWLCGGATGT RHTWTQIDNH
SCGRYKDEAD ARINDALRSH KRYMHYFERY KQHLDSLTKE KNNRAKLTSR IAAAEHDGTE
SRDFSWLVKA LDQLRTARQV LSNSYAFAYF FFGGQLYAEE FSEDENRVNQ NLFEDSQEML
AGEVERLSGL VERAKELTLD PQLRLDAINS SVNINSRIVK FFELVENDLY GKLQSSSAQI
AVYRA
//