ID A0A668ASU5_9TELE Unreviewed; 1036 AA.
AC A0A668ASU5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=Ankyrin repeat and IBR domain-containing protein 1 {ECO:0000256|ARBA:ARBA00069741};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ANKIB1 {ECO:0000313|Ensembl:ENSMMDP00005051869.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005051869.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005051869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMMDP00005051869.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00008278}.
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DR AlphaFoldDB; A0A668ASU5; -.
DR Ensembl; ENSMMDT00005052881.1; ENSMMDP00005051869.1; ENSMMDG00005023419.1.
DR GeneTree; ENSGT00940000157621; -.
DR Proteomes; UP000472263; Chromosome 16.
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; cd20361; Rcat_RBR_ANKIB1; 1.
DR CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR FunFam; 1.20.120.1750:FF:000003; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 1.25.40.20:FF:000040; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000129; RBR-type E3 ubiquitin transferase; 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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR InterPro; IPR047563; RING-HC_RBR_ANKIB1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR003903; UIM_dom.
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; PF00023; Ank; 2.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
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 REPEAT 45..78
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 145..177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 328..568
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 332..378
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..807
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 116290 MW; 7C4D614DF6BFEEF5 CRC64;
MGNTATKFRK ALINGDELLA CQLYDSNPQF KDALDPNATY GEPYQHNTPL HYAARHAMAR
LLRSFLLSKD GNPNKRNVHN ETSLHLLCMG PQILTSEGAL HPRISRPYED EQRRAECLQI
ILTWTGAKLD QGEYESADVN ATDNKKNTCL HYAAASGMKT CVELLVQRDG DLFAENENRE
TPCDCAEKQH HKELALSLES QMVFSLAPEA EGIEAEYAAL DRRELYEGLR PQELRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMTNAEE CCQRSGVQMP NPPPSGYNAW
DTLPSPRTPR TTRSSITSPD QISLTPADED SCGICLSSIS VFEEPVDMSC GHEFCRACWE
GFLNLKIQEG EAHNIFCPAF DCFQLVPVEV IESVVSREMD RRYLQFDIKA FVENNPAIRW
CPQAGCERAV RLNTQGPGST TSDPLSFPLL RAPAVDCGKG HLFCWECQGE AHEPCDCETW
KMWLQKVTEM RPEELAGVSE AYEDAANCLW LLTNSKPCAN CKSPIQKNEG CNHMQCAKCK
YDFCWICLEE WKKHSSSTGG YYRCTRYEVI QQVEEQSKEM TVEAEKKHKS FQELDRFMHY
YTRFKNHEHS YQLEQRLLKT AKEKMEQLSR ALSGREGGPP DTTFIEDAVL ELLKTRRILK
CSYPYGFFLE PKSTKKEIYE LMQTDLEMVT EDLAQKVNRP YLRTPRHKII RAACLVQQKR
QEFLASVARG VAPNDSPEAP RRSFAGGTWD WEYLGFASPE EYAEFQYRRR HRQRRRGDMS
SLRSNTPDPD DPSDSTLGIT GPLTGLGSLD DDDPNILLAI QLSLQDSGMA GGNANHEFIA
NEASLGAIGT SLPSRLEQSA PSVEVLHRAS LSSSELLDLG DSLARLGNIN ITSHESHHRI
YGGASSSSAA AANANLLGNI MAWFHDMNPQ GITLVPSTST STDVDTLHTT GGGCTQEEEK
AVRLSEAEEK EPAVTERPTH LDLVGLDYMA TVDTSGSHVE REGAKVCHID TPRCDSVSDQ
LPSTSSSEWE EQVHLV
//
