ID A0A667WZK5_9TELE Unreviewed; 1247 AA.
AC A0A667WZK5;
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=LOC115367637 {ECO:0000313|Ensembl:ENSMMDP00005005849.1};
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:ENSMMDP00005005849.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005005849.1}
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:ENSMMDP00005005849.1}
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; A0A667WZK5; -.
DR Ensembl; ENSMMDT00005006004.1; ENSMMDP00005005849.1; ENSMMDG00005003270.1.
DR GeneTree; ENSGT00940000165758; -.
DR Proteomes; UP000472263; Chromosome 11.
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; 1.
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; 1.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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 146..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 334..572
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 338..384
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 827..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..635
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 996..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1056
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1125
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 139685 MW; 8950DD241156DF93 CRC64;
MGNTATKFRK ALVSGDEALA WQLYEGNPQF REGLDPNASY GEQYQHNTPL HYVCRHAMTR
LLRSFLYSKE GNPNKRNVHN ETCLHVLCQG PQILLLPEGA LSPRLARPQR DEQRRADCLQ
MILSWTGARL DRGQYERANV NATDNHHSTC LHYAAAAGMK SCVELLIQSE ADLFVEDEDK
LTPCDHAERQ HHTELALSLE SQMVFSSSSA HASALDKLSS LPQDPYEGLK LQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSDSEG CCQRSGVAMP TPPPSGYNAW
DTLPSPRTPR TPRSPLTLTL TSPTDSCLTP AEEGLTTCGI CLCSISVFED PVDMSCGHEF
CRACWEGFLN VKIQEGDAHN IFCPAYDCYQ LVPVHVIESV ISREMDQRYL QFDIKAFVEN
NPAIRWCPAV RCERAVRLTR PGPGDNDPHS FPLLPSPAVD CGKGHLFCWY CLGEAHEPCD
CQTWRNWLQK VTEMKPEELA GVSEAYEDAA NCLWLLTNSK PCANCKSPIQ KNEGCNHMQC
AKCKYDFCWI CLEEWKKHSS STGGYYRCTR YEVIQQLEEQ SKEMTVEAEK KHKSFQELDR
FMHYYTRFKN HEHSYKLEQK LLKTAKEKME QLSRAFISRE GTPPDTQFIE DGVCELLKTR
RVLKCSYPYG FFLQQGSTQK EIFELMQTDL EMVVEDLAQK VNRPYLRTPC HKIISAARLV
QQKRQEFLAS VARGVAPNDS PEAPRRNYPG GSWDWEYLGF ASPEVKENAA SVIPYTNTLT
HPYSVSQFDV CAPEGPERSE GRRRALGSLD EDDPNILLAI QLSLQESRRE RSLEGGMEGA
RGSSFPPSLL DPPRPPTRTD SSPQPAELLE LGDSLMKLGN ITTPYDLDTH TFDTHTQDQP
CSHHTYNHST LTAAYTVEAN YSDRSHRQAQ NTLTAPYLLD HITISQSSDP SGDSKEQSHC
HSSTYLAEAE HTGSYELEHT QNPAHPSSYK REHSATYESN LKPDSSYNPH SALTSSYTQE
RPASYVLERT PKAASQPPGQ LCLPSPDLEP ELLLSPVIPP GGAFTPSDPE SLEPLDPAAS
AQLLDNIMAW FSNNINPQNN TQSLALIPSP PTTETESSPD TVTETGSERH TSREVTPAPV
WQPLVGELEV GRGVMSPSLG AGGVEGQETL RPNTLELENR EADKEGVNTG CVANVSLDEA
DTHPCSHSQH GDGPVHTAQA RETDLDLTLQ LEEDQSPEEW EEQVHLV
//
