ID A0A674APP1_SALTR Unreviewed; 1124 AA.
AC A0A674APP1;
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:ENSSTUP00000061015.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000061015.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000061015.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A674APP1; -.
DR FunCoup; A0A674APP1; 1228.
DR Ensembl; ENSSTUT00000064383.1; ENSSTUP00000061015.1; ENSSTUG00000026039.1.
DR GeneTree; ENSGT00940000157621; -.
DR InParanoid; A0A674APP1; -.
DR OMA; GPMEDPW; -.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000472277; 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; 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; PS50297; ANK_REP_REGION; 1.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
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 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..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 295..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 125952 MW; F17373363AC3878E CRC64;
MGNTATKFRK ALMNGDEGLA YQLYEGSPQF KESLDPNTSY GEPYQHNTPL HYAARHAMTR
LIRSFLFSKD GNPNKRNVHN ETSLHLLCMG PQILMGDGAL QPRLARPELD QMKRAECLQI
ILKWTGAKLD QGEYENANVN ATDNKKNTSL HYAAAAGMKK CVEILVNREA DLFAENEDRE
TPCDCAEKQH HKELALSLES QMVFRVSPEG IEAEYTALDH RELYEGLRPQ ELRRLKDMLI
VETADMLQTP LFTAEALLRA HDWDRENLLE AWMSNAQECC QRSGVHMPSA PPSGYNAWDT
LPSPRTPRTT RTSITSPDEI SLTPGDDGRT LCGICMCPLS IFEEPVDMSC GHEFCRACWE
GFLNLKIQEG EAHNIVCPAH DCFHLVPVEV IESVVSREMD KRYLQFDIKA FVENNPAIRW
CPKAGCERAV RLSSQGPGSS SSDPFSLPLL RAPAVDCGKG HVFCWECQGE AHEPCDCQTW
KMWLAEVTEM RPQELAGVSE AYEDAANCLW LLSNAKPCAN CKSPIQKNEG CNHMQCAKCK
YDFCWICLEE WKKHSSSTGG YYRCTRYEVI NQVEEQNKDM TVEAEKKHKG FQELDRFMHY
YTRFKNHEHS YQLEQRLLKT AKDKMEQLSR ALSGRDGGPP DTTFIEDAVL ELLKTRSILK
CSYPYGFFLE IKSTKKEIFE LMQTDLEMVT EDLAQKVNRP YLRTPRHKII RAACLVQQKR
QEFLASVARG VAPSDSPEAP RRSFGGGTWD WEYLGFASPE EYAEFQYRRR HRDRQQRRQR
GDIPHLDDPS DSTLADTQEM GGGRRRGPPM GSLDEDDPNI LLAIQLSLQE SGLAMAGDTP
EFLSNEASLG AIGTSLPSRL DAEPQGVEVG PRGAISSSEL LELEDRVMRL GNMGTISSQR
LYEGVPGVYA LHHHPSQQHY SNHNLNTFRE PSSGEALFSS SSDTTDSTTT TSTGLQDPSH
PNTNLLGNIM AWFHDMNPQS ITLIPSSTTT TTSSDTDFNT AAQTTANTAS VEEEEVQADL
HQPRAKPQKG EGELGEDGDC FPFLSQGLEE KEAERERPTH LDLTVGSEVM APSCMVTTGT
GDRAGERLAG GNVVHVDTPM CDSVTSDLLP STSSSEWEEQ IHLV
//
