ID A0A7L2N384_9PASS Unreviewed; 1095 AA.
AC A0A7L2N384;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
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};
DE Flags: Fragment;
GN Name=Ankib1 {ECO:0000313|EMBL:NXR66605.1};
GN ORFNames=RHASIB_R08577 {ECO:0000313|EMBL:NXR66605.1};
OS Rhadina sibilatrix.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Phylloscopidae; Rhadina.
OX NCBI_TaxID=2585818 {ECO:0000313|EMBL:NXR66605.1, ECO:0000313|Proteomes:UP000587697};
RN [1] {ECO:0000313|EMBL:NXR66605.1, ECO:0000313|Proteomes:UP000587697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-26 {ECO:0000313|EMBL:NXR66605.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXR66605.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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. {ECO:0000256|ARBA:ARBA00008278}.
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:NXR66605.1}.
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DR EMBL; VWYO01019366; NXR66605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L2N384; -.
DR Proteomes; UP000587697; 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; PF12796; Ank_2; 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 SMART; SM00184; RING; 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:UP000587697};
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 331..571
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 335..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 299..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..963
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXR66605.1"
FT NON_TER 1095
FT /evidence="ECO:0000313|EMBL:NXR66605.1"
SQ SEQUENCE 1095 AA; 123176 MW; 70661E96DCA35C30 CRC64;
NMGNTTTKFR KALINGDENL ACQIYESNPQ LKETLDPNTS YGETYQHNTP LHYAARHGMN
RILGTFLFVR DGNPNKRNVH NETSMHLLCM GPQIMISEGA LHPRLTRPSE DDCRRADCLQ
MILKWKGAKL DEGQYERAAI DAVDNKKNTP LHYAAASGMK TCVELLVKHG GDLFAENENK
DTPCDCAEKQ HHKELALNLE SRMVFSRDPE AESIEAEYAA LDKKEPYEGL RLQDLRRLKD
MLIVESADML QAPLFTAEAL LRAHDWDREK LLEAWMCNPE NCCQRSGVQM PTPPPSGYNA
WDTLPSPRTP RTTRSSVTSP DEISPSPGDM ETAVCDICMC NISVFEDPVD MPCGHDFCRA
CWEAFLNLKI QEGEAHNIFC PAYDCFQLVP VDIIESVVSK EMDKRYLQFD IKAFVENNPA
IKWCPIPGCE RAVRLTRQGS NSTGSDTLSF PMLKAPAVDC GKGHLFCWEC LGEAHEPCDC
QTWKDWLQKI SEMKPEELVG VSEAYEDAAN CLWLLTNSKP CANCKSPIQK NEGCNHMQCA
KCKYDFCWIC LEEWKKHSSS TGGYYRCTRY EVIQHVEEQS KEMTVEAEKK HRRFQELDRF
MHYYTRFKNH ELSYQLEQRL LKTAKEKMEQ LSRALSGTEG GCPDTTFIED AVQELLKTRR
ILKCSYPYGF FLEPKSTKKE IFELMQTDLE MVTEDLAQKV NRPYLRTPRH KIIRAACLVQ
QKRQEFLASV ARGVAPADSP EAPRRSFAGG TWDWEYLGFA SPEEYAEFQY RRRHRQRRRG
DMHSLLSNTP DPDDPSESTL DTQEGGSSRR HGTSMVSSAS MGILHSSSLH DYTPVSRSEN
QDSLQALSSL DEDDPNILLA IQLSLQESGL AIDEETRDFL NNEASLGAIG TSLPTRLDSA
PISIDNPRGA LSSSELLELG DSLMRLGAGN DPFSADRLHS HPCSETRSGL YSTSSDADSS
SQDPNTNENL LGNIMAWFHD MNPQSIALIP STSTETDEES QQPSTEDGSA GQPNLTDTGL
EPQEEHALFE DALKNEGRGT QTEESMSEEN IIPSETVSQI GDNNREVAST LDASGDISSQ
TPQTSSEWTE HVHLV
//
