ID A0A7K5G8Y1_9AVES Unreviewed; 1095 AA.
AC A0A7K5G8Y1;
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:NWS53441.1};
GN ORFNames=CHUBUR_R03465 {ECO:0000313|EMBL:NWS53441.1};
OS Chunga burmeisteri (Black-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Cariamiformes; Cariamidae; Chunga.
OX NCBI_TaxID=1352770 {ECO:0000313|EMBL:NWS53441.1, ECO:0000313|Proteomes:UP000541181};
RN [1] {ECO:0000313|EMBL:NWS53441.1, ECO:0000313|Proteomes:UP000541181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-CU-031-22 {ECO:0000313|EMBL:NWS53441.1};
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:NWS53441.1}.
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DR EMBL; VZRC01000057; NWS53441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K5G8Y1; -.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000541181; 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:UP000541181};
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 283..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..816
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..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 1022..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWS53441.1"
FT NON_TER 1095
FT /evidence="ECO:0000313|EMBL:NWS53441.1"
SQ SEQUENCE 1095 AA; 122981 MW; 7EA46B888CB066F0 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 LLEAWMSNPE NCCQRSGVQM PTPPPSGYNA
WDTLPSPRTP RTTRSSVTSP DEISPSPGDI 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 MGILRSSSLH DYTPVSRSEN
QDSLQALSSL DEDDPNILLA IQLSLQESGL AIDEETRDFL NNEASLGAIG TSLPTRLDSA
PISIDNPRGA LSSSELLELG DSLMRLGTGN DPFSADHLHS HPCSDTRSGL YSTSSDADSS
SQDPNTNENL LGNIMAWFHD MNPQSIALIP STSTETDEDS QQPSTEDGSA GQPNLTDTGL
EPQEKHALFE DALKNEGRGT QTEEGPSEET VIPGETVSQS GDNNREVTST LAASGDTSSQ
TPQTSSEWIE HVHLV
//
