ID A0A093PBY9_PYGAD Unreviewed; 1095 AA.
AC A0A093PBY9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 18-JUN-2025, entry version 53.
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 ORFNames=AS28_06590 {ECO:0000313|EMBL:KFW71715.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Sphenisciformes;
OC Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW71715.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW71715.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW71715.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL225407; KFW71715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PBY9; -.
DR STRING; 9238.A0A093PBY9; -.
DR Proteomes; UP000054081; 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:UP000054081};
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..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..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..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 1075..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW71715.1"
FT NON_TER 1095
FT /evidence="ECO:0000313|EMBL:KFW71715.1"
SQ SEQUENCE 1095 AA; 123056 MW; 7C58C45C41663D2E 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 MGILHSSSLH DYTPVSHSEN
QDSLQALSSL DEDDPNILLA IQLSLQESGL AIDEETRDFL NNEASLGAIG TSLPTRLDSA
RISIDNPRGA LSSSELLELG DSLMRLGAGS DPFSADRLHS HPCSDTRSGL YSTSSDADSS
SQDPNTSENL LGNIMAWFHD MNPQSIALIP STSTETDEDS QQPSTEDGSA GQPNLIDTGL
EPQEEHALFE DALKNEGRGT QTEESTSEEN IIPGEMVSQS GDDNREVTSA LDASGDTSSQ
TPQTSSEWIE HVHLV
//
