ID A0A091RQ26_NESNO Unreviewed; 1095 AA.
AC A0A091RQ26;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN ORFNames=N333_08964 {ECO:0000313|EMBL:KFQ44775.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ44775.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ44775.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ44775.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KK930206; KFQ44775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RQ26; -.
DR Proteomes; UP000053840; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 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:SF437; ANKYRIN REPEAT AND IBR DOMAIN-CONTAINING PROTEIN 1; 1.
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; 2.
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 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053840};
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 297..325
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..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ44775.1"
FT NON_TER 1095
FT /evidence="ECO:0000313|EMBL:KFQ44775.1"
SQ SEQUENCE 1095 AA; 123226 MW; A1BCF4DEB50F32BD 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 DEITPSPGDI ETTVCDICMC NISVFEDPVD MPCGHDFCRA
CWEAFLNLKI QEGEAHNIFC PAYDCFQLVP VDIIESVVSK EMDKRYLQFD IKAFVENNPA
IKWCPIPGCE RAVRLTKQGS 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 HPCSDTRSGL YSTSSDADSS
SQDPNTNENL LGNIMAWFHD MNPQSIALIP STSTETDEDS QQPNTEDGSA GQPKLIDTRL
EPQEEHALFE DALKNEGRGT QTEESTSEEN IIPGEMVSQS GDNNREVTST LDASGDASSQ
TPQTSSEWIE HVHLV
//