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Database: UniProt
Entry: A0A091RQ26_NESNO
LinkDB: A0A091RQ26_NESNO
Original site: A0A091RQ26_NESNO 
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
//
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