ID E7EYI2_DANRE Unreviewed; 1074 AA.
AC E7EYI2; A0A8M3AQF9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ankib1b {ECO:0000313|Ensembl:ENSDARP00000117914,
GN ECO:0000313|RefSeq:XP_009290458.1,
GN ECO:0000313|ZFIN:ZDB-GENE-100920-6};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000117914};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000117914}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000117914};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000117914, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000117914};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_009290458.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009290458.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; BX248082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009290458.1; XM_009292183.3.
DR PaxDb; 7955-ENSDARP00000098372; -.
DR Ensembl; ENSDART00000131227; ENSDARP00000117914; ENSDARG00000076829.
DR Ensembl; ENSDART00000131227.2; ENSDARP00000117914.1; ENSDARG00000076829.5.
DR GeneID; 561277; -.
DR KEGG; dre:561277; -.
DR AGR; ZFIN:ZDB-GENE-100920-6; -.
DR CTD; 561277; -.
DR ZFIN; ZDB-GENE-100920-6; ankib1b.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_1_0_1; -.
DR OMA; EXWDREK; -.
DR OrthoDB; 3084186at2759; -.
DR PhylomeDB; E7EYI2; -.
DR TreeFam; TF331104; -.
DR Proteomes; UP000000437; Chromosome 16.
DR Bgee; ENSDARG00000076829; Expressed in brain and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF465; 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 SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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 145..177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 330..570
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 334..380
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..633
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 301..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120782 MW; DE99A3B07D3E2D63 CRC64;
MGNTATKFRK ALISGDEVLA YQLYEGNPQF KESLDPNTSY GEPYQHNTPL HYAARHAMTR
ILRSFLFSKD GNPNKRNVHN ETALHVLCMG PLILLSEGAL QPRLARPYED ERRRAECLQM
ILKWTGAKLD RGKYESADVS ATDNKKNTPL HYAAASGMKT CVEFLVKRGA DLFAENENKE
TPCDCAERQH HKELALGLES QMVFSTDPNA EDIEAEYAAL DRREFYEGLR VQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSNAED CCQRSGVQMP IPPPRGYNTW
DTLPSPRTPR TTRSSITSPD EISLTPADDD HSLCGICMCA ASMFEEPVDI PCGHEFCRGC
WESFLNLKIQ EGEAHNIFCP AYDCFQLVPV EVIESIVSKE MDKRYLQFDI KAFVENNPAI
RWCPRAGCDR AVRLAGQGPG ASTSDPLSFP RLQAPAVDCG KGHLFCWECQ GEAHEPCDCQ
TWKMWLQKVT DMKPEELAGV SEAYEDAANC LWLLTNSKSC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQQVEEQSK EMTVEAEKKH KNFQELDRFM
HYYTRFKNHE HSYQLEERLL KTAKDKMEQL SKVLSGREGG PPDTTFIEDA VHELLKTRRI
LKCSYPYGFF LEPKSTKKEI FELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIRAACLVQQ
KRQEFLASVA RGVAPNDSPE APRRSFAGGT WDWEYLGFAS PEEYAEFQYR RRHRQRRRGD
MASLRSNTPD PDDPGHSTLD TQEIGGGQRP GLPMPHSSLD EDDPNILLAI QLSLQESGLM
AGGAGVDAQE ILSNEASLGA IGTSLPTRLD PVLCGIDVPR AALSSSELLE VGDSLKKLGN
ISGQNVPLRF DNLNNPARDP SEGPFHNPAR HMESSDFNSD NANLLGNIMA WFHDMNPQNI
SLVPSAGAMH QEFASQSARM PSESDCAVPQ WITGGDREVE REFDSGIIAG EREPVRPTQL
DLIGLDMCPP PSTVELGETP SALNPCHSDT PKCDSDPDQP SSSSSEWEGQ VHLV
//
