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Database: UniProt
Entry: A0A8C5NVD0_JACJA
LinkDB: A0A8C5NVD0_JACJA
Original site: A0A8C5NVD0_JACJA 
ID   A0A8C5NVD0_JACJA        Unreviewed;       784 AA.
AC   A0A8C5NVD0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, 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};
GN   Name=Ankib1 {ECO:0000313|Ensembl:ENSJJAP00000002379.1};
OS   Jaculus jaculus (Lesser Egyptian jerboa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Dipodoidea;
OC   Dipodidae; Dipodinae; Jaculus.
OX   NCBI_TaxID=51337 {ECO:0000313|Ensembl:ENSJJAP00000002379.1, ECO:0000313|Proteomes:UP000694385};
RN   [1] {ECO:0000313|Ensembl:ENSJJAP00000002379.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
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   Ensembl; ENSJJAT00000004656.1; ENSJJAP00000002379.1; ENSJJAG00000004011.1.
DR   GeneTree; ENSGT00940000157621; -.
DR   OMA; CNPENCC; -.
DR   Proteomes; UP000694385; 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; 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; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694385};
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          305..545
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          309..355
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          273..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          588..615
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        279..294
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  89720 MW;  3A8A18F75A85E16F CRC64;
     MGNTTTKFRK ALINGDENLA CQIYENNPQL KESLDPNTSY GEPYQHNTPL HYAARHGMNR
     ILGTFLFGRD GNPNKRNVHN ETSMHLLCMG PQIMISEGTL HPRLARPMED DFRRADCLQM
     ILRWKGAKLD QGEYERAAID AVDNKKNTPL HYAAASGMKA CVELLVKHGG DLFAENENKD
     TPCDCAEKQH HKDLALNLES QMVFSRDPEA EEIEAEYAAL DKRESIKRVQ ISIHFFPKDW
     DREKLLEAWM SNPENCCQRS GVQMPTPPPS GYNAWDTLPS PRTPRTTRSS VTSPDEISLS
     PGDLDTTLCD ICMCGISVFE DPVDMPCGHD FCRGCWESFL NLKIQEGEAH NIFCPAYECF
     QLVPVDIIES VVSKEMDKRY LQFDIKAFVE NNPAIKWCPT AGCERAVRLT KQGSSSSGSD
     TLSFPLLSAP AVDCGKGHLF CWECLGEAHE PCDCHTWKNW LQKITEMKPE ELVGVSEAYE
     DAANCLWLLT NSKPCANCKS PIQKNEGCNH MQCAKCKYDF CWICLEEWKK HSSSTGGYYR
     CTRYEVIQHV EEQSKEMTVE AEKKHKRFQE LDRFMHYYTR FKNHEHSYQL EQRLLKTAKE
     KMEQLSRALK ETEGGCPDTT FIEDAVHVLL KTRRILKCSY PYGFFLEPKS TKKEIFELMQ
     TDLEMVTEDL AQKVNRPYLR TPRHKIIKAA CLVQQKRQEF LASVARGVAP ADSPEAPRRS
     FAGGTWDWEY LGFASPEEYA EFQYRRRHRQ QRRRGDVHSL LSNPPDPSEP SESTFDIPEG
     GSSR
//
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