ID A0A671M7E9_9TELE Unreviewed; 1065 AA.
AC A0A671M7E9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
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=LOC107685566 {ECO:0000313|Ensembl:ENSSANP00000028941.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000028941.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000028941.1}
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 AlphaFoldDB; A0A671M7E9; -.
DR Ensembl; ENSSANT00000030810.1; ENSSANP00000028941.1; ENSSANG00000014523.1.
DR Proteomes; UP000472260; 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 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:UP000472260};
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 299..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 119744 MW; D03B23A13902935A CRC64;
MGNTATKFRK ALISGDEVLG YQLYEGSPQF KESLDPNTSY GEPYQHNTPL HYAARHAMTR
ILRSFLFSKD GNPNKRNMHN ETTLHVLCMG PNILLSEGVL QPRLARPYED ERRRAECLQM
ILKWTGAKLD RGEYESADVS ATDNKKNTPL HYAAASGMKT CVEFLVKRGA DLFAENENKE
TPCDCAERQH HKELALSLES QMVFSSDPHA EDIEAEYAAL DRREFYEGLR VQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSNAEN CCQRSGVQMP TPPPRGYNTW
DTLPSPRTPR TTHSSITSPD EISLTPADDD RSLCGICMCA ASMFEEPVDI PCGHEFCRGC
WESFLNMKIQ EGEAHNIFCP AYDCFQLVPV EVIESIVSRE MDKRYLQFDI KAFVENNPAI
RWCPRAGCDR AVRLAGQGPG ASTSGPLSFP RLQAPAVDCG KGHLFCWSCQ GEAHEPCDCQ
TWKMWLQKVT DMKPEELAGV SEAYEDAANC LWLLSNAKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQQVEEQSK EMTVEAEKKH KNFQELDRFM
HYYTRFKNHE HSYQLEDRLL KTAKDKMEQL SKVLSGREGG PPDTTFIEDA VHELLKTRRI
LKCSYPYGFF LEPKSTKKEI YELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIRAACLVQQ
KRQEFLASVA RGVAPNDSPE APRRSFAGGT WDWEYLGFAS PEAYAEFQYR RRHRQRRRGD
MASLRSNTPD PDDPGHSTLG MFCECVFILP RGSLDEDDPN ILLAIQLSLQ ESGLTAGGAG
IDAQEILANE ASLGAIGTSL PTRLDPVLCG IDVPRAALSS SELLEVGDSL KKLGNISGQN
VPPRYDNLNN PSCESAEGPF QAPSGHTETS DFSSDNANLL GNIMAWFHDM NPQNISLVPS
AGDFGIQSAR MTTEPTECAV PQWTPGGDRE AEHEFDSAIE REPIRPTQLD LVGLDMCPVP
PASSIKLGET PSGLNPCHFD TPKCDSDPDQ PNSSSSEWEG QEHHV
//
