ID A0A8T2JIM2_9PIPI Unreviewed; 1059 AA.
AC A0A8T2JIM2;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 18-JUN-2025, entry version 13.
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 ORFNames=GDO86_011823 {ECO:0000313|EMBL:KAG8443160.1};
OS Hymenochirus boettgeri (Congo dwarf clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Pipinae; Hymenochirus.
OX NCBI_TaxID=247094 {ECO:0000313|EMBL:KAG8443160.1, ECO:0000313|Proteomes:UP000812440};
RN [1] {ECO:0000313|EMBL:KAG8443160.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Female2 {ECO:0000313|EMBL:KAG8443160.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAG8443160.1};
RA Mudd A.B.;
RT "Comparative Genomics and Chromosome Evolution.";
RL Thesis (2020), ProQuest LLC, 789 East Eisenhower Parkway, Ann Arbor, MI,
RL USA.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG8443160.1}.
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DR EMBL; JAACNH010000005; KAG8443159.1; -; Genomic_DNA.
DR EMBL; JAACNH010000005; KAG8443160.1; -; Genomic_DNA.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000812440; Chromosome 6.
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; 2.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000812440};
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 287..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..633
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 119916 MW; C2BFC835C7AF2EE2 CRC64;
MGNATTKFRK ALISGDENLA YQIYESNLQL KDSLDPNTSY GEPYQHNTPL HYASRYGMGR
LLRAFLYGKD GNPNKRNIHN ESSMHLLCMG SHLLISEGAL DHRFARFMDD DRRRSECLKM
ILDWKGAKLD HGEYERASLD ATDNKKNTPL HYAAASGMKT CVELLVRSGS DLFSENENKD
TPCDCAEKQH HKDLALKLES QMVFSRDPEA DDIEAEYAAL DKREPYEGLT PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMCSPEN CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLSPGDID TPLCGICICN ISIFEDPVEI PCGHEFCRTC
WESFLNLKIQ EGEAHNIFCP AYDCFQLVPV DVIESVVSKE MDKRYLQFDI KAFVENNTAI
RWCPTPACER AVRLKKQGSN NSGSDTLTFP LLQAPAVDCG KGHLFCWECL GEAHEPCDCQ
TWKNWLQKVS EMKPEELVGV SEAFEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKSDFCWICL EEWKKHSSST GGYYRCTRYE VINQVEEQSK EMTVEAEKKH KRFQELDRFM
HYYTRFKNHE HSYRLEQRLI KTAKEKMEQL SRALSETGSP DTTFIEDAVQ ELLKTRRILK
CSYPYGFFLE PKSTKKEIFE LMQTDLEMVT EDLAQKVNRP YLRTPRHKII RATCLVQQKR
QEFLASVARG VAPADSPEAP RRSFAGGTWD WEYLGFASPE EYAEFQYRRR HRQRRRGDMH
SVRSNTPDPD DRSENTDSHE AGSSRRHGTS MALSSLDEDD PNILLAIQLS LQESGLAVDE
ETREFINNEA SLGAIGSSLP SRLDPAPISM DNPRSALSSS ELLEIGESLA RLGANSEPYA
TDNLLHPFSD AQRALCSTSS DLDLSSQDQN LSENLLGNIM AWFHEIHPQS IALIPSATSE
TDVDLQPLSA DEHIFPPTLR EQSQSLAEEH ALFQDALIND YRETQTEGGT SEDIVPFTDS
VSPGADQTID IISSITNSEN ISSRTPETAN EWVEQVHLV
//
