ID A0A2Y9H157_NEOSC Unreviewed; 1092 AA.
AC A0A2Y9H157;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 18-JUN-2025, entry version 34.
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|RefSeq:XP_021545268.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Monachinae; Monachini; Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021545268.1};
RN [1] {ECO:0000313|RefSeq:XP_021545268.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021545268.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_021545268.1; XM_021689593.2.
DR AlphaFoldDB; A0A2Y9H157; -.
DR STRING; 29088.A0A2Y9H157; -.
DR GeneID; 110579960; -.
DR KEGG; nsu:110579960; -.
DR InParanoid; A0A2Y9H157; -.
DR Proteomes; UP000248481; Chromosome 12.
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 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 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:UP000248481};
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 282..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 122496 MW; 3DABB503472A9163 CRC64;
MGNTTTKFRK ALINGDENLA CQIYENNPQL KESLDPNTSY GEPYQHNTPL HYAARHGMNR
ILGTFLFGRD GNPNKRNVHN ETSMHLLCMG PQIMISEGAL HPRLARPAED DFRRADCLQM
ILRWKGAKLD QGEYERAAID AVDNKKNTPL HYAAASGMKT CVELLVKHGG DLFAENENKD
TPCDCAEKQH HKDLALNLES QMVFSRDPEA EEIEAEYAAL DKREPYEGLR PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSNPEN CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLSPGDLD TSLCDICMCS ISVFEDPVDM PCGHDFCRGC
WESFLNLKIQ EGEAHNIFCP AYDCFQLVPV DIIESVVSKE MDKRYLQFDI KAFVENNPAI
KWCPTPGCER AVRLTKQGSN TSGSDTLNFP LLRAPAVDCG KGHLFCWECL GEAHEPCDCQ
TWKNWLQKIT EMKPEELVGV SEAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQHVEEQSK EMTVEAEKKH KRFQELDRFM
HYYTRFKNHE HSYQLEQRLL KTAKEKMEQL SRALKETEGG CPDTTFIEDA VHVLLKTRRI
LKCSYPYGFF LEPKSTKKEI FELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIKAACLVQQ
KRQEFLASVA RGVAPADSPE APRRSFAGGT WDWEYLGFAS PEEYAEFQYR RRHRQQRRRG
DVHSLLSNPP DPDEPSESTL DITDGGSGRR PGASVVSSAS MSVLHTSSLR DYTPASRSEN
QDSLQALSSL DEDDPNILLA IQLSLQESGL AIDEENRDFL NNEASLGAIG TSLPSRLDSV
PRNTDSPRAA MSSSELLELG DSLMRLGGES DPFSTDTLSS HPLSEARSEF CPSSSDPDSA
GQDANINDNL LGNIMAWFHD MNPQSIALIP PAATEISADS QLPCVKDESE GVRDVDLVPP
EEDSVFEDAV VSEGRRTQIE EENPLEENTL AGEAASPAGN SGNEAANKGD GSDVSSPTPQ
TSSDWLEQVH LV
//
