ID A0A6P8PT21_GEOSA Unreviewed; 1096 AA.
AC A0A6P8PT21;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
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_033787038.1,
GN ECO:0000313|RefSeq:XP_033787039.1};
OS Geotrypetes seraphini (Gaboon caecilian) (Caecilia seraphini).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Gymnophiona; Geotrypetes.
OX NCBI_TaxID=260995 {ECO:0000313|Proteomes:UP000515159, ECO:0000313|RefSeq:XP_033787039.1};
RN [1] {ECO:0000313|RefSeq:XP_033787038.1, ECO:0000313|RefSeq:XP_033787039.1}
RP IDENTIFICATION.
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}.
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DR RefSeq; XP_033787038.1; XM_033931147.1.
DR RefSeq; XP_033787039.1; XM_033931148.1.
DR FunCoup; A0A6P8PT21; 1618.
DR GeneID; 117354166; -.
DR KEGG; gsh:117354166; -.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000515159; Chromosome 2.
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; 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:UP000515159};
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 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..826
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"
SQ SEQUENCE 1096 AA; 123371 MW; C3B82EC69197624D CRC64;
MGNATTKFRK ALINGDENLA CQIYESNPQL KESLDPNSSY GEPYQHNTPL HYASKHGMAR
LLGTFLFTKD GNPNKRNVHN ETAMHMLCMG PQIMISDGAL HPRLTRPSED DFRRSDCLQM
ILRWKGAKLD QGEYERAAID AVDNKRNTSL HYAAASGMKA CVELLVKHGG DLFAENENKD
TPCDCAEKQH HKELALNLES QMVFSRDPEA DDIEAEYAAL DKREPYEGLR PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMCNPES CCQRSGVQMP TPPPSGYNAW
DTLPSPRTPR TTRSSVTSPD EISLSPGDVD TPLCGICMCN ISVFEDPVDI PCGHDFCRTC
WEAFLNLKIQ EGEAHNIFCP AYECFQLVPV DVIESVVSKE MDKRYLQFDI KAFVENNTAI
KWCPTPGCDR AVRLTKQGSN TSGPDTLRFP LLRAPAVDCG KGHLFCWECL GEAHEPCDCQ
TWKNWLQKVS EMKPEELVGV NEAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQQVEEQSK EMTVEAEKKH KRYQELDRFM
HYYTRFKNHE LSYQLEQRLL KTAKEKMELL SRALGGIQGG CPDTTFIEHA VHELLKTRHI
LKCSYPYGFF LEPKSTKKEI FELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIRAACLVLQ
KRQEFLASVA RGVAPADSPE APRRSFAGGT WDWEYLGFAS PERMKSQSSV IRRMSLCNKS
CLYRRRHRQR RRGELYSLRS TPDPDDASES TLDTQEGGGN RRHGTSMVSS ASMNILHSSS
FHDYTPVSHS ENQDSLQALS SLDEDDPNIL LAIQLSLQES GLTIDEETRD FLTNEASLGA
IGSSLPTRLG PAPINIDNSR AALSSSELLE LGDSLMRLGV ANNPYSADCS HPFSDARSGL
YTVSSDPDST SQDPTINENL LGNIMAWFHD MNPQSIALIP SASADIDEDS QQLSTEEQPG
QPTLTDVAQS VQEEHALFQD ALINEDRGTQ AEESTHEGNV LADMVPQIGN YVTNSEDVAS
QTPQTASEWT EQVHLV
//
