ID A0A6P7P1G9_BETSP Unreviewed; 1323 AA.
AC A0A6P7P1G9;
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=LOC114866062 {ECO:0000313|RefSeq:XP_029023504.1};
OS Betta splendens (Siamese fighting fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Osphronemidae; Betta.
OX NCBI_TaxID=158456 {ECO:0000313|Proteomes:UP000515150, ECO:0000313|RefSeq:XP_029023504.1};
RN [1] {ECO:0000313|RefSeq:XP_029023504.1}
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_029023504.1; XM_029167671.2.
DR GeneID; 114866062; -.
DR Proteomes; UP000515150; Chromosome 11.
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; 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:UP000515150};
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 146..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 338..576
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 342..388
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 772..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..639
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 811..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 148023 MW; E400259E3CA213B3 CRC64;
MGNTATKFRK ALVSGDEALA WQLYEGNPQF RDGLDPNSSY GEQYQHNTAL HYVCRHAMTR
LLRAFLFSKE GNPNKRNVHN ETCLHVLCQG PQILLLPEGA LSPRLARPQR DERRRADCLQ
MILSWTGARL EGGQYEKANV NATDNHHSTC LHYAAAAGMK NCVELLIQGE ADLFVEDEDK
LTPCDHAERH HHTELALSLE SQMVFSSSSA QQPNTGAHGE ATLLQYKEPY EGLKLQDLRR
LKDMLIVETA DMLQAPLFTA EALLRAHDWD REKLLEAWMS DAEGCCQRSG VTMPTPPPSG
FNAWDTLPSP RTPRTPRSPL TFTLTSPTDS CLTPGDEGLA TCGICLCSIS VFEDPVDMSC
GHEFCRACWE GFLNVKIQEG DAHNIFCPAY ECYQLVPVHV IESVVSREMD QRYLQFDIKA
FVENNPAIRW CPAARCERAV RLTRPGPGDS DPHSFPLLPS PAVDCGRGHL FCWECLGEAH
EPCDCQMWRN WLQKVTEMKP EELAGVSEAY EDAANCLWLL TNSKPCANCK SPIQKNEGCN
HMQCAKCKYD FCWICLEEWK KHSSSTGGYY RCTRYEVIQQ LEEQSKEMTV EAEKKHKSFQ
ELDRFMHYYT RFKNHEHSYK LEQKLLKTAK EKMEQLSKAF ICREGTPPDT RFIEDGVSEL
LKTRRVLKCS YPYGFFLQQG STQKEIFELM QTDLEMVVED LAQKVNRPYL RTPCHKIISA
ARLVQQKRQE FLASVARGVA PNDSPEPPRR TYPGGSWDWE YLGFASPEMG SRHSVMGVGD
QRERQSQDYA DIQYRRRHRA RRRGDMLSLH NLRSSSNTPE TSRRSDNTGP ERSDGHRRAL
GSLDEDDPNI LLAIQLSLQE SRRERGLDGG LDRMELERAL DRAQERRSAL VGEVDDVALH
SLNTDGPPGA RGPPFPTSVL DPPRPPNRTD STAQPPLSNA LPLPPPPPSL SAELLELGDS
LMKVGNTTAP YDANAHAQDK LCSHHTYNHN ALTAPYSIEP AYSEGSHRQL QNAHTAPYVH
DHITIKNTRY DSNEQNYCHS GPYLAEAENA ASCALEHNQN STRPSSCIRE HAAMYDTTPK
PNSSYNLGSE QGSSYTQERS AAYALDHPPK SDPTPPAQLC LPSPEPEPEL LLSPVIPPGG
PFTPSDPQSL EALDPTASAQ LLDNIMAWFN NNINPQNNPQ SLALIPSPPT TETDSSPDTH
TETESESQTS RGMTPAPLWQ PLEGDPEVER APANPCLGAA GSEGLKTARP RTLELESREA
GEESAEAGCV ADMSLDEVHT HPCFHQGNSP SHTAPTTERD SHLHLQLEGD QSPEVWEEQV
HLV
//
