ID A0A3Q1HTJ6_9TELE Unreviewed; 1123 AA.
AC A0A3Q1HTJ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 30.
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};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000031140.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000031140.1}
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; A0A3Q1HTJ6; -.
DR FunCoup; A0A3Q1HTJ6; 728.
DR STRING; 80966.ENSAPOP00000031140; -.
DR Ensembl; ENSAPOT00000023901.1; ENSAPOP00000031140.1; ENSAPOG00000000914.1.
DR GeneTree; ENSGT00940000157621; -.
DR InParanoid; A0A3Q1HTJ6; -.
DR OrthoDB; 69641at2759; -.
DR Proteomes; UP000257200; Unplaced.
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:UP000257200};
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 331..571
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 335..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 300..323
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 941..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..634
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 125158 MW; 4CB3EE1CA35B3142 CRC64;
MGNTATKFRK ALINGDEVLA CQLYESNPQF KEALDPNSTY GESYQHNTPL HYAARHAMTR
LLRSFIHSKD GNPNKRNVHN ETSLHLLCMG PQILTSEGAL QPRISRPYED EQRRAECLQI
VLAWTGAKLD HGEYESADIN ATDNKKNTCL HYASASGMKT CVELLVQREA DLFAENENRE
TPCDCAEKQH HKELALRLES QMVFSLAPEA EGIEAEYAAL DRRELYEGLR PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMTDAEE CCQRSGVQMP NPPPSGCNAW
DTLPSPRTPR TTRSSITSPD QISLMPADDD ESSLCGICMS SISVFEEPVD VSCGHEFCRA
CWEGFLNLKI QEGEAHNIFC PAFDCYQLVP VEVIESVVSR EMDRRYLQFD IKAFVENNSA
IRWCPEAGCE RAVRLNTQGP GTSTSDPLSF PLLRAPAVDC GKGHLFCWEC QGEAHEPCDC
ETWKLWLQKV NEMKPEELAG VSEAYEDAAN CLWMLTNSKP CANCKSPIQK NEGCNHMQCA
KCKYDFCWIC LEEWKKHSSS TGGYYRCTRY EVIQQVEEQS KEMTEEAEKK HKSFQELDRF
MHYYTRFKNH EHSYQLEQRL LKTAKEKMEQ LSRALSGREG GPPDTTFIED AVLELLKTRR
ILKCSYPYGF FLEPKSTKKE IYELMQTDLE MVTEDLAQKV NRPYLRTPRH KIIRAACLVQ
QKRQEFLASV ARGVAPNDSP EAPRRSFAGG TWDWEYLGFA SPEEYAEFQY RRRHRQRRRG
DMSSLRSNTP DPDDLSDSTL DTQDVGGGRR QGPLMGLGSL DDDDPNILLA IQLSLQDSGM
AGSGSHHEIL ANEASLGAIG TSLPSRLEQS GPGVEVLPRA SLSSSELLEL GDNLARLGNI
NLSSQYSAAT GVSISVQHCD SHHRAYGASV PIPVAPGGSN SSTGLFSSST DTTDSTTCGS
HDPSSSSALA ANANLLGNIM AWFHDMNPQG ITLVPPTSSD TDSSLGALHA GGGCLQDDDR
SGIVVLPESR KPQEVMADVG FCSQRLSDME EKECSVAERP TQLDLVGLDT MPLPYMATLD
ASGDHADRRG SKVCHVDSPL CDSVSDQLPS TSSSEWEEQV HLV
//
