ID A0A6G1PMY6_9TELE Unreviewed; 1104 AA.
AC A0A6G1PMY6;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
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=EXN66_Car007345 {ECO:0000313|EMBL:KAF3691670.1};
OS Channa argus (northern snakehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Channoidei; Channidae; Channa.
OX NCBI_TaxID=215402 {ECO:0000313|EMBL:KAF3691670.1, ECO:0000313|Proteomes:UP000503349};
RN [1] {ECO:0000313|EMBL:KAF3691670.1, ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OARG1902GOOAL {ECO:0000313|EMBL:KAF3691670.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF3691670.1};
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus Var Kimnra genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM015718; KAF3691670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1PMY6; -.
DR Proteomes; UP000503349; Chromosome 7.
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; 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:UP000503349};
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 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1104
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 984..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 123372 MW; 00FEBC7398A56AFC CRC64;
MGNTATKFRK ALINGDEVLA CQLYQSNPQF KEALDPNSTY GESYQHNTPL HYAARHAMTR
LLRFFLLSKD GNPNKRNMHN ETSLHLLCMG PQILTSEGAL QPRISRPYVD EQRRAECLQF
ILAWTGAKLD HGEYETADIN ATDNKKNTCL HYAAASGMKT CVELLVQREG DLFAENENRE
TPCDCAEKQR HKELALCLES QMVFSLAPEA EGIEAEYAAL DRRELYEGLR PQDLRKLKDM
LIVETADMLQ APLFTAEALL RANDWDREKL LEAWMSNAEE CCQRSGVQMP NPPPSGCNAW
DNLPSPRTPR TTRSSITSPD QISLMPTDED SSLCGICMSS ISVFEEPVDM SCGHEFCRAC
WEGFLNLKIQ EGEAHNIFCP AFDCYQLVPV EVIESVVSRE MDRRYLQFDI KAFVENNPAI
RWCPMAGCER AVRLNTQGPG NSTSDPLGFP LLRAPAVDCG KGHLFCWECR GEAHEPCDCE
TWKMWLQKVN EMRPEELAGV SEAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQQVEEQSK EMTEEAEKKH KSFQELDRFM
HYYTRFKNHE HSYQLEQRLL KTAKEKMEQL SRALSGREGG PPDTTFIEDA VLELLKTRRI
LKCSYPYGFF LEPKSTKKEI YELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIRAACLVQQ
KRQEFLASVA RGVAPNDSPE APRRSFAGGT WDWEYLGFAS PEEYAEFQYR RRHRQRRRGD
MSSLHSNTPD PDDPDTQDVG GGCRGPFMGL GSLDDDDPNI LLAIQLSLQD SGMALDESSH
EVLAGGASLG AIGTSLPSRL EQRAPGIEVL PRASLSSSEL LELGDNLARL GNISSHYSAT
PIPTAGLHCD GRHRAYGASV PISVAPSGSN SSTGHFSSSS DTIDSITCSA HDPSSSSTLA
ANANLLGNIM AWFHDMNPQG ITLLPSTSSN TDSNLGAHHA DGGGGQQDEN RKPQETIVDV
GFCSQRPSDE EEKECAVIER PTQLDLVGLD TMQLPYMATL DTNGDHAQCG GSKVCHVDTP
QCDSASDQLP STSSSEWEEQ VHLV
//
