ID A0A672YTC7_9TELE Unreviewed; 1222 AA.
AC A0A672YTC7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-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=LOC115428449 {ECO:0000313|Ensembl:ENSSORP00005007757.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005007757.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005007757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSORP00005007757.1}
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; A0A672YTC7; -.
DR Ensembl; ENSSORT00005008040.1; ENSSORP00005007757.1; ENSSORG00005004386.1.
DR InParanoid; A0A672YTC7; -.
DR Proteomes; UP000472271; 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:UP000472271};
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 336..574
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 340..386
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 762..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 576..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 774..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1098
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 136920 MW; 33E5C21319E3BD12 CRC64;
MGNTATKFRK ALVSGDEALA WQLYEGNPQF RDGLDPNASY GEQYQHNTPL HYVCRHAMTR
LLRSFLFSKE GNPNKRNVHN ETCLHVLCQG PQILLLPEGA LSPRLARPQR DEQRRADCLQ
MILSWTGARL EGGQYEKANV NATDNHHSTC LHYAAAAGMR SCVELLIQSE ADLFVEDEDK
LTPCDHAERH HHTELALSLE SQMVFSSSSA QQSNTDAHGE TNLLQYKEPF EGLKLQDLRR
LKDMLIVETA DMLQAPLFTA EALLRAHDWD REKLLEAWMS DAEGCCQRSG VAMPTPPPSG
YNAWDTLPSP RTPRTPRSPL TLTLTSPTDS CLTPGEEGLC GICLCSISVF EDPVDMSCGH
EFCRGCWEGF LNVKIQEGDA HNIFCPAFEC YQLVPVHVIE SVVSREMDQR YLQFDIKAFV
ENNPAIRWCP AARCERAVRL TRPGPGDSDP HSFPLLPSPA VDCGKGHLFC WYCLGEAHEP
CDCQMWRNWL QKVTEMKPEE LAGVSEAYED AANCLWLLTN SKPCANCKSP IQKNEGCNHM
QCAKCKYDFC WICLEEWKKH SSSTGGYYRC TRYEVIQQLE EQSKEMTVEA EKKHKSFQEL
DRFMHYYTRF KNHEHSYKLE QRLLKTAKEK MEQLSRAFIS EGTPPDTRFI EDGVSELLKT
RRVLKCSYPY GFFLQQGSTQ KEIFELMQTD LEMVVEDLAQ KVNRPYLRTP CHKIISAARL
VQQKRQEFLA SVARGVAPND SPEPPPNKGD CLQDYADIQY RRRHRPRRRG DMLSLQNLRS
SSNTPEASRR SDNTEGPERG EGRRRALGSL DEDDPNILLA IQLSLQESRR ERDGPSGARG
SSFPSSLLDP PRAELLELGD SLMKLGNITT PYDLDTHTQE QLCSHHTCSH SVLATPYTLE
SAYSDCSHRP DQNTRTTPYM LDHITDPRYD SKEQTYCHSS TYLAEAEHTA SCSLTQNPSH
PSPYSQDHQA TPKPDSSYTP FPEHSSSYTP ERPAAYALDR PPKPEPQPPS QLCLPSPELE
PELLLSPVIP PGGPFTPSDP QSLEALDPAA SAQLLDNIMA WFNNNINPQN NPQSLALIPS
PPTTETDSSP DTLTETESQT SRDMAPTPIW QPLEGEPAVV ADRGSASPHS GTTAVGARVE
VPKMSSGRPS TLELEADEEG VDAGCVADLS LDEAHTHPCS HSHLGGSSPT HTAPTTESEL
DLALQLEGDQ SPEEWEEQVH LV
//
