ID A0A8C6UT35_9GOBI Unreviewed; 1019 AA.
AC A0A8C6UT35;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
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 Neogobius melanostomus (round goby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Benthophilinae; Neogobiini;
OC Neogobius.
OX NCBI_TaxID=47308 {ECO:0000313|Ensembl:ENSNMLP00000040907.1, ECO:0000313|Proteomes:UP000694523};
RN [1] {ECO:0000313|Ensembl:ENSNMLP00000040907.1}
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 Ensembl; ENSNMLT00000045479.1; ENSNMLP00000040907.1; ENSNMLG00000025082.1.
DR Proteomes; UP000694523; 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; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694523};
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..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..791
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 114954 MW; 0B54B35AC761E707 CRC64;
MGNTATKFRK ALINGDELLA CQLYESNPQF KDALDPNSTY GESYQHNTPL HYAARHAMLR
LLRSFLQNKD GNPNKRNVHN ETSLHLLCMG PLILTSEGAL HPRITRPHED QQRRAECLRI
VLLWTGAKLD HGEYERADVN ATDNKKNTCL HYAAASGMKT CVELLVKREA DLFAENESRE
TPCDCAERQH HTELALGLES QMVFSQAPEA EGIEAEYAAL DRGELYEGLR PQDLRRLKDM
LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMKDAEE CCQRSRVQMP NPPPSGYNAW
DTLPSPRTPR TARSSITSPD QIGLLPAEEE SALCGICMSS ISIFEDPVDM TCGHEFCRAC
WEGFLNIKIQ EGEAHNIFCP AFDCYQLVPV EVIESVVSRE MDRRYLQFDI KAFVENNPAI
RWCPVAGCER AVRLNTRGPG SSTSDFLSFP LLRAPAVDCG KGHLFCWACQ GEAHEPCDCE
TWKAWLQKVS EMKPEELAGV TVAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQQVEEQEE TQEFQELDRF MHYYTRFKNH
EHSYQLEQRL LKTAKEKMEQ LSRALSGREG GPPDTTFIED AVLELLKTRR ILKCSYPYGF
FLEPKSTKKE IYELMQTDLE MVTEDLAQKV NRPYLRTPRH KIIRAACLIQ QKRQEFLASV
ARGVAPSDSP EAPRRSFAGG TWDWEYLGFA SPEEYAEFQY RRRHRQRRRG DMSSLHSNTP
DPDDDGLGSF DDDDPNILLA IQLSLQDSGM VGAGASDEPN DASLGPLAPL LEALTKTSLS
SSELLELGTM SLFSSSDSTT CSSHEPSSSS ALAVNTNLLG NIMAWFHDMN PQGITLVPPT
SSDTDSNLCA LHTEDEDESL QDEHDKSAVV IPENEQSLEA EVCVSALEKE CVVAERPTQL
ELVQLEPLPL PYPSPQESSA EPHFEAQRLC HVDTPQCDSV CEQLPSTSSS EWEEQVHLV
//
