ID A0A817F0A8_9BILA Unreviewed; 1101 AA.
AC A0A817F0A8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=RHK424_LOCUS1507 {ECO:0000313|EMBL:CAF2723844.1},
GN RMH319_LOCUS15704 {ECO:0000313|EMBL:CAF4142633.1};
OS Rotaria sp. Silwood2.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Rotaria.
OX NCBI_TaxID=2762512 {ECO:0000313|EMBL:CAF2723844.1, ECO:0000313|Proteomes:UP000663849};
RN [1] {ECO:0000313|EMBL:CAF2723844.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAF2723844.1}.
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DR EMBL; CAJNVN010000002; CAF2723844.1; -; Genomic_DNA.
DR EMBL; CAJOBM010003099; CAF4142633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A817F0A8; -.
DR Proteomes; UP000663849; Unassembled WGS sequence.
DR Proteomes; UP000663884; Unassembled WGS sequence.
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 FunFam; 3.30.40.10:FF:000051; 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; IPR044066; TRIAD_supradom.
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; PF12796; Ank_2; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF13639; zf-RING_2; 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; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000663884};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
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 69..101
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 234..469
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 238..284
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1034..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 126709 MW; 7FFA8FCF911288FD CRC64;
MILKSEVLLH LLHDHNGNAN KRNRLNQTSL HCLLKPGNEV RRNECLTLLL KWKDKHTNET
IDIDAKDSDD NTALHYAAKN GLKSCVESLL NAGAALYVEN REKLTPCELA EKNGHKDLAI
YLESRMIFSN SSEELEIDES PLMIDDTSCG LRIQDLQEAK DLLLVETADM LQLPLFTAEA
LLRHYEWSKE SLLQSWIDDP ISCCEISGVN PPLSLLHERG LTTIDINEFD TVHLSKECGI
CLKEFESGVE RIVISCDHQF CKDCWKQYLT FKIQEGSVHS IFCPAVDCFK FVPNEIIEKC
VDQNMARRYL QFDIKAFVDS NPNFKWCPHS NCTLAVQSPI FDRLQSSHMR EFSKSVNCRN
GHYFCWDCLQ EGHEPASCEN WKDWFEKIAE IKPEELKGTE EEEEIAANCL WLVTNSKKCP
NCSISIQKNE GCNHIKCVKC KYDFCWICLE AWKKHSSTTG GYFQCNRYET VNKIVAKEKE
LITAAEQRHL RMVELNKFVH YYTRFKNHEN SYKLEEPLSK SAKEKCEVIF AKSSQPTQVI
TTSATTNDEN NFESQTKFIE DAIKELLRAR RVLRCSYVYG YYLENSGHKK MIFEFIQTEF
EECTETLSQI IARPYLRTPK HRIVQVTKTV KRKRLEFLET IARGLIPPDT PPSLKKFSRQ
RWKYLLKDDV DGDDNELKKA IAASLKDLDP KNPWIVDRKG RHTNLVTLLN EWPELEMEMD
SGLVSCDDGA YCKRRHCYNR RARNPTTTIP FDYCSLKCLR LDRTEQLEGE EREMEQSLVG
LNGSPAITTP STTASVSTND SVYYQQSTDD TLSPVVVVVP SNDVMDLLRA IEMSRLQAVR
EHEQNINRPN TNSNNNNSIL STNDKIDYFN DLQQAIELSI KTKNQHKSTN EATACVESQQ
DDSQLIDVAA VAATMPSLDL FLENNVDTLN SIMMNLQPPI EKDVLYENSK IIDFAHKQNE
LKENLQKPDE LKEYEDFDLK CIETSFHQQQ TELKRKLSNK KNKDAILPLQ SNDIATVAAA
ATVSLTNKPH GVLQRKRSNR DVDIRPCEPN ERFDNYRPPA SQNDNQQYEH TWFNEPVSMS
TTRAIVERRP ITPSDDESSF T
//
