ID A0A813S3I1_9BILA Unreviewed; 882 AA.
AC A0A813S3I1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GPM918_LOCUS2928 {ECO:0000313|EMBL:CAF0789620.1},
GN OVA965_LOCUS5833 {ECO:0000313|EMBL:CAF0824751.1}, SRO942_LOCUS2928
GN {ECO:0000313|EMBL:CAF3573777.1}, TMI583_LOCUS5830
GN {ECO:0000313|EMBL:CAF3609144.1};
OS Didymodactylos carnosus.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Philodinida; Philodinidae; Didymodactylos.
OX NCBI_TaxID=1234261 {ECO:0000313|EMBL:CAF0789620.1, ECO:0000313|Proteomes:UP000663829};
RN [1] {ECO:0000313|EMBL:CAF0789620.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:CAF0789620.1}.
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DR EMBL; CAJNOQ010000340; CAF0789620.1; -; Genomic_DNA.
DR EMBL; CAJNOK010001686; CAF0824751.1; -; Genomic_DNA.
DR EMBL; CAJOBC010000340; CAF3573777.1; -; Genomic_DNA.
DR EMBL; CAJOBA010001686; CAF3609144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A813S3I1; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000663829; Unassembled WGS sequence.
DR Proteomes; UP000677228; Unassembled WGS sequence.
DR Proteomes; UP000681722; Unassembled WGS sequence.
DR Proteomes; UP000682733; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:2000779; P:regulation of double-strand break repair; IEA:TreeGrafter.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044198; DEK.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13468; DEK PROTEIN; 1.
DR PANTHER; PTHR13468:SF1; PROTEIN DEK; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000663829};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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 TRANSMEM 785..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 487..543
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 563..771
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 567..613
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 32..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..143
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..411
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 99826 MW; D5DAA6F0FF53CC5A CRC64;
MRFNITNDCA AFIYSTVSNI DYFHMTIDEN NKVDDDKVPE GKEPSSTEAD ILRDQTKDVN
VKTSAEIAEP TGPASSVTNN NNSDDADNRK QEPTTELDEI ATKQEVAEEP EKKSANSTKS
KRKSSSSPKK KAKSSSSTIP NDSSPDEKDG PVQKAISTDA NGEENANEVN SPSTQPTEDE
KPLFEQPILL EGKRRRTATA RLEINELTPK KEVQLPKGNG KPLGEIEYIN YQITNTNGEQ
LVPLQYICFG RKVAHANMKK TLRTFNGFDF KKGTSEYERT ISRLLKYKKS QLKVFLDVLG
LHQNGRNEEQ AERILDFLIE PYDEGKKLPK KVSKQNSASK KRQSTDSSSK ASGIKRNNKT
TSETIDESNM DSNDKDDPIE DDDDEEREEE EVDEYEPGKG KKKSSPKKKV RSLNNKNSAS
KDKGQKRKRV SATTKEDSKK IRNDTTVNDE NDDEKETTNA SGDTNETSPI SEDNVANNIK
HKNETKEPSE DSLRSTVKRI LNGVDLSGVT MKNVLKDVYS KYPDFDLTDR KDFIKDIVKE
MEYSEEVKEL CSSTKDSQNL LSPICQCPIC FHDIFDAQEI YKVNACSCMF CRKCVYQYCT
NQLEINFIPI ACPNANCNGI LSINELEPAL NTKQIQLYEK LLLNHEVALD RKKLFCPGVN
CGQICTIPDE NDLTKKAPIT CTNCRLTFCI KCREIWHEDR PCPDDGIPFE SEAEASIKRC
PRCQLPIERL VGCAQMLCRR CKHIFCWYCL TSLDNDFFLL HYERGPCRNR LGHTRISLFL
HRITIVGIFA GLSVLLLIAT PFLILATPCI ICCRCKESKS RSGYYAKWRR RFREARGRRA
SDELTTLEID QSTSLSKIET AAFSTPPIFT TRTDDHLEVS TE
//
