ID A0A813VV04_9BILA Unreviewed; 739 AA.
AC A0A813VV04;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=NZN594_LOCUS6281 {ECO:0000313|EMBL:CAF0848491.1};
OS Rotaria sp. Silwood1.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Rotaria.
OX NCBI_TaxID=2762511 {ECO:0000313|EMBL:CAF0848491.1, ECO:0000313|Proteomes:UP000663835};
RN [1] {ECO:0000313|EMBL:CAF0848491.1}
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 -!- 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:CAF0848491.1}.
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DR EMBL; CAJNOP010000005; CAF0848491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A813VV04; -.
DR Proteomes; UP000663835; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
DR GO; GO:0043130; F:ubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR CDD; cd20338; BRcat_RBR_RNF19; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 1.20.120.1750:FF:000017; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000424; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR051628; LUBAC_E3_Ligases.
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; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000663835};
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 434..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..424
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 207..252
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..104
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..149
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 81074 MW; 01E7546CC8A0D4C3 CRC64;
MGNIGSKRKC SVDISKRSKE TRNTEIAEAF SSSTMFSKTR NQRTSIKQVP TTDSSSISTK
DRPPVTTTPS SLMNSNFLSL PTNSTSTQPT TQRLSNTSTS NNDNESVRRR FLNLLRFTTS
RPSSSVRFSR PRDTNLSKQQ QQQQQQQQQN FSTISIHDNG SITSSLAFIK DELIESVAAS
ANEHVINIIP STTTNQLHDN NNNIETCVLC CQEYPLEDFE RLTLCSHSYC RTCLKSYLKL
EITEGRVTLN CPQSDCPERI HPSDISRILE KQPDLISKYE QFMVRRVLQS IADTRWCPAP
DCGFAVIASG YASCPEIQCL RPGCNTSFCY HCKAIWHPNK TCEDAAREKL SSKIRSGSFI
SLGSAQQRDE IKQCPRCQAS ILKMDDGSCN HMTCPICEAE FCWLCGREIS DLHYLSPSGC
TFWGKKQWSR KKVILWQVAT LIGAPVIIAL IAGVAVPGVI IGVPVWAGRK IFKKFNKSHY
SKTKRNILVT LGVVGSVVAS PIIAALAVGI GVPILLAYVY GVIPISLCRT GGCGVGTRNE
LSDGDSPNID NILPFSLRDV PIARTLLNDN QSVMTHPTIG GDSTSLSNSV AHLIDDRSNE
STKALPGTGA VSLCESLPPS NRLEVQAEVS DCKSFDIESI TISEKSSKTM DSLKALAGSI
KDACTVPGVE YNNDTICGGT GDFNGRKSSL LSSASDYARS INVEQQQQHS TLNRAGSPNS
DKTVSFFDER VTLKSKKKY
//
