ID A0A851JNL8_9PASS Unreviewed; 631 AA.
AC A0A851JNL8;
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};
DE Flags: Fragment;
GN Name=Rnf19b_1 {ECO:0000313|EMBL:NXB79886.1};
GN ORFNames=DONATR_R00900 {ECO:0000313|EMBL:NXB79886.1};
OS Donacobius atricapilla.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Mimidae; Donacobius.
OX NCBI_TaxID=237420 {ECO:0000313|EMBL:NXB79886.1, ECO:0000313|Proteomes:UP000660704};
RN [1] {ECO:0000313|EMBL:NXB79886.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-001-63 {ECO:0000313|EMBL:NXB79886.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXB79886.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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:NXB79886.1}.
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DR EMBL; WBMY01014656; NXB79886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A851JNL8; -.
DR Proteomes; UP000660704; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 1.20.120.1750:FF:000001; 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:000052; 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; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
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; 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; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:NXB79886.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000660704};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW 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 236..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..226
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 7..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 489..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXB79886.1"
FT NON_TER 631
FT /evidence="ECO:0000313|EMBL:NXB79886.1"
SQ SEQUENCE 631 AA; 68639 MW; 45BB85347B7AE59A CRC64;
GEEELECPLC LVRQPAENAP RLLSCPHRSC GACLRQYLRI EITESRVNIC CPECSERLNP
ADIRRLLRDS PHLVAKYEEF MLRRCLAADP DCRWCPAPDC GYAVIAYGCA SCPKLTCERD
GCQTEFCYHC KQIWHPNQTC DMARQQRAQT LRVRTKHTSG LSYGQESGPA DDIKPCPRCS
AYIIKMNDGS CNHMTCAVCG CEFCWLCMKE ISDLHYLSPS GCTFWGKKPW SRKKKILWQL
GTLIGAPVGI SLIAGIAIPA MVIGIPVYVG RKIHSRYEGK KTSKHKRNLA ITGGVTLSVI
ASPVIAAVSV GIGVPIMLAY VYGVVPISLC RGGGCGVSTA NGKGVKIEFD EDDGPITVAD
AWRALKNPSI GESSIEGLTS VLSTSGSPTD GLSVIQGNYS ETASFAALSG GTLSGGVLSG
SKGKYSRLEV QADVQKEIFP KDSVSLGAIS DNASTRAMAG SIISSYNPQD RECNNMEIQV
DIEAKPSHYQ LTSGSSTEDS LHVHTQMAEN EEEEEEEEEE EEEEEDKQEQ TCKHQSCEQK
DCVASQTWDI TLAQPESIRS DLESSDSQSD DVPDITSDEC ESPHCQTAAG CPQTPRARGA
QSPSAHLSHC AQAEGCRLDE MVQLECIEAR V
//
