ID A0A8C3NI83_GEOPR Unreviewed; 717 AA.
AC A0A8C3NI83; A0A8U8BLB0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19B {ECO:0000313|Ensembl:ENSCPVP00000020299.2};
OS Geospiza parvula (Small tree-finch) (Camarhynchus parvulus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Camarhynchus.
OX NCBI_TaxID=87175 {ECO:0000313|Ensembl:ENSCPVP00000020299.2, ECO:0000313|Proteomes:UP000694382};
RN [1] {ECO:0000313|Ensembl:ENSCPVP00000020299.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Enbody D E., Pettersson E M.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCPVP00000020299.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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}.
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DR Ensembl; ENSCPVT00000021219.2; ENSCPVP00000020299.2; ENSCPVG00000014750.2.
DR Proteomes; UP000694382; Chromosome 23.
DR GO; GO:0016020; C:membrane; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694382};
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}.
FT TRANSMEM 324..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 77383 MW; 51FF9B88D1EED99E CRC64;
MGSERDSESP RSSSIHSAAA KCPKPGRRRR LSFQSVFSAA AASAAGGRRR AKAEPPPAAP
PPPPPPPPAP PPPPPPPPPP EEAPVVPEGE EELECPLCLV RQPAENAPRL LSCPHRSCGA
CLRQYLRIEI TESRVNICCP ECSERLNPAD IRRLLRDSPH LVAKYEEFML RRCLAADPDC
RWCPAPDCGY AVIAYGCASC PKLTCEREGC QTEFCYHCKQ IWHPNQTCDM ARQQRAQTLR
VRTKHTSGLS YGQESGPADD IKPCPRCSAY IIKMNDGSCN HMTCAVCGCE FCWLCMKEIS
DLHYLSPSGC TFWGKKPWSR KKKILWQLGT LIGAPVGISL IAGIAIPAMV IGIPVYVGRK
IHSRYEGKKT SKHKRNLAIT GGVTLSVIAS PVIAAVSVGI GVPIMLAYVY GVVPISLCRG
GGCGVSTANG KGVKIEFDED DGPITVADAW RALKNPSIGE SSIEGLTSVL STSGSPTDGL
SVIQGNYSET ASFAALSGGT LSGGVLSGSK GKYSRLEVQA DVQKEIFPKD SVSLGAISDN
ASTRAMAGSI ISSYNPQDRE CNNMEIQVDI EAKPSHYQLT SGSSTEDSLH VHTQMAENEE
EEEEEEEEEE DDKQEQTCRH QSCEQKDCIG SQTWDITLAQ PESIRSDLES SDSQSDDVPD
LTSDECESPQ CQTAAGCPQT PRARAAQSPS AHLSHCAQAE GCRLDEMVQL ECIEARV
//
