ID A0A852AYC3_9CORV Unreviewed; 613 AA.
AC A0A852AYC3;
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_0 {ECO:0000313|EMBL:NXP61181.1};
GN ORFNames=CHLCYA_R09679 {ECO:0000313|EMBL:NXP61181.1};
OS Chloropsis cyanopogon.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Irenidae; Chloropsis.
OX NCBI_TaxID=1218682 {ECO:0000313|EMBL:NXP61181.1, ECO:0000313|Proteomes:UP000614263};
RN [1] {ECO:0000313|EMBL:NXP61181.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-002-57 {ECO:0000313|EMBL:NXP61181.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXP61181.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (OCT-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:NXP61181.1}.
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DR EMBL; WEZZ01014245; NXP61181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A852AYC3; -.
DR Proteomes; UP000614263; 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 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; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:NXP61181.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000614263};
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 220..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..210
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 473..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXP61181.1"
FT NON_TER 613
FT /evidence="ECO:0000313|EMBL:NXP61181.1"
SQ SEQUENCE 613 AA; 66541 MW; C61A1CE10E181594 CRC64;
ENAPRLLSCP HRSCGACLRQ YLRIEITESR VNICCPECSE RLNPADIRRL LRDSPHLVAK
YEEFMLRRCL AADPDCRWCP APDCGYAVIA YGCASCPKLT CERDGCQTEF CYHCKQIWHP
NQTCDMARQQ RAQTLRVRTK HTSGLSYGQE SGPADDIKPC PRCSAYIIKM NDGSCNHMTC
AVCGCEFCWL CMKEISDLHY LSPSGCTFWG KKPWSRKKKI LWQLGTLIGA PVGISLIAGI
AIPAMVIGIP VYVGRKIHSR YEGKKTSKHK RNLAITGGVT LSVIASPVIA AVSVGIGVPI
MLAYVYGVVP ISLCRGGGCG VSTANGKGVK IEFDEDDGPI TVADAWRALK NPSIGESSIE
GLTSVLSTSG SPTDGLSVIQ GNYSETASFA ALSGGTLSGG VLSGSKGKYS RLEVQADVQK
EIFPKDSVSL GAISDNASTR AMAGSIISSY NPQDRECNNM EIQVDIEAKP SHYQLTSGSS
TEDSLHVHTQ MAENEEEEEE EEEEEEDGKE EQTCKHQSCE QKDCIASQTW DITLAQPESI
RSDLESSDSQ SDDVPDITSD ECESPLCQTA AGCPHTPRAR GAQSPSAHLS HCAQAEGCRL
DEMVQLECIE ARV
//
