ID A0A7L1U2M6_PHANI Unreviewed; 612 AA.
AC A0A7L1U2M6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
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 {ECO:0000313|EMBL:NXO67922.1};
GN ORFNames=PHANIT_R14100 {ECO:0000313|EMBL:NXO67922.1};
OS Phainopepla nitens (Phainopepla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Bombycillidae; Phainopepla.
OX NCBI_TaxID=161653 {ECO:0000313|EMBL:NXO67922.1, ECO:0000313|Proteomes:UP000579685};
RN [1] {ECO:0000313|EMBL:NXO67922.1, ECO:0000313|Proteomes:UP000579685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-32 {ECO:0000313|EMBL:NXO67922.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXO67922.1};
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:NXO67922.1}.
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DR EMBL; VXBQ01008826; NXO67922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L1U2M6; -.
DR Proteomes; UP000579685; 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:NXO67922.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000579685};
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 217..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..207
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 470..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXO67922.1"
FT NON_TER 612
FT /evidence="ECO:0000313|EMBL:NXO67922.1"
SQ SEQUENCE 612 AA; 66514 MW; EBE91663C357394A CRC64;
PRLLSCPHRS CGACLRQYLR IEITESRVNI CCPECSERLN PADIRRLLRD SPHLVAKYEE
FMLRRCLAAD PDCRWCPAPD CGYAVIAYGC ASCPKLTCER EGCQTEFCYH CKQIWHPNQT
CDMARQQRAQ TLRVRTKHTS GLSYGQESGP ADDIKPCPRC SAYIIKMNDG SCNHMTCAVC
GCEFCWLCMK EISDLHYLSP SGCTFWGKKP WSRKKKILWQ LGTLIGAPVG ISLIAGIAIP
AMVIGIPVYV GRKIHSRYEG KKTSKHKRNL AITGGVTLSV IASPVIAAVS VGIGVPIMLA
YVYGVVPISL CRGGGCGVST ANGKGVKIEF DEDDGPITVA DAWRALKNPS IGESSIEGLT
SVLSTSGSPT DGLSVIQGNY SETASFAALS GGTLSGGVLS GSKGKYSRLE VQGDVQKEIF
PKDSVSLGAI SDNASTRAMA GSIISSYNPQ DRECNNMEIQ VDIEAKPSHY QLTSGSSTED
SLHVHTQMAE NEEEEDEEEE EEEEEEGEQE QTCKHQSCEQ KDCIASQTWD ITLAQPESIR
SDLESSDSQS DDVPDITSDE CESPHCQTAA GCPQTPRARG AQSPSAHLSH CAQAEGCRLE
EMVQLECIEA RV
//
