ID A0A669Q4B8_PHACC Unreviewed; 729 AA.
AC A0A669Q4B8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
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:ENSPCLP00000008866.1};
OS Phasianus colchicus (Common pheasant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Phasianus.
OX NCBI_TaxID=9054 {ECO:0000313|Ensembl:ENSPCLP00000008866.1, ECO:0000313|Proteomes:UP000472261};
RN [1] {ECO:0000313|Ensembl:ENSPCLP00000008866.1}
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 RefSeq; XP_031450623.1; XM_031594763.1.
DR AlphaFoldDB; A0A669Q4B8; -.
DR Ensembl; ENSPCLT00000012040.1; ENSPCLP00000008866.1; ENSPCLG00000007357.1.
DR GeneID; 116229952; -.
DR OMA; EQEQTCK; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000472261; Unplaced.
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; SSF101447; Formin homology 2 domain (FH2 domain); 1.
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:UP000472261};
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 333..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..323
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 104..152
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..95
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..626
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 77994 MW; 338C1CD2F450A956 CRC64;
MGSERDSESP RSSSIHSAAA KCPKPGRRRR LSFQSVFSAA AASAAGGRRR AKADPPPAAP
PPPPAAPPAP PPPPPPPPPP PPEEAPAAAA AAAAEGSGEE ELECPLCLVR QPAENAPRLL
SCPHRSCGAC LRQYLRIEIT ESRVNICCPE CSERLNPADI RRLLRDSPHL VAKYEEFMLR
RCLAADPDCR WCPAPDCGYA VIAYGCASCP KLTCERDGCQ TEFCYHCKQI WHPNQTCDMA
RQQRAQTLRV RTKHTSGLSY GQESGPADDI KPCPRCSAYI IKMNDGSCNH MTCAVCGCEF
CWLCMKEISD LHYLSPSGCT FWGKKPWSRK KKILWQLGTL IGAPVGISLI AGIAIPAMVI
GIPVYVGRKI HSRYEGKKTS KHKRNLAITG GVTLSVIASP VIAAVSVGIG VPIMLAYVYG
VVPISLCRGG GCGVSTANGK GVKIEFDEDD GPITVADAWR ALKNPSIGES SIEGLTSVLS
TSGSPTDGLS VMQSNYSETA SFAALSGGTL SGGVLSGGKG KYSRLEVQAD VQKEIFPKDS
VSLGAISDNA STRAMAGSII SSYNPQDREC NNMEIQVDIE AKPSHYQLAS GSSTEDSLHV
HTQMAENEEE EEEEGEEEEE EEDGEQEQTC KHQSCEQKDC VASKTWDITL AQPESIRSDL
ESSDSQSDDV PDLTSDDCGS PRSHSAAPCP QTPSARGAES PSAHLSHCAH AEGCRLDEMV
TLECIEARV
//
