VIE1_BHV4D
ID VIE1_BHV4D Reviewed; 285 AA.
AC P27426;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable E3 ubiquitin-protein ligase IE1;
DE EC=2.3.2.27;
DE AltName: Full=32.7 kDa immediate early protein IE1;
DE AltName: Full=RING-type E3 ubiquitin transferase IE1;
GN Name=IE1;
OS Bovine herpesvirus 4 (strain DN-599) (BoHV-4) (Movar virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10355;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9689; Panthera leo (Lion).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1716688; DOI=10.1128/jvi.65.10.5211-5224.1991;
RA van Santen V.L.;
RT "Characterization of the bovine herpesvirus 4 major immediate-early
RT transcript.";
RL J. Virol. 65:5211-5224(1991).
CC -!- FUNCTION: Controls the expression of later classes of genes and also of
CC the IE genes (Potential). E3 ubiquitin-protein ligase (Probable). E3
CC ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating
CC enzyme in the form of a thioester and then directly transfer the
CC ubiquitin to targeted substrates. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; M60043; AAA96266.1; -; Genomic_DNA.
DR PIR; A40504; EDBED9.
DR RefSeq; NP_076504.1; NC_002665.1.
DR SMR; P27426; -.
DR GeneID; 1684910; -.
DR KEGG; vg:1684910; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044003; P:modulation by symbiont of host process; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 3: Inferred from homology;
KW DNA-binding; Early protein; Membrane; Metal-binding; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Probable E3 ubiquitin-protein ligase IE1"
FT /id="PRO_0000056349"
FT TOPO_DOM 1..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 124..183
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 285 AA; 32693 MW; 98347DF3EC183610 CRC64;
MASKDSDVRC VKCQSLKPTT PLTGQDRCAR CVAINELKPW ISTCNINPCY DGDLSESNET
IEMMDINSCR EDTPSDAESE TRFMPFVAHS KQPKHTSKNP TKGEIQYFPV EKCKDIHRVE
NQSSIDEEGK QCWICRDGES LPEARYCNCY GDLQYCHEEC LKTWISMSGE KKCKFCQTPY
KVNRQLSLKR GLPGYWDRDD RFVFIAGFIG MGTILAGWIA SFFYLLVVLC GKYFTYKDVM
IVVGGLAIIQ VVGLMFSLFM YFQIGNLLRQ YINYMTETNI DPLRT
