Detail Information for IndEnz0002004163
IED ID IndEnz0002004163
Enzyme Type ID protease004163
Protein Name Large tegument protein deneddylase
EC 3.4.19.12
EC 3.4.22.-
Gene Name BPLF1
Organism Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Gammaherpesvirinae Lymphocryptovirus Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4) Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Enzyme Sequence MSNGDWGQSQRTRGTGPVRGIRTMDVNAPGGGSGGSALRILGTASCNQAHCKFGRFAGIQCVSNCVLYLVKSFLAGRPLTSRPELDEVLDEGARLDALMRQSGILKGHEMAQLTDVPSSVVLRGGGRVHIYRSAEIFGLVLFPAQIANSAVVQSLAEVLHGSYNGVAQFILYICDIYAGAIIIETDGSFYLFDPHCQKDAAPGTPAHVRVSTYAHDILQYVGAPGAQYTCVHLYFLPEAFETEDPRIFMLEHYGVYDFYEANGSGFDLVGPELVSSDGEAAGTPGADSSPPVMLPFERRIIPYNLRPLPSRSFTSDSFPAARYSPAKTNSPPSSPASAAPASAAPASAAPASAAPASAAPASAAPASAAPASAAPASSPPLFIPIPGLGHTPGVPAPSTPPRASSGAAPQTPKRKKGLGKDSPHKKPTSGRRLPLSSTTDTEDDQLPRTHVPPHRPPSAARLPPPVIPIPHQSPPASPTPHPAPVSTIAPSVTPSPRLPLQIPIPLPQAAPSNPKIPLTTPSPSPTAAAAPTTTTLSPPPTQQQPPQSAAPAPSPLLPQQQPTPSAAPAPSPLLPQQQPPPSAARAPSPLPPQQQPLPSATPAPPPAQQLPPSATTLEPEKNHPPAADRAGTEISPSPPFGQQPSFGDDASGGSGLVRYLSDLEEPFLSMSDSEEAESDLASDIPTTEDEDMFEDEVFSNSLESGSSAPTSPITLDTARSQYYQTTFDIETPEMDFVPLESNIARIAGHTYQEQAIVYDPASNREVPEADALSMIDYLLVTVVLEQGLIRSRDRSSVLNLLEFLKDWSGHLQVPTLDLEQLLTSELNIQNLANMLSENKGRAGEFHKHLAAKLEACLPSLATKDAVRVDAGAKMLAEIPQLAESDDGKFDLEAARRRLTDLLSGGDQEAGEGGGEPEDNSIYRGPHVDVPLVLDDESWKRLLSLAEAARTAVARQQAGVDEEDVRFLALLTAIEYGAPPAASVPPFVHNVAVRSKNAALHVRRCTADIRDKVASAASDYLSYLEDPSLPTVMDFDDLLTHLRHTCQIIASLPLLNIRYTSIEWDYRELLYLGTALSDMSGIPWPLERVEEDDPSIAPLPEFETVAKKQKELETTRENEKRLRTILDDIEAMLGLAGVASAPGAPISPASPSATPANHDNPEATPPLADTAALTIPVIEKYIANAGSIVGAAKNPTYIRLRDTIQQIVRSKKYLMNILKSITFYTIDNYIASFEESIDHLYRDLPVLDPEVQDGIDRILDPMVSEALHTFEMGNRLTLEPARLVALQNFATHSTLKETAAAVNLLPGLLAVYDATITGQAPEDALRLLSGLQNQLSQTLIPGKLKKRFLSYLQKLKNNNNDQLRQKEVQAWRLEAEGFKPATEEQLEAFLDTAPNKELKRQYEKKLRQLMETGRKEKEKLREQEDKERQERRAREANEAWARIRKALGARPEPAPTSPDDWNTLLASLLPDNTDSAAAAAAAVARNTDILDSLTQILAAMLLGITRVRRERLRSLLVDDGGAAERMEAAEPGWFTDIETGPLARLDAWPATPAATAKEGGGGRGAEEAAGALFRARTAADAIRSALAQTRQALQSPDMKSAVVNTDLEAPYAEYERGLAGLLEKRRAAEAALTAIVSEYVDRTLPEATNDPGQANLPPPPTIPQATAPPRLASDSALWPKKPQLLTRRERDDLLQATGDFFSELLTEAEAAEVRALEEQVRESQTLMAKAHEMAASTRRGFHTALEAVLSRSRDEAPDDELRSLLPSPPKAPVQAPLEAALARAAAGNGSWPYRKSLAAAKWIRGICEAVRGLSEGALALAGGAGAWLNLAAAADGEIHELTRLLEVEGMAQNSMDGMEELRLALATLDPKRVAGGKETVADWKRRLSRLEAIIQEAQEESQLQGTLQDLVTQARGHTDPRQLKIVVEAARGLALGASAGSQYALLKDKLLRYASAKQSFLAFYETAQPTVFVKHPLTNNLPLLITISAPPTGWGNGAPTRRAQFLAAAGPAKYAGTLWLETESPCDPLNPAYVSADTQEPLNYIPVYHNFLEYVMPTVLENPEAFSLTPAGRPQAIGPPQDDQERRRRTLASVASARLSAAAADSYWDTWPDVESNAGELLREYVSAPKALMEDLADNPIVAMTLLAHASLIASRNHPPYPAPATDREVILLEQREMMALLVGTHPAYAAAFLGAPSFYAGLGLVSALARDGGLGDLLSDSVLTYRLVRSPASGRGGMPSTTRGSNDGEDARRLTRHRIAGPPTGFIFFQDAWEEMDTRAALWPHPEFLGLVHNQSTARARACMLLLARRCFAPEALQQLWHSLRPLEGPVAFQDYLRDFVKQAYTRGEELPRAEGLEVPRETPSSYGTVTGRALRNLMPYGTPITGPKRGSGDTIPVSVFEAAVAAAFLGRPLTLFVSSQYLFNLKTLGQVRVVAPLLYCDGHSEPFRSLVETISLNFLQDLDGYSESFEPEMSIFARQAVWLRELLTEARAAKPKEARPPTVAILANRKNIIWKCFTYRHNLPDVQFYFNAAGASRWPTDVLNPSFYEHEDPPLPVGYQLPPNPRNVQELFSGFPPRVGHGLVSGDGFQSADNTPASSDRLQQLGGGETDQGEKGSTTAESEASGPPSPQSPLLEKVAPGRPRDWLSPTSSPRDVTVTPGLAAPITLPGPRLMARPYFGAETRASESPDRSPGSSPRPWPKDSLELLPQPAPQQPPSSPWASEQGPIVYTLSPHSTPSTASGSQKKHTIQIPGLVPSQKPSYPPSAPYKPGQSTGGIAPTPSAASLTTFGLQPQDTQASSQDPPYGHSIMQREKKQQGGREEAAEIRPSATRLPTAVGLRPRAPVVAAGAAASATPAFDPGEAPSGFPIPQAPALGSGLAAPAHTPVGALAPRPQKTQAQRPQDAAALPTPTIKAVGARPVPKATGALAAGARPRGQPTAAPPSAASPPRVSLPVRSRQQQSPAIPLPPMHSGSEPGARPEVRLSQYRHAGPQTYTVRKEAPPSAASQLPKMPKCKDSMYYPPSGSARYPAPFQALSFSQSVASPAPSSDQTTLLWNTPSVVTQFLSIEDIIREVVTGGSTSGDLVVPSGSPSSLSTAAPEQDLRYSLTLSQASRVLSRFVSQLRRKLERSTHRLIADLERLKFLYL
Enzyme Length 3149
Uniprot Accession Number P03186
Absorption
Active Site ACT_SITE 61; /evidence="ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:20190741"; ACT_SITE 193; /evidence="ECO:0000255|HAMAP-Rule:MF_04044"; ACT_SITE 195; /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:20190741};
DNA Binding
EC Number 3.4.19.12; 3.4.22.-
Enzyme Function FUNCTION: Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein. {ECO:0000250|UniProtKB:P10220, ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:19244336, ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:22474075}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (15); Domain (1); Mutagenesis (1); Region (13); Repeat (8); Site (1)
Keywords 3D-structure;Host cytoplasm;Host nucleus;Host-virus interaction;Hydrolase;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway;Virion;Virion tegument
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:15534216}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04044, ECO:0000269|PubMed:15534216}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04044}. Note=Tightly associated with the capsid. {ECO:0000255|HAMAP-Rule:MF_04044}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (4)
Cross Reference PDB 6W2D; 6W2E; 7BQX; 7BR7;
Mapped Pubmed ID 32620850; 32719506;
Motif
Gene Encoded By
Mass 337,959
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.19.12;