| IED ID | IndEnz0002016360 |
| Enzyme Type ID | protease016360 |
| Protein Name |
Large tegument protein deneddylase EC 3.4.19.12 EC 3.4.22.- |
| Gene Name | ORF22 |
| Organism | Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Alphaherpesvirinae Varicellovirus Human herpesvirus 3 (HHV-3) (Varicella-zoster virus) Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3) |
| Enzyme Sequence | MDIIPPIAVTVAGVGSRNQFDGALGPASGLSCLRTSLSFLHMTYAHGINATLSSDMIDGCLQEGAAWTTDLSNMGRGVPDMCALVDLPNRISYIKLGDTTSTCCVLSRIYGDSHFFTVPDEGFMCTQIPARAFFDDVWMGREESYTIITVDSTGMAIYRQGNISFIFDPHGHGTIGQAVVVRVNTTDVYSYIASEYTHRPDNVESQWAAALVFFVTANDGPVSEEALSSAVTLIYGSCDTYFTDEQYCEKLVTAQHPLLLSPPNSTTIVLNKSSIVPLHQNVGESVSLEATLHSTLTNTVALDPRCSYSEVDPWHAVLETTSTGSGVLDCRRRRRPSWTPPSSEENLACIDDGLVNNTHSTDNLHKPAKKVLKFKPTVDVPDKTQVAHVLPRLREVANTPDVVLNVSNVDTPESSPTFSRNMNVGSSLKDRKPFLFEQSGDVNMVVEKLLQHGHEISNGYVQNAVGTLDTVITGHTNVPIWVTRPLVMPDEKDPLELFINLTILRLTGFVVENGTRTHHGATSVVSDFIGPLGEILTGFPSAAELIRVTSLILTNMPGAEYAIKTVLRKKCTIGMLIIAKFGLVAMRVQDTTGALHAELDVLEADLGGSSPIDLYSRLSTGLISILNSPIISHPGLFAELIPTRTGSLSERIRLLCELVSARETRYMREHTALVSSVKALENALRSTRNKIDAIQIPEVPQEPPEETDIPPEELIRRVYEIRSEVTMLLTSAVTEYFTRGVLYSTRALIAEQSPRRFRVATASTAPIQRLLDSLPEFDAKLTAIISSLSIHPPPETIQNLPVVSLLKELIKEGEDLNTDTALVSWLSVVGEAQTAGYLSRREFDELSRTIKTINTRATQRASAEAELSCFNTLSAAVDQAVKDYETYNNGEVKYPEITRDDLLATIVRATDDLVRQIKILSDPMIQSGLQPSIKRRLETRLKEVQTYANEARTTQDTIKSRKQAAYNKLGGLLRPVTGFVGLRAAVDLLPELASELDVQGALVNLRTKVLEAPVEIRSQLTGDFWALFNQYRDILEHPGNARTSVLGGLGACFTAIIEIVPIPTEYRPSLLAFFGDVADVLASDIATVSTNPESESAINAVVATLSKATLVSSTVPALSFVLSLYKKYQALQQEITNTHKLTELQKQLGDDFSTLAVSSGHLKFISSSNVDDYEINDAILSIQTNVHALMDTVKLVEVELQKLPPHCIAGTSTLSRVVKDLHKLVTMAHEKKEQAKVLITDCERAHKQQTTRVLYERWTRDIIACLEAMETRHVFNGTELARLRDMAAAGGFDIHAVYPQARQVVAACETTAVTALDTVFRHNPHTPENTNIPPPLALLRGLTWFDDFSITAPVFTVMFPGVSIEGLLLLMRIRAVVLLSADTSINGIPNYRDMILRTSGDLLQIPALAGYVDFYTRSYDQFITESVTLSELRADIRQAAGAKLTEANKALEEVTHVRAHETAKLALKEGVFITLPSEGLLIRAIEYFTTFDHKRFIGTAYERVLQTMVDRDLKEANAELAQFRMVCQATKNRAIQILQNIVDTANATEQQEDVDFTNLKTLLKLTPPPKTIALAIDRSTSVQDIVTQFALLLGRLEEETGTLDIQAVDWMYQARNIIDSHPLSVRIDGTGPLHTYKDRVDKLYALRTKLDLLRRRIETGEVTWDDAWTTFKRETGDMLASGDTYATSVDSIKALQASASVVDMLCSEPEFFLLPVETKNRLQKKQQERKTALDVVLQKQRQFEETASRLRALIERIPTESDHDVLRMLLHDFDQFTHLPIWIKTQYMTFRNLLMVRLGLYASYAEIFPPASPNGVFAPIPAMSGVCLEDQSRCIRARVAAFMGEASVVQTFREARSSIDALFGKNLTFYLDTDGVPLRYRVCYKSVGVKLGTMLCSQGGLSLRPALPDEGIVEETTLSALRVANEVNELRIEYESAIKSGFSAFSTFVRHRHAEWGKTNARRAIAEIYAGLITTTLTRQYGVHWDKLIYSFEKHHLTSVMGNGLTKPIQRRGDVRVLELTLSDIVTILVATTPVHLLNFARLDLIKQHEYMARTLRPVIEAAFRGRLLVRSLDGDPKGNARAFFNAAPSKHKLPLALGSNQDPTGGRIFAFRMADWKLVKMPQKITDPFAPWQLSPPPGVKANVDAVTRIMATDRLATITVLGRMCLPPISLVSMWNTLQPEEFAYRTQDDVDIIVDARLDLSSTLNARFDTAPSNTTLEWNTDRKVITDAYIQTGATTVFTVTGAAPTHVSNVTAFDIATTAILFGAPLVIAMELTSVFSQNSGLTLGLKLFDSRHMATDSGISSAVSPDIVSWGLRLLHMDPHPIENACLIVQLEKLSALIANKPLTNNPPCLLLLDEHMNPSYVLWERKDSIPAPDYVVFWGPESLIDLPYIDSDEDSFPSCPDDPFYSQIIAGYAPQGPPNLDTTDFYPTEPLFKSPVQVVRSSKCKKMPVQPVQPAQPVQPAQPAQPVQPAQPIEPGTQIVVQNFKKPQSVKTTLSQKDIPLYVETESETAVLIPKQLTTSIKTTVCKSITPPNNQLSDWKNNPQQNQTLNQAFNKPILEITSIPTDDSISYRTWIEKSNQTQKRHQNDPRMYNSKTVFHPVNNQLPSWVDTAADAPQTDLLTNYKTRQPSPNFPRDVHTWGVSSNPFNSPNRDLYESDFSEPSDGYSSESENSIVLSLDEHRSCRVPRHVRVVNADVVTGRRYVRGTALGALALLSQACRRMIDNVRYTRKLLMDHTEDIFQGLGYVKLLLDGTYI |
| Enzyme Length | 2763 |
| Uniprot Accession Number | Q4JQX9 |
| Absorption | |
| Active Site | ACT_SITE 32; /evidence=ECO:0000255|HAMAP-Rule:MF_04044; ACT_SITE 168; /evidence=ECO:0000255|HAMAP-Rule:MF_04044; ACT_SITE 170; /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}; |
| 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:0000255|HAMAP-Rule:MF_04044}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Natural variant (1); Region (4); Repeat (8); Site (1) |
| Keywords | Host cytoplasm;Host nucleus;Host-virus interaction;Hydrolase;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Protease;Repeat;Thiol protease;Ubl conjugation pathway;Virion;Virion tegument |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04044}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04044}. 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16339411; 20205919; |
| Motif | |
| Gene Encoded By | |
| Mass | 306,336 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |