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Protein

Large tegument protein deneddylase

Gene

UL36

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation9 Publications

Catalytic activityi

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).UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei52Important for catalytic activityUniRule annotation1
Active sitei65UniRule annotation1 Publication1
Active sitei197UniRule annotation1
Active sitei199UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • modulation by virus of host protein ubiquitination Source: UniProtKB-KW
  • nuclear capsid assembly Source: AgBase
  • viral DNA genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Host-virus interaction, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway

Protein family/group databases

MEROPSiC76.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Large tegument protein deneddylaseUniRule annotation (EC:3.4.19.12UniRule annotation1 Publication, EC:3.4.22.-UniRule annotation1 Publication)
Gene namesi
ORF Names:UL36
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome

Subcellular locationi

  • Virion tegument UniRule annotation1 Publication
  • Host cytoplasm UniRule annotation3 Publications
  • Host nucleus UniRule annotation2 Publications

  • Note: Tightly associated with the capsid.UniRule annotation

GO - Cellular componenti

  • host cell cytoplasm Source: AgBase
  • host cell nucleus Source: UniProtKB-SubCell
  • viral tegument Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Virion, Virion tegument

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65C → A: Complete loss of deubiquitination activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001160351 – 3164Large tegument protein deneddylaseAdd BLAST3164

Post-translational modificationi

Proteolytically processed, possibly into several polypeptides. Enzymatic activity is only detectable following cleavage of the UL36 protein, which occurs late during viral replication.1 Publication

Proteomic databases

PRIDEiP10220.

Interactioni

Subunit structurei

Interacts with host CUL1 and CUL4A; these interactions inhibit the E3 ligase activity of cullins. Interacts with inner tegument protein. Interacts with capsid vertex specific component CVC2. Interacts with the major capsid protein/MCP (By similarity). Interacts with VP16; this interaction is important for outer tegument association to the capsid. May form homodimers.UniRule annotationBy similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UL37P102212EBI-7694334,EBI-6880600

Protein-protein interaction databases

BioGridi971402. 4 interactors.
IntActiP10220. 3 interactors.
MINTiMINT-6732711.

Structurei

Secondary structure

13164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1625 – 1665Combined sources41
Helixi1672 – 1678Combined sources7
Helixi1684 – 1720Combined sources37
Turni1723 – 1725Combined sources3
Beta strandi1729 – 1731Combined sources3
Helixi1736 – 1738Combined sources3
Helixi1739 – 1746Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TT0X-ray2.60A/B1625-1757[»]
4TT1X-ray2.75A/B1625-1757[»]
ProteinModelPortaliP10220.
SMRiP10220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 263Peptidase C76UniRule annotationAdd BLAST219
Repeati2911 – 291212
Repeati2913 – 291422
Repeati2915 – 291632
Repeati2917 – 291842
Repeati2919 – 292052
Repeati2921 – 292262
Repeati2923 – 292472
Repeati2925 – 292682
Repeati2927 – 292892
Repeati2929 – 2930102
Repeati2931 – 2932112
Repeati2933 – 2934122
Repeati2935 – 2936132
Repeati2937 – 2938142
Repeati2939 – 2940152
Repeati2941 – 2942162
Repeati2943 – 2944172
Repeati2945 – 2946182
Repeati2947 – 2948192
Repeati2949 – 2950202
Repeati2951 – 2952212
Repeati2953 – 2954222
Repeati2955 – 2956232
Repeati2957 – 2958242
Repeati2959 – 2960252
Repeati2961 – 2962262
Repeati2963 – 2964272
Repeati2965 – 2966282
Repeati2967 – 2968292
Repeati2969 – 2970302
Repeati2971 – 2972312
Repeati2973 – 2974322
Repeati2975 – 2976332
Repeati2977 – 2978342
Repeati2979 – 2980352

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 273Deubiquitination activityUniRule annotationAdd BLAST273
Regioni426 – 432Nuclear localization signal2 Publications7
Regioni579 – 609Interaction with inner tegument proteinUniRule annotationAdd BLAST31
Regioni579 – 609Interaction with UL371 PublicationAdd BLAST31
Regioni2911 – 298035 X 2 AA tandem repeats of P-QAdd BLAST70

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi307 – 494Pro-richAdd BLAST188
Compositional biasi1161 – 1288Ala-richAdd BLAST128

Sequence similaritiesi

Belongs to the herpesviridae large tegument protein family.UniRule annotation
Contains 1 peptidase C76 domain.UniRule annotation

Keywords - Domaini

Repeat

Family and domain databases

HAMAPiMF_04044. HSV_LTP. 1 hit.
InterProiIPR005210. Herpes_LT_deneddylase.
IPR006928. htUSP.
[Graphical view]
PfamiPF04843. Herpes_teg_N. 1 hit.
PF03586. Herpes_UL36. 1 hit.
[Graphical view]
PROSITEiPS51521. HTUSP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGGNNTNPG GPVHKQAGSL ASRAHMIAGT PPHSTMERGG DRDIVVTGAR
60 70 80 90 100
NQFAPDLEPG GSVSCMRSSL SFLSLIFDVG PRDVLSAEAI EGCLVEGGEW
110 120 130 140 150
TRATAGPGPP RMCSIVELPN FLEYPGARGG LRCVFSRVYG EVGFFGEPAA
160 170 180 190 200
GLLETQCPAH TFFAGPWALR PLSYTLLTIG PLGMGLFRDG DTAYLFDPHG
210 220 230 240 250
LPEGTPAFIA KVRAGDMYPY LTYYTRDRPD VRWAGAMVFF VPSGPEPAAP
260 270 280 290 300
ADLTAAALHL YGASETYLQD EAFSERRVAI THPLRGEIAG LGEPCVGVGP
310 320 330 340 350
REGVGGPGPH PPTAAQSPPP TRARRDDRAS ETSRGTAGPS AKPEAKRPNR
360 370 380 390 400
APDDVWAVAL KGTPPTDPPS ADPPSADPPS AIPPPPPSAP KTPAAEAAEE
410 420 430 440 450
DDDDMRVLEM GVVPVGRHRA RYSAGLPKRR RPTWTPPSSV EDLTSGEKTK
460 470 480 490 500
RSAPPAKTKK KSTPKGKTPV GAAVPASVPE PVLASAPPDP AGPPVAEAGE
510 520 530 540 550
DDGPTVPASS QALEALKTRR SPEPPGADLA QLFEAHPNVA ATAVKFTACS
560 570 580 590 600
AALAREVAAC SRLTISALRS PYPASPGLLE LCVIFFFERV LAFLIENGAR
610 620 630 640 650
THTQAGVAGP AAALLEFTLN MLPWKTAVGD FLASTRLSLA DVAAHLPLVQ
660 670 680 690 700
HVLDENSLIG RLALAKLILV ARDVIRETDA FYGELADLEL QLRAAPPANL
710 720 730 740 750
YTRLGEWLLE RSQAHPDTLF APATPTHPEP LLYRVQALAK FARGEEIRVE
760 770 780 790 800
AEDRQMREAL DALARGVDAV SQHAGPLGVM PAPAGAAPQG APRPPPLGPE
810 820 830 840 850
AVQVRLEEVR TQARRAIEGA VKEYFYRGAV YSAKALQASD NNDRRFHVAS
860 870 880 890 900
AAVVPVVQLL ESLPVFDQHT RDIAQRAAIP APPPIATSPT AILLRDLIQR
910 920 930 940 950
GQTLDAPEDL AAWLSVLTDA ANQGLIERKP LDELARSIRD INDQQARRSS
960 970 980 990 1000
GLAELRRFDA LDAALGQQLD SDAAFVPAPG ASPYPDDGGL SPEATRMAEE
1010 1020 1030 1040 1050
ALRQARAMDA AKLTAELAPD ARARLRERAR SLEAMLEGAR ERAKVARDAR
1060 1070 1080 1090 1100
EKFLHKLQGV LRPLPDFVGL KACPAVLATL RASLPAGWSD LPEAVRGAPP
1110 1120 1130 1140 1150
EVTAALRADM WGLLGQYRDA LEHPTPDTAT ALSGLHPSFV VVLKNLFADA
1160 1170 1180 1190 1200
PETPFLLQFF ADHAPIIAHA VSNAINAGSA AVATADPAST VDAAVRAHRV
1210 1220 1230 1240 1250
LVDAVTALGA AASDPASPLA FLAAMADSAA GYVKATRLAL DARVAIAQLT
1260 1270 1280 1290 1300
TLGSAAADLV VQVRRAANQP EGEHASLIQA ATRATTGARE SLAGHEGRFG
1310 1320 1330 1340 1350
GLLHAEGTAG DHSPSGRALQ ELGKVIGATR RRADELEAAT ADLREKMAAQ
1360 1370 1380 1390 1400
RARSSHERWA ADVEAVLDRV ESGAEFDVVE LRRLQALAGT HGYNPRDFRK
1410 1420 1430 1440 1450
RAEQALGTNA KAVTLALETA LAFNPYTPEN QRHPMLPPLA AIHRIDWSAA
1460 1470 1480 1490 1500
FGAAADTYAD MFRVDTEPLA RLLRLAGGLL ERAQANDGFI DYHEAVLHLS
1510 1520 1530 1540 1550
EDLGGVPALR QYVPFFQKGY AEYVDIRDRL DALRADARRA IGSVALDLAA
1560 1570 1580 1590 1600
AAEEISAVRN DPAAAAELVR AGVTLPCPSE DALVACVAAL ERVDQSPVKD
1610 1620 1630 1640 1650
TAYAHYVAFV TRQDLADTKD AVVRAKQQRA EATERVTAGL REVLAARERR
1660 1670 1680 1690 1700
AQLEAEGLAN LKTLLKVVAV PATVAKTLDQ ARSAEEIADQ VEILVDQTEK
1710 1720 1730 1740 1750
ARELDVQAVA WLEHAQRTFE THPLSAASGD GPGLLTRQGA RLQALFDTRR
1760 1770 1780 1790 1800
RVEALRRSLE EAEAEWDEVW GRFGRVRGGA WKSPEGFRAA CEQLRALQDT
1810 1820 1830 1840 1850
TNTVSGLRAQ RDYERLPAKY QGVLGAKSAE RAGAVEELGG RVAQHADLSA
1860 1870 1880 1890 1900
RLRDEVVPRV AWEMNFDTLG GLLAEFDAVA GDLAPWAVEE FRGARELIQR
1910 1920 1930 1940 1950
RMGLYSAYAK ATGQTGAGAA AAPAPLLVDL RALDARARAS APPGQEADPQ
1960 1970 1980 1990 2000
MLRRRGEAYL RVSGGPGPLV LREATSTLDR PFAPSFLVPD GTPLQYALCF
2010 2020 2030 2040 2050
PAVTDKLGAL LMCPEAACIR PPLPTDTLES ASTVTAMYVL TVINRLQLAL
2060 2070 2080 2090 2100
SDAQAANFQL FGRFVRHRQA RWGASMDAAA ELYVALVATT LTREFGCRWA
2110 2120 2130 2140 2150
QLEWGGDAAA PGPPLGPQSS TRHRVSFNEN DVLVALVASS PEHIYTFWRL
2160 2170 2180 2190 2200
DLVRQHEYMH LTLPRAFQNA ADSMLFVQRL TPHPDARIRV LPAFSAGGPP
2210 2220 2230 2240 2250
TRGLMFGTRL ADWRRGKLSE TDPLAPWRSV PELGTERGAA LGKLSPAQAL
2260 2270 2280 2290 2300
AAVSVLGRMC LPSTALVALW TCMFPDDYTE YDSFDALLTA RLESGQTLSP
2310 2320 2330 2340 2350
SGGREASPPA PPNALYRPTG QHVAVPAAAT HRTPAARVTA MDLVLAAVLL
2360 2370 2380 2390 2400
GAPVVVALRN TTAFSRESEL ELCLTLFDSR ARGPDAALRD AVSSDIETWA
2410 2420 2430 2440 2450
VRLLHADLNP IENACLAAQL PRLSALIAER PLARGPPCLV LVDISMTPVA
2460 2470 2480 2490 2500
VLWENPDPPG PPDVRFVGSE ATEELPFVAG GEDVLAASAT DEDPFLARAI
2510 2520 2530 2540 2550
LGRPFDASLL SGELFPGHPV YQRAPDDQSP SVPNPTPGPV DLVGAEGSLG
2560 2570 2580 2590 2600
PGSLAPTLFT DATPGEPVPP RMWAWIHGLE ELASDDSGGP APLLAPDPLS
2610 2620 2630 2640 2650
PTADQSVPTS QCAPRPPGPA VTAREARPGV PAESTRPAPV GPRDDFRRLP
2660 2670 2680 2690 2700
SPQSSPAPPD ATAPRPPASS RASAASSSGS RARRHRRARS LARATQASAT
2710 2720 2730 2740 2750
TQGWRPPALP DTVAPVTDFA RPPAPPKPPE PAPHALVSGV PLPLGPQAAG
2760 2770 2780 2790 2800
QASPALPIDP VPPPVATGTV LPGGENRRPP LTSGPAPTPP RVPVGGPQRR
2810 2820 2830 2840 2850
LTRPAVASLS ESRESLPSPW DPADPTAPVL GRNPAEPTSS SPAGPSPPPP
2860 2870 2880 2890 2900
AVQPVAPPPT SGPPPTYLTL EGGVAPGGPV SRRPTTRQPV ATPTTSARPR
2910 2920 2930 2940 2950
GHLTVSRLSA PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ
2960 2970 2980 2990 3000
PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPQ NGHVAPGEYP AVRFRAPQNR
3010 3020 3030 3040 3050
PSVPASASST NPRTGSSLSG VSSWASSLAL HIDATPPPVS LLQTLYVSDD
3060 3070 3080 3090 3100
EDSDATSLFL SDSEAEALDP LPGEPHSPIT NEPFSALSAD DSQEVTRLQF
3110 3120 3130 3140 3150
GPPPVSANAV LSRRYVQRTG RSALAVLIRA CYRLQQQLQR TRRALLHHSD
3160
AVLTSLHHVR MLLG
Length:3,164
Mass (Da):335,862
Last modified:July 1, 1989 - v1
Checksum:iCC5D31FF4F9FE3F4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti234A → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti307P → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti375 – 379Missing in strain: Nonneuroinvasive mutant HF10. 5
Natural varianti392T → P in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti620N → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti624W → R in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti671A → V in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti885I → M in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1023A → V in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1244V → G in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1373G → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1389G → D in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1419T → M in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1470A → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1604A → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1605H → D in strain: 17 syn+ and Nonneuroinvasive mutant HF10. 1
Natural varianti1642E → D in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1695V → L in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1729G → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1777R → C in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1888V → M in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti1973E → K in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2267V → A in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2540V → A in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2545A → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2646F → V in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2666P → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2748A → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2856A → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2875A → T in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2894T → A in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti2973 – 2978Missing in strain: Nonneuroinvasive mutant HF10. 6
Natural varianti3095V → A in strain: Nonneuroinvasive mutant HF10. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32311.1.
DQ889502 Genomic DNA. Translation: ABI63498.1.
FJ593289 Genomic DNA. Translation: ACM62259.1.
PIRiI30085. WMBEH6.
RefSeqiYP_009137111.1. NC_001806.2.

Genome annotation databases

GeneIDi2703357.
KEGGivg:2703357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32311.1.
DQ889502 Genomic DNA. Translation: ABI63498.1.
FJ593289 Genomic DNA. Translation: ACM62259.1.
PIRiI30085. WMBEH6.
RefSeqiYP_009137111.1. NC_001806.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TT0X-ray2.60A/B1625-1757[»]
4TT1X-ray2.75A/B1625-1757[»]
ProteinModelPortaliP10220.
SMRiP10220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971402. 4 interactors.
IntActiP10220. 3 interactors.
MINTiMINT-6732711.

Protein family/group databases

MEROPSiC76.001.

Proteomic databases

PRIDEiP10220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703357.
KEGGivg:2703357.

Family and domain databases

HAMAPiMF_04044. HSV_LTP. 1 hit.
InterProiIPR005210. Herpes_LT_deneddylase.
IPR006928. htUSP.
[Graphical view]
PfamiPF04843. Herpes_teg_N. 1 hit.
PF03586. Herpes_UL36. 1 hit.
[Graphical view]
PROSITEiPS51521. HTUSP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLTP_HHV11
AccessioniPrimary (citable) accession number: P10220
Secondary accession number(s): B9VQG4, Q09I97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.