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Large tegument protein deneddylase (EC 3.4.19.12) (EC 3.4.22.-)

 A0A0S2I7M2_HHV1         Unreviewed;      3133 AA.
A0A0S2I7M2;
17-FEB-2016, integrated into UniProtKB/TrEMBL.
17-FEB-2016, sequence version 1.
28-MAR-2018, entry version 12.
RecName: Full=Large tegument protein deneddylase {ECO:0000256|HAMAP-Rule:MF_04044};
EC=3.4.19.12 {ECO:0000256|HAMAP-Rule:MF_04044};
EC=3.4.22.- {ECO:0000256|HAMAP-Rule:MF_04044};
Name=UL36 {ECO:0000313|EMBL:ALO18709.1};
Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10298 {ECO:0000313|EMBL:ALO18709.1, ECO:0000313|Proteomes:UP000110586};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:ALO18709.1, ECO:0000313|Proteomes:UP000110586}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KOS 1.1 {ECO:0000313|EMBL:ALO18709.1};
PubMed=26547038; DOI=10.1016/j.virol.2015.09.026;
Colgrove R.C., Liu X., Griffiths A., Raja P., Deluca N.A.,
Newman R.M., Coen D.M., Knipe D.M.;
"History and genomic sequence analysis of the herpes simplex virus 1
KOS and KOS1.1 sub-strains.";
Virology 487:215-221(2015).
-!- 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:0000256|HAMAP-Rule:MF_04044}.
-!- CATALYTIC ACTIVITY: 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).
{ECO:0000256|HAMAP-Rule:MF_04044}.
-!- SUBUNIT: 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.
{ECO:0000256|HAMAP-Rule:MF_04044}.
-!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP-
Rule:MF_04044}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04044}.
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04044}. Note=Tightly
associated with the capsid. {ECO:0000256|HAMAP-Rule:MF_04044}.
-!- SIMILARITY: Belongs to the herpesviridae large tegument protein
family. {ECO:0000256|PROSITE-ProRule:PRU00854}.
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EMBL; KT887224; ALO18709.1; -; Genomic_DNA.
Proteomes; UP000110586; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
GO; GO:0019784; F:NEDD8-specific protease activity; IEA:InterPro.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-UniRule.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-UniRule.
GO; GO:0039693; P:viral DNA genome replication; IEA:InterPro.
HAMAP; MF_04044; HSV_LTP; 1.
InterPro; IPR005210; Herpes_LT_deneddylase.
InterPro; IPR034702; HSV_LTP.
InterPro; IPR006928; htUSP_central_domain.
Pfam; PF04843; Herpes_teg_N; 1.
Pfam; PF03586; Herpes_UL36; 1.
PROSITE; PS51521; HTUSP; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000110586};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04044};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04044};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04044};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04044};
Modulation of host ubiquitin pathway by viral deubiquitinase
{ECO:0000256|HAMAP-Rule:MF_04044};
Modulation of host ubiquitin pathway by virus {ECO:0000256|HAMAP-
Rule:MF_04044}; Protease {ECO:0000256|HAMAP-Rule:MF_04044};
Repeat {ECO:0000256|HAMAP-Rule:MF_04044};
Thiol protease {ECO:0000256|HAMAP-Rule:MF_04044};
Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_04044};
Virion {ECO:0000256|HAMAP-Rule:MF_04044, ECO:0000256|PROSITE-
ProRule:PRU00854};
Virion tegument {ECO:0000256|HAMAP-Rule:MF_04044, ECO:0000256|PROSITE-
ProRule:PRU00854}.
DOMAIN 20 238 Peptidase C76.
{ECO:0000259|PROSITE:PS51521}.
REGION 1 248 Deubiquitination activity.
{ECO:0000256|HAMAP-Rule:MF_04044}.
REGION 549 579 Interaction with inner tegument protein.
{ECO:0000256|HAMAP-Rule:MF_04044}.
COILED 992 1019 {ECO:0000256|SAM:Coils}.
COILED 1289 1323 {ECO:0000256|SAM:Coils}.
COILED 1585 1605 {ECO:0000256|SAM:Coils}.
COILED 1651 1671 {ECO:0000256|SAM:Coils}.
COILED 1715 1735 {ECO:0000256|SAM:Coils}.
ACT_SITE 40 40 {ECO:0000256|HAMAP-Rule:MF_04044,
ECO:0000256|PROSITE-ProRule:PRU00854}.
ACT_SITE 172 172 {ECO:0000256|HAMAP-Rule:MF_04044,
ECO:0000256|PROSITE-ProRule:PRU00854}.
ACT_SITE 174 174 {ECO:0000256|HAMAP-Rule:MF_04044,
ECO:0000256|PROSITE-ProRule:PRU00854}.
SITE 27 27 Important for catalytic activity.
{ECO:0000256|PROSITE-ProRule:PRU00854}.
SEQUENCE 3133 AA; 333186 MW; F485DBE2CC6D4FBC CRC64;
MIAGTPPHST MERGGDRDIV VTGARNQFAP DLEPGGSVSC MRSSLSFLSL IFDVGPRDVL
SAEAIEGCLV EGGEWTRATA GPGPPRMCSI VELPNFLEYP GARGGLRCVF SRVYGEVGFF
GEPAAGLLET QCPAHTFFAG PWALRPLSYT LLTIGPLGMG LFRDGDTAYL FDPHGLPEGT
PAFIAKVRAG DMYPYLTYYT RDRPDVRWAG AMVFFVPSGP EPAAPADLTA AALHLYGASE
TYMQDEAFSE RRVAITHPLR GEIAGLGEPC VGVGPREGGG GPGPHPPTAA QSPPPTRARR
DDRASETSRG TAGPSAKPEA KRPNRAPDDV WAVALKGTPP TDPPSADPPS AIPPPPPSAP
KTPAAEAAEE DDDDMRVLEM GVVPVGRHRA RYSAGLPKRR RPTWTPPSSV EDLTSGEKTK
RSAPPAKTKK KSTPKGKTPV GAAVPASVPE PVLASAPPDP AGPPVAEAGE DDGPMVPASS
QALEALKTRR SPEPPGADLA QLFEAHPNVA ATAVKFTACS ATLAREVAAC SRLTISALRS
PYPASPGLLE LCVIFFFERV LAFLIENGAR THTQAGVAGP AAALLEFTLS MLPRKTAVGD
FLASTRLSLA DVAAHLPLVQ HVLDENSLIG RLALAKLILV ARDVIRETDA FYGELADLEL
QLRAAPPANL YTRLGEWLLE RSQAHPDTLF APATPTHPEP LLYRVQALAK FARGEEIRVE
AEDRQMREAL DALARGVDAV SQHAGPLGVM PAPAGAAPQG APRPPPLGPE AVQVRLEEVR
TQARRAIEGA VKEYFYRGAV YSAKALQASD NNDRRFHVAS AAVVPVVQLL ESLPVFDQHT
RDIAQRAAIP APPPIATSPT AILLRDLIQR GQTLDAPEDL AAWLSVLTDA ANQGLIERKP
LDELARSIRD INDQQARRSS GLAELRRFDA LDAALGQQLD SDAAFVPAPG ASPYPDDGGL
SPEATRMAEE ALRQARAMDA AKLTAELAPD ARARLRERAR SLEAMLEGAR ERAKVARDAR
EKFLHKLQGV LRPLPDFVGL KACPAVLATL RASLPAGWSD LPEAVRGAPP EVTAALRADM
WGLLGQYRDA LEHPTPDTAT ALSGLHPSFV VVLKNLFADA PETPFLLQFF ADHAPIIAHA
VSNAINAGSA AVATADPAST VDAAVRAHRV LVDAVTALGA AASDPASPLA FLAAMADSAA
GYVKATRLAL DARGAIAQLT TLGSAAADLV VQVRRAANQP EGEHASLIQA ATRATTGARE
SLAGHEGRFG GLLHAEGTAG DHSPSGRALQ ELGKVIGATR RRADELEAAI ADLREKMAAQ
RARSSHERWA ADVEAVLDRV ESGAEFDVVE LRRLQALAGT HGYNPRDFRK RAEQALGTNA
KAVTLALETA LAFNPYTPEN QRHPMLPPLA AIHRIDWSAA FGAAADTYAD MFRVDTEPLA
RLLRLAGGLL ERAQANDGFI DYHEAVLHLS EDLGGVPALR QYVPFFQKGY AEYVDIRDRL
DALRADARRA IGSVALDLAA AAEEISAVRN DPAAAAELVR AGVTLPCPSE DALVACVAAL
ERVDQSPVKD TAYADYVAFV TRQDLADTKD AVVRAKQQRA EATERVTAGL REVLAARERR
AQLEAEGLAN LKTLLKVVAV PATVAKTLDQ ARSAEEIADQ VEILLDQTEK ARELDVQAVA
WLEHAQRTFE THPLNAASGD GPGLLTRQGA RLQALFDTRR RVEALRRSLE EAEAEWDEVW
GRFGRVRGGA WKSPEGFRAA CEQLRALQDT TNTVSGLRAQ RDYERLPAKY QGVLGAKSAE
RAGAVEELGG RVAQHADLSA RLRDEVVPRV AWEMNFDTLG GLLAEFDAVA GDLAPWAVEE
FRGARELIQR RMGLYSAYAK ATGQTGAGAA AAPAPLLVDL RALDARARAS APPGQEADPQ
MLRRRGEAYL RVSGGPGPLV LREATSTLDR PFAPSFLVPD GTPLQYALCF PAVTDKLGAL
LMCPEAACIR PPLPTDTLES ASTVTAMYVI TVINRLQLAL SDAQAANFQL FGRFVRHRQA
RWGASMDAAA ELYVALVATT LTREFGCRWA QLEWGGDAAA PGPPLGPHSS TRHRVSFNEN
DVLVALVASS PEHIYTFWRL DLVRQHEYMH LTLPRAFQNA ADSMLFVQRL TPHPDARIRV
LPVFSTGGPP TRGLMFGTRL ADWRRGKLSE TDPLAPWRSV PELGTERGAA LGKLSPAQAL
AAVSVLGRMC LPSTALAALW TCMFPDDYTE YDSFDALLTA RLESGQTLSP SGGREASPPA
PPNALYRPTG QHVAVPAAAT HRTPAARVTA MDLVLAAVLL GAPVVVALRN TTAFSRESEL
ELCLTLFDSR ARGPDAALRD AVSSDIETWA VRLLHADLNP IENACLAAQL PRLSALIAER
PLARGPPCLV LVDISMTPVA VLWENPDPPG PPDVRFVGSE ATEELPFVAG GEDVLAASAT
DEDPFLARAI LGRPFDASLL SGELFPGHPV YQRAPDDQSP SVPNPTPGPA DLVGTEGSLG
PGSLAPTLFT DATPGEPVPP RMWAWIHGLE ELASDDSGGP APLLAPDPLS PTADQSVPTS
QCAPRPPGPA VTAREARPGV PAESTRPAPV GPRDDFRRLP SPQSSPAPPD ATAPRPPASS
RASAASSSGS RARRHRRARS LARATQASAT TQGWRPPALP DTVAPVTDFA RPPAPPKPPE
PALHALVSGV PLPLGPQFAG QASPALPIDP VPPPVATGTV LPGGENRRPP LTSGPAPTPP
RVPVGGPQRR LTRPAVASLS ESRESLPSPW DPADPTAPVL GRNPAEPTSS SPAGPSPPPP
AVQPVTPPPT SGPPPTYLTL EGGVTPGGPV SRRPTTRQPV ATPTTSARPR GHLTVNRLSA
PQPQPQPQPQ PQPQPQPQPQ PQPQPQPQPP QPQPQPQPQP QPQPQPQPQP QPQPQPQPQP
QPQPQPQPQN GHVAPGEYPA VRFRAPQNRP SVPASASSTN PRTGSSLSGV SSWASSLALH
IDATPPPVSL LQTLYVSDDE DSDTTSLFLS DSEAEALDPL PREPHSPITN EPFSALSADD
SQEVTRLQFG PPPVSANAVL SRRYVQRTGR SALAVLIRAC YRLQQQLQRT RRALLHHSDA
VLTSLHHVRM LLG


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