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

 LTP_VZVD                Reviewed;        2763 AA.
P09278;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
20-JUN-2018, entry version 88.
RecName: Full=Large tegument protein deneddylase {ECO:0000255|HAMAP-Rule:MF_04044};
EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_04044};
EC=3.4.22.- {ECO:0000255|HAMAP-Rule:MF_04044};
ORFNames=ORF22;
Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Varicellovirus.
NCBI_TaxID=10338;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=3018124;
Davison A.J., Scott J.E.;
"The complete DNA sequence of varicella-zoster virus.";
J. Gen. Virol. 67:1759-1816(1986).
-!- 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}.
-!- 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:0000255|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:0000255|HAMAP-Rule:MF_04044}.
-!- 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}.
-!- SIMILARITY: Belongs to the herpesviridae large tegument protein
family. {ECO:0000255|HAMAP-Rule:MF_04044}.
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EMBL; X04370; CAA27905.1; -; Genomic_DNA.
PIR; D27343; WZBE22.
ProteinModelPortal; P09278; -.
SMR; P09278; -.
PRIDE; P09278; -.
OrthoDB; VOG09000001; -.
Proteomes; UP000002602; 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-EC.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039693; P:viral DNA genome replication; IEA:InterPro.
HAMAP; MF_04044; HSV_LTP; 1.
InterPro; IPR005210; Herpes_LT_deneddylase.
InterPro; IPR006928; Herpes_teg_USP.
InterPro; IPR034702; HSV_LTP.
InterPro; IPR038765; Papain_like_cys_pep_sf.
Pfam; PF04843; Herpes_teg_N; 1.
Pfam; PF03586; Herpes_UL36; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PROSITE; PS51521; HTUSP; 1.
3: Inferred from homology;
Complete proteome; 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.
CHAIN 1 2763 Large tegument protein deneddylase.
/FTId=PRO_0000116037.
DOMAIN 12 237 Peptidase C76. {ECO:0000255|HAMAP-
Rule:MF_04044}.
REPEAT 2458 2460 1.
REPEAT 2461 2463 2.
REPEAT 2464 2466 3.
REPEAT 2467 2469 4.
REPEAT 2470 2472 5.
REGION 1 247 Deubiquitination activity.
{ECO:0000255|HAMAP-Rule:MF_04044}.
REGION 495 523 Interaction with inner tegument protein.
{ECO:0000255|HAMAP-Rule:MF_04044}.
REGION 2458 2472 5 X 3 AA repeats of P-A-Q.
COMPBIAS 331 335 Poly-Arg.
COMPBIAS 1367 1370 Poly-Leu.
COMPBIAS 2356 2359 Poly-Leu.
ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_04044}.
ACT_SITE 168 168 {ECO:0000255|HAMAP-Rule:MF_04044}.
ACT_SITE 170 170 {ECO:0000255|HAMAP-Rule:MF_04044}.
SITE 19 19 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_04044}.
SEQUENCE 2763 AA; 306343 MW; 0995F7745B9542F5 CRC64;
MDIIPPIAVT VAGVGSRNQF DGALGPASGL SCLRTSLSFL HMTYAHGINA TLSSDMIDGC
LQEGAAWTTD LSNMGRGVPD MCALVDLPNR ISYIKLGDTT STCCVLSRIY GDSHFFTVPD
EGFMCTQIPA RAFFDDVWMG REESYTIITV DSTGMAIYRQ GNISFIFDPH GHGTIGQAVV
VRVNTTDVYS YIASEYTHRP DNVESQWAAA LVFFVTANDG PVSEEALSSA VTLIYGSCDT
YFTDEQYCEK LVTAQHPLLL SPPNSTTIVL NKSSIVPLHQ NVGESVSLEA TLHSTLTNTV
ALDPRCSYSE VDPWHAVLET TSTGSGVLDC RRRRRPSWTP PSSEENLACI DDGLVNNTHS
TDNLHKPAKK VLKFKPTVDV PDKTQVAHVL PRLREVANTP DVVLNVSNVD TPESSPTFSR
NMNVGSSLKD RKPFLFEQSG DVNMVVEKLL QHGHEISNGY VQNAVGTLDT VITGHTNVPI
WVTRPLVMPD EKDPLELFIN LTILRLTGFV VENGTRTHHG ATSVVSDFIG PLGEILTGFP
SAAELIRVTS LILTNMPGAE YAIKTVLRKK CTIGMLIIAK FGLVAMRVQD TTGALHAELD
VLEADLGGSS PIDLYSRLST GLISILNSPI ISHPGLFAEL IPTRTGSLSE RIRLLCELVS
ARETRYMREH TALVSSVKAL ENALRSTRNK IDAIQIPEVP QEPPEETDIP PEELIRRVYE
IRSEVTMLLT SAVTEYFTRG VLYSTRALIA EQSPRRFRVA TASTAPIQRL LDSLPEFDAK
LTAIISSLSI HPPPETIQNL PVVSLLKELI KEGEDLNTDT ALVSWLSVVG EAQTAGYLSR
REFDELSRTI KTINTRATQR ASAEAELSCF NTLSAAVDQA VKDYETYNNG EVKYPEITRD
DLLATIVRAT DDLVRQIKIL SDPMIQSGLQ PSIKRRLETR LKEVQTYANE ARTTQDTIKS
RKQAAYNKLG GLLRPVTGFV GLRAAVDLLP ELASELDVQG ALVNLRTKVL EAPVEIRSQL
TGDFWALFNQ YRDILEHPGN ARTSVLGGLG ACFTAIIEIV PIPTEYRPSL LAFFGDVADV
LASDIATVST NPESESAINA VVATLSKATL VSSTVPALSF VLSLYKKYQA LQQEITNTHK
LTELQKQLGD DFSTLAVSSG HLKFISSSNV DDYEINDAIL SIQTNVHALM DTVKLVEVEL
QKLPPHCIAG TSTLSRVVKD LHKLVTMAHE KKEQAKVLIT DCERAHKQQT TRVLYERWTR
DIIACLEAME TRHIFNGTEL ARLRDMAAAG GFDIHAVYPQ ARQVVAACET TAVTALDTVF
RHNPYTPENT NIPPPLALLR GLTWFDDFSI TAPVFTVMFP GVSIEGLLLL MRIRAVVLLS
ADTSINGIPN YRDMILRTSG DLLQIPALAG YVDFYTRSYD QFITESVTLS ELRADIRQAA
GAKLTEANKA LEEVTHVRAH ETAKLALKEG VFITLPSEGL LIRAIEYFTT FDHKRFIGTA
YERVLQTMVD RDLKEANAEL AQFRMVCQAT KNRAIQILQN IVDTANATEQ QEDVDFTNLK
TLLKLTPPPK TIALAIDRST SVQDIVTQFA LLLGRLEEET GTLDIQAVDW MYQARNIIDS
HPLSVRIDGT GPLHTYKDRV DKLYALRTKL DLLRRRIETG EVTWDDAWTT FKRETGDMLA
SGDTYATSVD SIKALQASAS VVDMLCSEPE FFLLPVETKN RLQKKQQERK TALDVVLQKQ
RQFEETASRL RALIERIPTE SDHDVLRMLL RDFDQFTHLP IWIKTQYMTF RNLLMVRLGL
YASYAEIFPP ASPNGVFAPI PAMSGVCLED QSRCIRARVA AFMGEASVVQ TFREARSSID
ALFGKNLTFY LDTDGVPLRY RVCYKSVGVK LGTMLCSQGG LSLRPALPDE GIVEETTLSA
LRVANEVNEL RIEYESAIKS GFSAFSTFVR HRHAEWGKTN ARRAIAEIYA GLITTTLTRQ
YGVHWDKLIY SFEKHHLTSV MGNGLTKPIQ RRGDVRVLEL TLSDIVTILV ATTPVHLLNF
ARLDLIKQHE YMARTLRPVI EAAFRGRLLV RSLDGDPKGN ARAFFNAAPS KHKLPLALGS
NQDPTGGRIF AFRMADWKLV KMPQKITDPF APWQLSPPPG VKANVDAVTR IMATDRLATI
TVLGRMCLPP ISLVSMWNTL QPEEFAYRTQ DDVDIIVDAR LDLSSTLNAR FDTAPSNTTL
EWNTDRKVIT DAYIQTGATT VFTVTGAAPT HVSNVTAFDI ATTAILFGAP LVIAMELTSV
FSQNSGLTLG LKLFDSRHMA TDSGISSAVS PDIVSWGLRL LHMDPHPIEN ACLIVQLEKL
SALIANKPLT NNPPCLLLLD EHMNPSYVLW ERKDSIPAPD YVVFWGPESL IDLPYIDSDE
DSFPSCPDDP FYSQIIAGYA PQGPPNLDTT DFYPTEPLFK SPVQVVRSSK CKKMPVRPAQ
PAQPAQPAQP AQTVQPAQPI EPGTQIVVQN FKKPQSVKTT LSQKDIPLYV ETESETAVLI
PKQLTTSIKT TVCKSITPPN NQLSDWKNNP QQNQTLNQAF SKPILEITSI PTDDSISYRT
WIEKSNQTQK RHQNDPRMYN SKTVFHPVNN QLPSWVDTAA DAPQTDLLTN YKTRQPSPNF
PRDVHTWGVS SNPFNSPNRD LYQSDFSEPS DGYSSESENS IVLSLDEHRS CRVPRHVRVV
NADVVTGRRY VRGTALGALA LLSQACRRMI DNVRYTRKLL MDHTEDIFQG LGYVKLLLDG
TYI


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