LTP_PSHV1
ID LTP_PSHV1 Reviewed; 3195 AA.
AC Q6UDJ5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Large tegument protein deneddylase {ECO:0000255|HAMAP-Rule:MF_04044};
DE EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_04044};
DE EC=3.4.22.- {ECO:0000255|HAMAP-Rule:MF_04044};
GN Name=UL36;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
CC -!- FUNCTION: Large tegument protein that plays multiple roles in the viral
CC cycle. During viral entry, remains associated with the capsid while
CC most of the tegument is detached and participates in the capsid
CC transport toward the host nucleus. Plays a role in the routing of the
CC capsid at the nuclear pore complex and subsequent uncoating. Within the
CC host nucleus, acts as a deneddylase and promotes the degradation of
CC nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes
CC nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These
CC modifications prevent host cell cycle S-phase progression and create a
CC favorable environment allowing efficient viral genome replication.
CC Participates later in the secondary envelopment of capsids. Indeed,
CC plays a linker role for the association of the outer viral tegument to
CC the capsids together with the inner tegument protein.
CC {ECO:0000255|HAMAP-Rule:MF_04044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04044};
CC -!- SUBUNIT: Interacts with host CUL1 and CUL4A; these interactions inhibit
CC the E3 ligase activity of cullins. Interacts with inner tegument
CC protein. Interacts with capsid vertex specific component CVC2.
CC Interacts with the major capsid protein/MCP. {ECO:0000255|HAMAP-
CC Rule:MF_04044}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-
CC Rule:MF_04044}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04044}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04044}. Note=Tightly associated with
CC the capsid. {ECO:0000255|HAMAP-Rule:MF_04044}.
CC -!- SIMILARITY: Belongs to the herpesviridae large tegument protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04044}.
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DR EMBL; AY372243; AAQ73715.1; -; Genomic_DNA.
DR RefSeq; NP_944409.1; NC_005264.1.
DR SMR; Q6UDJ5; -.
DR PRIDE; Q6UDJ5; -.
DR GeneID; 2657005; -.
DR KEGG; vg:2657005; -.
DR Proteomes; UP000006840; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019784; F:deNEDDylase activity; IEA:InterPro.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:InterPro.
DR HAMAP; MF_04044; HSV_LTP; 1.
DR InterPro; IPR005210; Herpes_LT_deneddylase.
DR InterPro; IPR006928; Herpes_teg_USP.
DR InterPro; IPR034702; HSV_LTP.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF04843; Herpes_teg_N; 1.
DR Pfam; PF03586; Herpes_UL36; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51521; HTUSP; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Host-virus interaction; Hydrolase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway;
KW Virion; Virion tegument.
FT CHAIN 1..3195
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000406796"
FT DOMAIN 10..242
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 287..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2407..2776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2829..3068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3128..3147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2472..2486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2502..2529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2594..2610
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2645..2673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2750..2770
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2863..2879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2955..3019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3020..3043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3046..3068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 173
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 17
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 3195 AA; 344441 MW; 04404B41D1563EFC CRC64;
MWPPGLGTVV AAASRSQFDA MYEEMCYAMC VETSAAFLRA CELAGPQAVQ SQNVLDTILD
QGAEITRTSV ACETLPGGVK RYNMIDCQEL PRLWRGSGQE PDMLLLHTTT FGNIPYDSTF
DYEEKVLMLN GQQLGEKAAA MAREGAAAVL VIGNRGLGVA FTGGRHDPVF VFDPHGWMGG
AAYMSRLPNP TSLTGFIADY VERRSGIVVT LTFLLWLYPD GWNIEQESPE LRVEVISAAL
RAISQPPDFV FLDQFSETVV SPALPVPMGA LRADRFAAKS IRAILARGTA PSPKKKPDSG
EHGLPAGRPK PPKRHTPRSQ NPALLDSTEK LSNLSPVKVK KPNKGKKMSV IAEPPSAAAR
TEQRGPGDSL GALAERPPWR LQGVRAAADV IAVPAASALA GLPEKPSDKL RGVLKYLPEA
PTGGLSLGSG NALWAAILGT RVASLTDRLL VFLVENGITI RKAESEVGFL LDPVLAALAH
RPDRGAVASL IGDTRLNLFA LVARKAALLR LTELRDDRVS AVLVHKVQQV SSAIVSDTKT
ISAKLGALVD EISSEHPADA YGTLEKELLA FSLEKTAVVE RPDETTAPIL ELVERAAEIV
DAIEKETRAK AEREDRARRA DEKLLAFAHS VWDEIDDIAG DVTRGVDVGS SQASAAASLA
KRERIDIPEP SSMPPREDYS ELKILDDKAK ANAQKITDSA GKMLKVYANV IDYSISAFTS
GTQSAIGRFA LASPALDHMK AWLDRIAYAD TLVDSLAGLT GRRESASPDW GRLSSLEPVR
ILEGLIETGA DLSSDENLNH WTFQLFGAHA AGFMPSPSKW ISAIHGINTR AHEVGLSATA
LAELETEIKA AEAMVADPGV RLECAKHALE SAKAAVAGKS DPEQKARLAA AQARAAKLVD
SCQRDLDEAK RLVDEATKRD AEIKKAAAAL LRPVEKYQGL RGLGRSMAAA GLSDDAVAGI
VAADTQVARV LRADAEAILA NYERDFAELR GAQLLGTSAP LLRAVNFIDP RSGLGLLEPG
SRIFLSEAND DLMDAVEDAR TTRNTDSCSR AISALERIKW VIVEAEGAGQ WPKFAVAAAR
ALEGLRAKAL IDDRAGLVRT TLAGMLKRAA IVSETVAKDT DDPEAAAERA LKFVEMARRE
LRELELTDAE ELSSQDYVAL ERALVELAEA SRQKSIGLKK HAWRSRLRTL LERDRDDGEF
SLDAWDQARD EGECYGGRDA VNDDLIKLAR AVIDGRIQLG LRLVRAFFAN NPYAAQASQA
LPGDARGPVE LLESIRVAKW IFAFPGVADT YEYLFGISVV KLKALCEIGE EIVEAFDAAG
SSDKNIDMHA FVQTVAGKLF QVSELTEFFD FYVRSYELFL DIRAALAETA GRVGALERTA
LEQLGAEERA AESIRDPEAA KERLERGDRD PDALTAMREL HGGLKLESKK QFEKTAYLEP
LEYGYAEARR ELERAIANVD AAKKLSQARV KDFLSSLLRE REANDQELSR NLKTLKSVLA
ARSPKDVVAA LNGAETLDAV VKIYADRLAE AEAENEAAIV GAETMEWLKF AAKTIDGSKM
ARETGGVGPT AAYAERLEKL CRARADADAK LKRLKDLYES FELALASAKE AGGKQKDESE
DGWRRYEAAA NNLLTSAEAL GAQLRDEGNE QAGIKLLLLR EPAAAAYEKG LENAAAVIKD
VRTTLDDTSA GMRRLLTLYE AAKTEFAKPG LERLQKEISY AIAKYPVPKW FLALHAAVGK
LVELRLGLYH AYEGLKISTI PYAPVAPESE YVMPDAALTA ARVTAYMARS GKSVMTVTTH
SLGIVGRAVV DEANQILEYK LCYATVSEKV AALWAAGSRL GAGQFGGLVL RDARDERGVE
KFLGRGHAAV SLAATAAWLS GADTMITAEL GSYVTFCATG HWPAMRDRKQ LSMTVAACTT
YCALAYATLT STYGSAADTA VDSHGQFVPP EKFEAANTSG AVAAGAARGA KRKFALSIQD
VLILLAACEP AHLTYFCRLD LLRQVEYMHK TLEAVLSRAV RDRVGVSCLE PPKADDTRKY
MPVVMPAARG RFDKSYGACF AIDRHDWDSV KAPHYVGKML EPWKTLPGTR ENAERLERIC
GGTADAADGF TATLMMLAAT AIPANLLEAM WALLGPRDED LGENWQLGEG EVEGQWSGGA
ASAAAAAMLR FMLRRAAAVD NYTVATSGGT AGLALDSLSA KLLGPAGGSI MFLLKEDAVN
LRRLLAFDVA LLSILFGAKV VIAYETSALS RESGLLLCSS VFDARRGNRF ADILCADHRA
CASDSAAAAA DALKKIALAD PNRIENACLL QQVEELASAL HSKPLSYAQP FLFLANTSNQ
ITQVLIPAKA RPSEFFVTLR RDAAYEEVPL RRADRQAFPD EIDAKDIEGG DLFFSATVGG
EVPVLDNPAH IAPAPPEYDR GEGNLFPFAG SRRSAPSEEE ALSKAAGSKR NQIDAHGQNI
SQPARAGNTK IERASGKNRK TENNVTEHQT AARGRAAAPP TETKTTEKRQ KCPPRESPLS
RDERAPHDGL SAGAAEPRPP RGDSDDDRHK HETPHGVSDK AAEPPAVPSA EPRGPSTELI
GGNWKSLPKT KPRRTSSGLR RKHQASASVH KHRTHGSSDD DSEDGEATYG FGSCRGRQRR
STLGGKKRSG TDRTAEFLKK ATCVDKLEKF SRSGESPKAQ NGTADVACDR LGERGNELSP
PRAPASSPPP PGKQADHGID QREIVPPNAQ YGITTVVDPR QVRLPSSDDG DPAEEEDARD
VEEGEEDVAG QWDSNYDVCL PTYDTDHAAQ EEKDFDLASN NGTGGALPAA DHAISAINDW
VIADTDASAG VGTDWSEEDE DAPAADDGRS TNVEVATHGY TSDDSAADDE SKRARATRDS
SPPQHYPASP LAPSTPSSLP TPADTDNDTA ILELDRNSGG DTDSNDDHAP PTDTGDAPPL
CSEGELTPST DEECAVVQDD ARKKQENSSH ERKDDGVRWE IDLDSDQGDY SDASDDCKIP
DGPRVAPEKD IKNKQLEKSE SDSCGGQGDP STEPQQPLWE VYSPYDNSDS DDKAGNRKDP
KLDGAALDMR SSRLRADAKS ITSYVNDINE AVRDGGSAAA EFFARSEQSC IDSEDDARHL
DKSRATLASD LDDHQSDQPR ESLAPLDPET RSKMYTSLAV TCRLILRGMR HAQDAASAGV
AELLTETNRI KMMLN
