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   24-JAN-2024, entry version 69.
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; Orthoherpesviridae; Alphaherpesvirinae; Iltovirus;
OC   Iltovirus psittacidalpha1; Psittacid alphaherpesvirus 1.
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   GeneID; 2657005; -.
DR   KEGG; vg:2657005; -.
DR   Proteomes; UP000006840; Segment.
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 symbiont 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   Gene3D; 3.90.70.120; -; 1.
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; Cysteine proteinases; 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
//