LTP_GAHVM
ID LTP_GAHVM Reviewed; 3342 AA.
AC Q9E6N3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=MDV049;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14229.1; -; Genomic_DNA.
DR RefSeq; YP_001033965.1; NC_002229.3.
DR PRIDE; Q9E6N3; -.
DR GeneID; 4811510; -.
DR KEGG; vg:4811510; -.
DR Proteomes; UP000008072; 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..3342
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000406498"
FT DOMAIN 78..298
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..302
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 472..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..656
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 2584..2603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2654..2987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3196..3279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2586..2600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2699..2903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2905..2942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3222..3252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3265..3279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 232
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 234
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 85
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 3342 AA; 367314 MW; 49B6E04418E54890 CRC64;
MTDSTDSRQA TTNCRKYSRT TSNAPMLAAN VLRDKSTSGL CSLDRKHDPY FGQIMDNPEV
ILDEWAKMVI DTTDVTVVAV GIRNQFAPDL SPASSVSCLR SSLAFLRIVF AYGLDTVISS
DAIDRLLLQG KAWTIATSED GTYTTCVPHD LPNRIISKDA GGNLCVAFSS SYGEFEFYLE
ENTPTILDTQ ISARTFIEQI WKKKRGDVYC LIVVGVLGIG VYRSGDGIYI FDPHGHGHIG
QACIVRVSEG YFYQYLTSYA DPSATPDWSA TFVYFVSTVS ICPPRDEIIS TVSRIYGTSD
IVLDLGRARE EDNRKVVSAD FDPPSRPQPR LTKLVIGSTD TTIQGSDYPC IQAEDLNGED
SRPLDHNLSY NDAPTNTESV APPSTKDCRD CINIQNPGET LDDTHSTIVD PSTKDSISVT
AWQGVFSDVI EDPPPKTNFQ FSFGTFAKVA ENKIGTTSVE GCIRNYARHK RRRPLWTPQS
SSENISLDGS SSSLSRKHSR KSKRTLESRI VEAVTSTESS DVTENVDTYP PVISNIPDEP
TLGSSPTTSN RGEDTTVEHL LKNRPLFNFK SLTEDEDGLV QDRLWSDEYL SHYPLADIRD
KIEDVACSID SGLRIIVHVG SPYDSDGGLL YVCMMDIFAR LFNYIIENGA RTTSDRESVV
GYEMAALLKA FTIPVYFTTF IASTGMVLSE ASESIDLIER VLAENSKIGN LALSKMILVA
LEVEEVTDEL HKSLDAIEKE VGTADPYGIY ERMAAILVDT LYHNSGKLYS EKTSSNSNQT
LTDRVISLCT LIRDIEAVAI RKAELILAEM EALEAGVRWM NTTLDAFIMG GSGSSPMIDA
ADIVAKTSSA VVTQRLGDIG KTVIDVVGHS LREYYLKVAL YSVKALTASS SDVSRFKIVV
TDQYEKINRF ASSLSVIDDV MVLIASRSNA RVPSPVSQAF ESELLGNLLE IGSDLDVPEK
LTTWKNLMTS MQVGGWISRR ELDMLMKEID IVNEKATRHE TVLTELERLN ELETRFGSYT
DLDTTVELQK LDEAIKIGED IVKLAIVLED KKNATSLSSD VREKLRDTRR KNETFITHLR
ERYQEVKSTI EDLYSSIRKI LRPLPKFVGL RALDSKVKVI TESIPRGMGS FENFLASAPS
DIIGSLQSDL WVLFIQYKTI LSRPTTEVAA ELSGLGVPFA LAIRLVFGPQ GSYPAASVFF
GKHADVLSAT IAAAAVEPMS VEKTMAVVST LKAAISDIDR ANAIAPPQGI MSISSTERSD
AFLFLKALLS TAEIAADVAN RGQHLESLIQ SVRTILDNLI TSNHKIRSLN PREVISENDT
SVVASAKVEF SNAIQTVGNV TATLSTFEGL TYTSNPHIQR KIAELSKLIR SANQRAGELD
IAIQTYEHNR ISAERSRSED LWISSINSLL LNAEVKSEFD AMEINRLEDA ARTGGYDTIR
YKSRAEKIVI AHARVLESSI ESVLKFNPYS TQNMVHGLSP PIAALKSITW GDSFMTAAPY
YTKLFGVNCD TVMDLLHISI AILRHANANS GNVDYYLLMG ELESALKSYP NLVKYVNFYR
SGYVKFMSFL AHLEQRRVEA HHASGRVALE ISAALEDLAR THSPEGARRA LEYGVSIIIP
SVNTIMSIAE ELKKDHVEEL EGTAYSEYGA HLLRRDTDAM TSLIHRVTTA IEDAKTRGEA
ILKNLAEASY AADRESAELL ANLKNLLRLV SMPSHIAKAI DRSETVNDIV TQAALLLTKV
EETKELDSQT VEWLRHAESV IDSHDLTVRI DESGPMSIYA DRIDALVNLS KRLEELKSEL
ALAEVAWDDT WATFVHDKDR IDKSSEGFSS ARESAARTKV SVNMINALRS NAEYPRLPAK
IIGLIDTKYR DRVVVLDAFL TTVKEIEATQ KQMEGLCEKI PSTFAINDLK KIYTQFEDIA
KRLPKWYTKR VARYSRLLTL RLALYAGYSN TFEGNVGDPM LLPFDAGDAN NGANHTSNVG
VVNRYLKHRV ASWIRPKVVA TLQEAFSEID SPGCLTYLDS TDKPLRYSLC FRTVGEKLAA
CLCEPAAIGI KPQIPIQPIT TEETEAAAGM LSDIMTFRLG FVHDMANHLY SFTKYVRTKR
HNWMQSDYIK ALGTIYCALI AITLTRKNRS NLSDIYFIPG RRTPIVDKKE LKKNAANGRG
KQVVRLDPAD VMVTIMANIP GHMLTFSKLD LIDQYDFMDK TIYEVMTDSI STVAFVNCLS
VQLSKDNIPD PNCRPLSLTG SVWDPAGGSL FSVRYSDWRQ GKLSDTDPLK LWEDLDGDAA
DGLAKIRAAI PSSLLTTTTV LARMCIPPTA LAVIWSSLLP DGLEQNCKSY DDVVTARGDL
ASSLDVTTSL LSCSENKNIS SITDSPNLYD LTGNVTTFTV VSTPPSRVLR VNAMDIATTA
TLFGARIVIA AECPEAYSSE SGLSLCIRLF DSRHGSRGCF LEPTAVSSDM TSWGTKLLIT
DNNPIENACL GQQLEHLSRI VASKPLASAP PCLLIVDSGM APIKVLWSKE ILDPIPIIRL
ISEDDALISE LPYVDAGIRK EPELANEHMV IADVQEASKF FSDESRIYPC PIYNKCVSPD
LSRDGDADIS SNRIDSEDDT YADSMGSGYL SIDPESMWDR VVENDMEGAQ VQLLLPGDII
HHNDRHVSEN MNYPQIGHLD ISPNYRDPID ETSSNPPPFP KHSNLFPSDH DPTSESSSKP
TPAPKPTPAP KPTPAPKPTP APKPTPAPKP TPAPKPTPAP KPKPPPDPDF KPSPAPKPSP
ASKPTPAPKP SPAPKPKPPP DPDFKPTPAP KPSPASKPKP PPDPDFKPTP APKPKPPPDP
DFKPSPAPKP SPAPKPKPPP DPDFKPTPAP KPSPASKPSP ASKPKPPPAP DSKPSPAPKP
KPPPTPDSKP SPAPKPKSPS ASKPLPVLFP NSDSKTSPVP NPNTFSASKI PPTSSIAEET
KPCQSNLPAI PLITKPDSVK NGYTTLKTDD KRKGSQSRYR NEKSRKHMHN THTAVYNTTF
NWTGTAAASS RHDMELNQYS PGIVTFDNLI DKEGYRHESE TIPRESYSEH RKDLDWMSTP
TVIANASSSL ITNNDYGGIG GIDLKKYRFK NGTGLLRQGS PTTRLHCRKN NSSRSITDIL
VGTASPTNEP SPLLQRLKAH TISGDKKANM DAGTIRGRLY DYSSFWPPCI QGACSTSPKT
IDLKYLSSEQ ATVAYPKHDD THHQTPTGLA PNDKHSDMHI SSIITETDTK ENSIPGYNNI
PMRHSSESES LTSLDSDSDD SHLHVSGSTD TTTDGSSTSR VIPADALLTR RDFRNASRGA
LYALTKACKK VARQIVYVRE QLRTKVATLA IELFKIKMIL TG
