LTP_EHV2
ID LTP_EHV2 Reviewed; 3755 AA.
AC Q66666;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=64;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(1995).
RN [2]
RP SEQUENCE REVISION.
RA Davison A.J.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; U20824; AAC13852.2; -; Genomic_DNA.
DR PIR; S55659; S55659.
DR RefSeq; NP_042661.2; NC_001650.2.
DR PRIDE; Q66666; -.
DR GeneID; 1461044; -.
DR KEGG; vg:1461044; -.
DR Proteomes; UP000007083; 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:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_04044; HSV_LTP; 1.
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 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..3755
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000406058"
FT DOMAIN 27..241
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..251
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 260..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2565..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3135..3678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2571..2590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3147..3168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3169..3193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3386..3400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3425..3443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3564..3580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3581..3597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3619..3634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3658..3674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 3755 AA; 403660 MW; 91A13D4607CED354 CRC64;
MEGIKIDELD LKTQAIFLHY QKFTLEGLAS NHQGVACKFG RYAGMQCLSN CTAYLLYTYY
NGGVPLKDRT ELDHVLNVGS KIDFVLRQGG SIAPDQYVQI AEIPGTVITS QVNCHIYQSN
EIFGLLGVDA PVIHDDVRSL KHVLTRNYNR VTQYMICICN AMALAVVIKD KRYYLFNPHC
VPGIANSVAH VISTPDADDL VSYVGPTGVE YTGAFLYFVP AEVDIGNHAA FIANHYKVLR
FNRPNAIQVD VSEADGGGAC IRELPKDSSD GAPADGNSAP PLESKRTRSA ESAKEVGQKL
VKRRQKKGFA PYTKSKPPNG RDEAAADEVA RVLPNTGATP ERTVSPGVAP MSEDRPASED
FYPDSEHPDS DFSDTDPDLA QSQLDESLLA RDQSLEPNAD VEFGAEGAPR TAPETPVVGD
GNSSFDSFHL PTTRDPGERC GRVTAADEHA VGGASLGVES LQPPTTLAPD ERSRGRSGDG
RGGPSAADDR VVGVVNSSDN SFQTPTTPAP DESRRLSRLE GEGGDAGTAS EDVAVPGGDS
RRAGEKVTHP HTGPSARGSR SPEGVPGAED AGRGASPGHR VPVSARSSQA QQAVSGPNSQ
AEGDEGLPPR DTDGRGKAAR RSRPGGDGAP AFNLWHGDVN SHKESPPPRP SEKTGEDPSM
VKTAKGDMSP LYGDPSTGTL MHKCSDRPTP ESIHACTREL DENMVLDEDG GSGCGDGRGD
VRSGGESAPS DRNSLSESAS LGARPPPERR LPETREDWEG EGDAMMAIEA GPEGDSAKRP
VYGKVSADGG SSFPDAGASA RKTGPRAAKK KGGEKKRKGR GVEGGSIPAS SPGSEVGCEG
GARSPTAHPA QLAQREEGVS DGGDGYSSAD SLVTGYEGNY RERSHPVTSL PTEDEDMAFE
EEGEREGGAA AEETSDARGA QGTGDFNSLK QPKTPLSCLP LDQKPGSRVR GKKGRNRGGA
AGEERVVAGG KLDAGYTDPG DVTVFPASSF GPCETVSLGA SGSAHARQEG GGNEELPSDE
SIGSECLSRS ESLKHSGSYR PSERARGGRG SVEDGEGSYD GNFPGEGPRR PGTTDLSEGY
LVPRRQFLSR DRRRGGEEGG GEDDGMSAED GLPPDEKWLP MTAELSGDSA VRDNHFSDGD
ERRGARGNGG EGWGDDTLRT DSWRNLKTTD LGEDSVVSGS RYPSMEQQSV GEGGRDGLPA
DGKREPKAAD RGSGSTAPGS RVPSAGREPG GQCEGEDHVA MDEGAPGPGS PLVKKKQDND
TLFPHRGDHR APEPANPVSL LVLANPPSAP VSRAAEDMLT DMASLKRKRS RAGTASDSED
DAGPNDYHAH QSKSANWGDA LDDDIWIDDV PEPARSPESP DLGSERLFSS SSEESLHTAD
EGGDDGAGEG GAGDEEGSGL EEDDEFEGEG ARGATAQGQG VDFSEVDTFI GNMRQFSHRE
SLPLIVDASI SRGFREANAL HTIDKLITNI IIESGVVTGP AHPSKAKNLL RFIVLWGRKL
GIPTRELEIF METELEISRL CSAIDDGAFP EGLFLSHVLT KVNRCLPAIY TQTRGIVKKI
ASILTAETQK VEGRETVADP RGYAGILTEA FDKDAYIICT KGESVEIVKK IAALREAVAA
RNAEIARESN SFEALMGALR AYGPVPEGVG PMESQPGVKD RAFAEAVGEV MGDLTERVRN
VTSEFTDSLA AGHMDTTYLP DLETLIQNID STIRLLGFAA RELRMEKKPL MAAAQQLTYM
GGELAAIANA DWAHRPAEPV TQVKEINDLR SRLAQLQKED ENAQATERIL ADVEGMLDDI
TSQRGEGGAV SRTLTVPMLE NYLKNAGALI GESHNEKYLR LKERLRELAS SEDFLVNLIN
TTTLFSVTQT LAKIEQILGG SPHLATGEKV RQAFEGAGEQ IIADAMEAVA ARDPARLDVA
ATGSLPRFLR HSPAPGAEDT GAALFALSEA VKLEKGSKGR IRWRGVEGKL SDAHSLVARS
AAKGAQKRKL FALIQGLRKD YAAQEQREIM EDWKAFVTEA PINSMEDVND ILRAAPNEEA
REFAAKKLEE RVREMREAEA KLEKEAEEML TQAVKRRGLQ CWGRIQNAFD NMAFGGITGE
DWAAVAAEFQ REGSTLSSTL PGQLSKLTDK VEAEVEALLL NKVVSMLPNG PAFKPPAFDW
LTPYRAHMNF YLKSFPLPKL NRQAEAVEAK MSQIEQAIEG ADVYEAVAGT PLEAPVARAL
RLLRAARDEA AGLKGQIDEG ERAYVQGVER AGEGGEPPAK PKAEIPKKLL TYEQTLSLAN
LPEDFQKNVL QNETLMLNQL REYLGRVTEN INSLESRAKT SRGEANARLA AVIEENLPQA
NVSISSRRLD KSDPVGFLEG IVRDKQIVES DPYSATRESL VWLHRTFKAL LPLCPASLKR
RMELLGEEIL REKGRAVELH ELELRAHETD DVGVLTEAIE TLEARRVTGG KAAVEGWVKK
RDAYRKMVED LALRSEVEKR LGPLVEKSRE ALDAPDLAVL QEEAAALLLE AKTGGLDKSA
PETHERVLEL QMYLRFKLDF LKHYLDSQRP VFEAAPLSRA LYWSNSQGER ESRENSGEGE
GVEGGERRGE GGGEGSPSGA PLRLAPRLSI YRSLARQATK FPARWLETRP SVDPVPETLV
PNAQEPPIHL QPVFSNFLEL LLFLPETHPR VGPGRGPLYG TLAKRLGVEL RDMLDNQWGD
IAAHVQGVLD AYRASRIGSA RDNPFFAMTL FAHAVNVAAR GLDAGRRNPE AEVLPVTHRQ
WAQLLLATRP ELAAACLRAP SLRGAVEVLR TVAPSLRLLT PTLFLEDMYF PRSRPEVDHL
KALPPPRAFL FRPGRWPAAD VTQALWGSDG FAPLFPPKED GRARAGFLLW ALLTVDHVVL
GQLWSTLPPL DMGLKSPLHL LYALAAAEYP NTVPDAERES GGEPGTPYPY GPPTGSYYTL
GPTEAGGAEK VPVTGFEVAV GCLLRGVSAH IFIDSERPWA PKTNSGGEID LVAPVLDCTG
AVDPFKSLKA VPRKTLSPSA ELFDGLAGRE EVEVFGRQAA WLGERKRGGR KRDRFIVVLD
PNNYLKGSYL GNARPPGDAP PVELAIEENK NWPAEALAPN LQAASPIPKS RVAAEYKKLT
EKYMDLALKQ VFAEFPGSVH DPPDSREEEE GEGEAGQGAE EWQEEEWEER EEPRPPRRLG
ERGRREREVV EAVAPAPRDY SRPRVPPRRE PSGGPRSPAR DRDTLGGGAG SREKVSEGRG
RPRVQLSRSP KPRPAASQVQ GPREEVGFSP GRARRGGSTA HAPPETDTAD YIEPPKSGVG
AGSGPPEKKQ QGAAEAEAPA PREGEGAAQE APGEGTPEPA SIGKTSKGKK KPLFTKLPPS
SVDLKDLFKK PGLGIYGGLT SPRFSDESES EGEGKGESES EPESPNTTAL PASGESEPQP
LEEAGVAKQN TNTAPFLDGP VSQQSQAPPP PGRARPAPAA ASENWERGAP DTPNTTPSSK
GGRVKVKLPS KGETQPAELK PKPEPAAPDH RSPSAWQRSP LEAAPGTAAP RVQLGAPPRP
RQAAAVPAEH KSENKKPTLS FDAPPSAKPQ SQQISASTHT PQPQPSPPPP PLYAPKPPKI
NLNLRPDQTK GATAGGPPHA ITTPPPPHTP PPRAESPLEE TTYEFWDSEE DDSPPARPPR
ARLPVFPPGA PRGPSVSHTP IELEHILNGD YPQSPTTDVE EALDEEPVRE LYLHEEPVTE
GKHALLELIS NIRARVVQTT RLILDKINQI QFLYL
