LTP_HHV7J
ID LTP_HHV7J Reviewed; 2059 AA.
AC P52362;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Large tegument protein deneddylase;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P10220};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P10220};
GN Name=U31;
OS Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
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:0000250|UniProtKB:P10220}.
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:0000250|UniProtKB:P10220};
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.
CC {ECO:0000250|UniProtKB:P10220}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P10220}.
CC Host cytoplasm {ECO:0000250|UniProtKB:P10220}. Host nucleus
CC {ECO:0000250|UniProtKB:P10220}. Note=Tightly associated with the
CC capsid. {ECO:0000250|UniProtKB:P10220}.
CC -!- SIMILARITY: Belongs to the herpesviridae large tegument protein family.
CC {ECO:0000250|UniProtKB:P10220}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43400; AAC54693.1; -; Genomic_DNA.
DR PIR; T41933; T41933.
DR SMR; P52362; -.
DR PRIDE; P52362; -.
DR Proteomes; UP000009246; 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-EC.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006928; Herpes_teg_USP.
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..2059
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000116042"
FT DOMAIN 3..220
FT /note="Peptidase C76"
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT REGION 1..230
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT REGION 245..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT COMPBIAS 254..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 23
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT ACT_SITE 155
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT ACT_SITE 157
FT /evidence="ECO:0000250|UniProtKB:P10220"
FT SITE 10
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P10220"
SQ SEQUENCE 2059 AA; 239477 MW; AAE6CA6DEDC5D316 CRC64;
MRIIAGSTNQ NDPKYGPRAG KQCMSNCFSF LHTVYLNGIN NVLNKESIDI IMENGALLDN
ISTTTLKLET GNIPEYRFFT EIPKKISSNF GETIHELSRP FNGTLESQHI DNEVYLGLLD
FLLYGKNKKP AFIVITIGVM ARAIFIVDEL FYLFDSHASD TENSAAIYIC EDIDELYALL
AIENVAEFYY DAVFSYFIET TDLSLEDGDA TILILKTYKD PDIALSLNDF LTMYSSTSST
KTAETNTLIS KQSPSKRKQE KTSLNSNSLE KKRKQGSSLK YYNNEVDLVP SFYELRPQFN
NILFELSNFP IVKENVNWTL YIQKFATKST QPFTKPFIWN RVFHLFSQVV DALIMIKNDH
WDETQQQKQF FTHFLPFKEF SEEFENAIEA CRENNLDLIL LYKNYLSKTT AFKNLERILL
TKFSAIVSPV HEKHYTLVNT WLTNLIQKLV KHPEDTNAFI NDYVLKNPLN HFICLNKKEK
QSIALLLNKK RMSMLKDVEI EKNGFVQLQA FIENIGEAPA NYLDPENARK VNVEEVSEKD
IPTLSTDKVS IPNESMFTSN KKHSIEKLIH AKLKAILSTM GQRLTRIIQE NYNNIAAGFL
PVNDLNNLFA YLVKLYFDVY SITINGFVVE NELIKNIEQI YDNTQYLRFG LTRFNMQNLT
PFTISVRKMF LDFFLSQKTL IDRAEEIIEN LEFKSVTPEG KQKLATKNML REQLEQLNAM
DVDDTINLKT DTLTHQVLFS DQELRMIQDF ILQLSIHNIP SINFVKSLKL HIILEKRPDI
LLALQEKVQN ILYFYFQDLV NEIPAQENVL STMLFIIELF PADSRIHLLE TGYISRHIVK
KWLNMKSLQD AEDLIRFINI NKEQLGKFEH QPFGKEIQKL IEKIHLFYKQ KVIEYQEDVW
SEMAKNIILT SPSELSQFLA SAPTQRIIQK HKNNLDQKLL IHMENQAKQA MEDDKKRVAC
SKINLERHLN DLLLLLKDRQ FASIQASVLI VCENIFKTIP DDNLIIQFSH ALLSVLLDIE
KDLKSYSSEI LEKILINRPL ETSRLLVFKD AYGNLKEFLN ALKQSLFATA DVQNKADFLI
QILDFTYKFR HKTNKGKLLH SIYNEDFKLY EETLTELRKK ATDAKESLTK LFKASEQKIE
LSRTIPLKEI YLNIETVNFQ GYGNVVFRES AFKRAIEVEI KNYEMKLNDL IKHFNSHLKT
KIDHIQILNL SFDNKWKDFV SKSKISFPPE LTISSQELIK DPIKVITETL NKASNDLAYV
ISEKILKWLI VFVKELNTFF VATMSEFGEV IPFDYKHFRA LEYEINSKYI EIENKIICNE
IIENTDNIEK LSTLIKQIDP NRIAGGKQKF QDYLSKILTA ETNQQQTRYK EQLKKQYFDL
LDNIAHFRFA FDFNHQQNLI LKLKDKFKTL RTDTVFERFP NLDDTFVSSM NVENFLQALE
ALSHFVQAAQ NFLQNVLTEQ ADLFPQTNFI PVELSTVKTI PKSDINLRMK IHTPQTFFQV
DSVFNTQLIV DEKGIPVQFY NVFHNIVFKF FALNYKKIIV PDKVLNLVST KYKILTTLKS
ILSVVKSFWK EIINFDLTSY FQGKAEFTFQ NVFPIINLKI FIYIITQAWS VTSDETQHSF
ELPLEKFSLL IIANNPEFLF GSLQCPVDLA INSLIPLLEK KKYFTAFTIS DNPPKLSMDE
LKIVCLDLNT WSEITLEKYT FKKNSLMQLC MGKEKFFIYL LSALVLPQNF LNYIWIQYKP
SCCAQDSFQQ LIQDLCFEYT HQNHIKPISL NLQEPNALKH GERILSKFVL EKNANTSLFS
IFLGKQFLLD YLLFSYLTAT EMTFSYYVDS IKNFLLTIRH LENVQQNVDF RTILQSRNFD
LKYLLTQSWT QNVLEQSIFH VQLDKIIADI KQPQLSLKKI PLVLFNGDNE VVSTYVPPEQ
ASQTEQSFRI KNIFPNPVQE YSSKNVILFT NYPKNTKFLF NSPPPKTAAK SYKLPDTTDD
INTETLSSPT IQRIPIKGLV PKENEIVFLP EKNTAHTDSK ETKTHLIDTF NILSQTKGEI
KTFSTDFDQT ISKLKHLYF
