LTP_HHV6Z
ID LTP_HHV6Z Reviewed; 2077 AA.
AC Q9QJ37;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=U31;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
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; AF157706; AAD49645.1; -; Genomic_DNA.
DR RefSeq; NP_050212.1; NC_000898.1.
DR SMR; Q9QJ37; -.
DR PRIDE; Q9QJ37; -.
DR GeneID; 1497033; -.
DR KEGG; vg:1497033; -.
DR Proteomes; UP000006930; 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..2077
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000408401"
FT DOMAIN 3..221
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..231
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 287
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 156
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 158
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 10
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 2077 AA; 240285 MW; 49D4C3F872A5BDF8 CRC64;
MKIITSSTNQ NDSKYGPRAG KQCMSNSFSF LHTVYLNGIN NSLNAGTIDA IMEEGYHLDT
ASTLALMLDN SDSQDYRLLT EIPRRIHSRY GVTQHELSRP FNGTLDTQKI DNEVYFGLID
FILYGKTKNC PAFAVITIGV LSRAIFFLNN TLYLFDSHPT EREATAAIYI CQDIEEAYEL
LTAHGTEGFY YDASFIFFIE TSNLSLSSHD AELLILKTYK DPDIAITLDK FSSTEIHDIK
KTDDIGSQQD LVAAKTTYLE RAPQKRKKNS HSLELELNDK KKKDTASLTY YATEVDLIPS
FYELRSQFQS LFHDLKSFPI MKSQFNWTIY LQDSPMNPNQ PFATPFLWNR VFHLLCQIVD
VFVGVGSTND DSSKQKQQTI FINYLLPFKD FSEVFNEALT ACQENNLDIL LIYNNYLCKT
TTFRTLERIL LSKFLAIADN EHEKHYEWVK SWTTQMLQEM PKKLDDIENY LKAYVSQNPV
KHFHEFVCLN KAEKHNIAVL LNEKRKEIQE DIERDKNIFA QLSNFIDKLG ETPALPIESE
NVHKVHTSDI TEAIVPRFMT ESIELPNIST LNNTQQLSLE KQISEKLTNT IHTLRNKFTK
IVQDNYNNLA AGFMPVTELN CLFAYLVNLY FNIEVLKHSG LNINTELLQE VEKLYDNTQF
LRFGTSHFNI NNLSNFTLSI RKMFVDFYNS QKPSDRASEI LAAIESILAD PSKNKTIVNI
EMIKSQLEEL GKMEISTTEN KQTAEITKQI LGDQELTPIY DFLHHLSAYN LPNTTTVKNL
HLHFILEKRP DIAAILHDKI QSILDICIDD MLNDITVPEQ TFSTVLFLVD LFPNSTEKTA
LFESVLTLRQ LAKKCANLKT LEEFDDLAQF ITTNSEQLQN MMKQHFGKKI PTLMDHIKFL
YSQKIITAEE KNWIQRAKTA VITSPEELTA FLATAPTKHA LQTCKPELDK ALQRHMEEQM
KQTAENDKKH ILTIRNTLEK RLNDILLILK DGQFSSLETV HLNLLETFLK QLQDNDLIIH
FTHALLPVLK DIETTISKTI SDILEKILIK TPLNPEQMSK EEQKYTPLLS FLSKFKKTTF
CTEDVKTEID QMQKSITFLT KIATSTNKYT RISHSVYGQE LNLYEERITE LKKETNKIKE
QLSKEYAVAE KKILLSSQDA KTNKIYLVLN THTLKEIKNT QFRETAFAKA LTVEVNNKEN
QLQELLNHFN AHLKAKMDQN HITKLSFDTK WTAFVSDSRL YFPDFVDIKL QDFISDPFKV
ISQLMNKAAN EMPYIQAEIT LKWLTQLVHD INKFCLSAIS EFGKEAIPFN YAALRDLEYQ
INTKYVEIEN KVICNETVEN TKNIPKLTKL LKELDPKRVA GGQKQYQTLM NKILTSETSM
QQTYEKEQLK KEYFETVNNV ASFKLAFNFP KQRQNVERLM EKFKSLPKGQ PFEKFPEEND
LFSDSLITEN YINGLRALLN FITAAQNYIQ NTLLKQWAVF QQQNFIPIDY SVANVKPISD
LYARLRIERD RQVFYQVNSV FGTQLIVDET GVPLQFHNIF YNAVVKFFSL NYKQIHVPED
TPRLVSSQYK LLSVCKSFII ILQQFWENII TLDLGPYLRD GTQNFKRELI PIVNLKLFIY
IITQAWTASE DSTVSTAFEL PIKQFTLLIL CSHPEYLYGC LSHPTDLVIN SLAKSIDKDS
LYDTFVVSHN PPEKPMHLMR SICIDTQLWQ SAKLMKDTFQ QTFFTQLCPQ NEKFFIYLTA
FLILPYKFLN YIWIQYKPIT FTQRSYQNLI KDLCSEYVHQ NKITMSSVTP HEPDTIKSGE
KITSKITVHK AQNTPTLTRL QAQEYVFDYI LYSFLTGYEM TFAMYIDTIE KTYLLCMRHL
ENVLHDKDFQ SVLRARTFDI NYILKQSWTK NIVEHSIFSV QLNKIVSYLN HTNRATPNIP
LILFNYDNEV VNVYLPPMST DPKKVAFYIK NPFHFPVQEY EATDLISFHL YPKTTDILNQ
LPPNKTVSTR PYNLSSETLT TKNLSEPKFK QPTVTGLMPK SQSIILSTDT NVLETSPDIK
ANTASAAIKD VTLAREQISE FSESINTTLS KLKSLYL
