LTP_SHV21
ID LTP_SHV21 Reviewed; 2469 AA.
AC Q01056;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 85.
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; Synonyms=EERF2;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT saimiri (HVS) L-DNA: general conservation of genetic organization between
RT HVS and Epstein-Barr virus.";
RL Virology 188:296-310(1992).
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; X64346; CAA45687.1; -; Genomic_DNA.
DR EMBL; M86409; AAA46140.1; -; Genomic_DNA.
DR RefSeq; NP_040266.1; NC_001350.1.
DR SMR; Q01056; -.
DR PRIDE; Q01056; -.
DR GeneID; 1682468; -.
DR KEGG; vg:1682468; -.
DR Proteomes; UP000000587; 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..2469
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000116039"
FT DOMAIN 13..225
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..237
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 244..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 346..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 20
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 2469 AA; 280168 MW; D2B4B8DC08644CDB CRC64;
MDIHPLFKKL NLEGIASTHQ ADEKYGQYAG SQCLSNCVMF LVSSYYNDET PVTSLHGLNE
ILKYGAKIDF ILRRSGQLGH NQYAQLHHIP GYIAGPKWAC FIYQSIEMFG MLGHESPINE
PFVASLKSLL SKNYNTTVQY FLAICNSKSM GILIKDKKIF IFDPHSCPLV PNSPAHVFST
SNVNDAIEYL SPPNVQYTGS FLYFVPKEYI GHSHYIMNHY RVINYEKLHG PNIDLTSQEG
LIIEISPPNT PKPTSTQKPP KTPRTPKPAT PKAPKTPRKP KTPKESTIPY DKSKKPPKIP
KTSKKSKKVL TKDTALTPQH KTIEEHLREL LPPITETVED NTLFNHPVER TTPGTDSLLS
GINSTTKRED DLEDDDNVTS KLKEDEDDWI DDIPIPEVLD TETTHSDQET IYMIGDENIH
DWSYSDDDID DTLDISFIQL DNLITSLDNI PKNNTFPRII DKTSNQPIKE GKALHSIDRI
LKNIVLEHGL ITSSSISISK CKSLLQFVIL WGEKLSIPTR DLKTILKTEL IITEIAEIAL
TKLTNDTFRN NVITKLNKCM LKLKSESVDS YKHLSALLNN IILKIQTIDT EIELKTLSTV
FTSELGKDFS VVCTKKESET IMAAIKNLKE KISTRKQELH TEENYFQSVL IAMETFQPIP
LPTRVIEIQP SKKAQQLHEK SKLVEQKLTI DANNVLTDLL HTMKQDKTDI SPAPDFTTVL
KNIQSTLQLL QTCVTDLNID KKFISNTVQQ LSYIGWEVAE LSHSQWNFPK ADPVIPLKIL
DDIKKEIQQV TTKQKNEETL SKILADVQTL LENAKQSDTL SIPILQHYIT KAGTLVGERE
NQKFESLKNT VQKLSTSEEF LKTLIDSTTL ENVQLQIQEI SDILQSNQYI HQSETIKQAF
FDKSNTIINN ILQLINQQKY TTVTQPMLIA VKRFLSEAKF RESNTICEII STLVSLGSLL
SKSTTVEALK DALKSIDTLK EKLTAVDRPL KRELYNVIRK LQKQLKTLLE QQEFDNWKME
VDSFVPTPSR DVKTFIQNAP SMKAKQYAKK ALKDQIQAME IDVDPESVIE DNIKANGQKA
WQKIQSAFQD LNFSILIPDD WLSLAKEYTR PKSTLFTVIG PILLKFVEEV LESVKNLKEA
KLKSLLPNGP VFTPPKFDWI HYYESNVNFH LKTINLPKVS TVAHNIGHEL SLLSQALNSK
TLPEAVVGTS LEQHAAKFSC MFKTLEATWH DHQVDTRTKI DEYIEDLRND TKKHIVAPQI
QSPNRFLSPE DIQEINSLPK LFRDSLLENE SRLLASQKNE FQMLENTVKA AELQYKATQE
DIISNMSEAI NSLLPLAPAY ILAIPTIPTD PLKYVENIIQ DKRLLNTEPY QITIECLNWL
NTACKTLLSI CPKSQKQRLV VLDQSINTHL NITQQFYNLE KTANTTDDLS VLQNAISTLD
LKRVQGGKAT VDSWQSKLQQ MKAMLDNISK SAQTLASLDI LWGTALTSVS TAHLGELLQK
ADPLQKDIES LSSTNTDLLS RVTELIHFIK FKRGFLSYYE EGQKEVFQRY PLTQNIRPSQ
PTEINNLLRL ALFVLLKNKD ASAWIWTETL PLVDSNKLAY VPPNKGPLYT CSQYLKLLEA
QLLDPSLSKV ILSDNRPLAG IAQARLGIDS TVLLARAFPD IQKHAEEVLT AYKNSIVSHT
QNEFMAMTIV CHMIKIIMND FYPQNFNINT VPIYVNHTKL LQIILTMWPR LIKASLCQQS
FQEATSLLQT TLKPLFLKIT DLTLENNIYN PASHCSDALL FFPQKWKSIN IQSIMWEHPS
FLAICKNKSR ARITFLALAF KIIDPTILNQ LWTSLNPANT SDSTSYSLLL NHLVATEFDK
NVPSTFLEPG NPSLAYAYGT QTGNIIGTKS YVPQKSPPIS VTAFEIALGA LIFQVPVKLF
VTDKTPVLSS PELGDMLIVS ELLDCTGTTE PFKTMIEAPK SSLSTNLNKQ YVSPPHELEV
FSRQASWLQH ILSSSNFKNN IVATIDYSTT FLNAYVVPEK LPFKQESFCF IPKIDSLQWP
NNTFTTFLPL VEMPSNIELH YAKVTEPFNK TVLSTMFNVF PTHILPTQEE HDQSISSKSP
TFKIEHDYNT NSVYNNHINN INLTNNSTYH QYKDVLPQPL ADKLSYEPKD LQNLASTTEP
QIEDIFSELS IKETDNTAKA PLLYPQKQPK TKKFLSPVHT KHKTSNSIIF EENTTVKVQP
NTCIQHSDLH KDTNTPRQQI SNAPCFIPNH KVPVIIKPSQ EKLKANTVHT NTDDLSPKKP
QILIANNNNI FKQSDKQHKH QYTQISKPKI FINQDSNNPI KQPHHNPPQP LIKPTDPQQL
TLSNDIISSD QTTKNLNVQR KPIIVIPNNN YALNQVQKLS NLPSIKTKPY ITLKDIQSNS
KTLYDESPIT IPILEHLDIE PIVSISYLEK RVDETKFIIL EFIKHTKQNI IKTTNLLIHQ
IMKIKTLYL