LTP_EBVG
ID LTP_EBVG Reviewed; 3176 AA.
AC Q3KSU8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 ORFNames=BPLF1;
OS Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
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; AY961628; AAY41102.1; -; Genomic_DNA.
DR SMR; Q3KSU8; -.
DR IntAct; Q3KSU8; 14.
DR PRIDE; Q3KSU8; -.
DR Proteomes; UP000007641; 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; Repeat;
KW Thiol protease; Ubl conjugation pathway; Virion; Virion tegument.
FT CHAIN 1..3176
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000375970"
FT DOMAIN 41..258
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REPEAT 335..339
FT /note="1"
FT REPEAT 340..344
FT /note="2"
FT REPEAT 345..349
FT /note="3"
FT REPEAT 350..354
FT /note="4"
FT REPEAT 355..359
FT /note="5"
FT REPEAT 360..364
FT /note="6; approximate"
FT REPEAT 365..369
FT /note="7; approximate"
FT REPEAT 370..374
FT /note="8"
FT REPEAT 375..379
FT /note="9"
FT REPEAT 380..384
FT /note="10; approximate"
FT REGION 1..268
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..384
FT /note="10 X 5 AA approximate repeats of P-A-S-A-A"
FT REGION 375..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..611
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 928..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2610..3008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3023..3043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2616..2657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2732..2748
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2749..2784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2804..2835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2842..2856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2920..2934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2982..2996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 193
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 48
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 3176 AA; 340605 MW; 1D4CDE9D746627D6 CRC64;
MSNGDWGQSQ RPRGTGPMRG IRTMDVNAPG GGSGGSALRI LGTASCNQAH CKFGRFAGIQ
CVSNCVLYLV KSFLAGRPLT SRPELDEVLD EGARLDALMR QSGILKGHEM AQLTDVPSSV
VLRGGGRVHI YRSAEIFGLV LFPAQIANSA VVQSLAEVLH GSYNGVAQFI LYICDIYAGG
IIIETDGSFY LFDPHCQKDA APGTPAHVRV STYAHDILQY VGAPGAQYTC VHLYFLPEAF
ETEDPRIFML EHYGVYDFYE ANGSGFDLVG PELVSSDGEA AGTPDADSSP PVMLPFERRI
IPYNLRPLPS RSFTSDSFPA ARYSPAKTNS PPPSPASAAP ASAAPASAAP ASAAPASAAQ
ASVAPASVAP ASAAPASAAP DSAAPASSPP LFIPIPGLGH TPGVPAPSTP PRASGSAAPQ
TPKRKKGLGK DSPHKKPTSG RRLPLSSTTD TEDDQLPRPP VPPHRPPSAA RLPPPVIPIP
HQSPPASPTP RRAPVSTIAP SVTPSPRLPL QIPIPLPQAA PSNPEIPLTT PSPSPTAAAA
PTATTLSPPP TQQQPLQSAA PAPSPPPTQQ QPPQSAAPAP SPLLPQQQPP PSAAPAPSPL
LPQQQPPPSA ARAPSPLPPQ QQPLPSATPA PPPAQQLPPS ATTLEPEKNN PSAADRAGTE
ISPSPPFGQQ PSFGDDASGG SGLVRYLSDL EEPFLSMSDS EEAESDLASD IPTTEDEDMF
EDEVFSNSLE SGSSAPTSPI TLDTARSQYY QTTFDIETPE MDFVPLESNI ARIAGHTYQE
QAIVYDPASN REVPEADALS MIDYLLVTVV LEQGLIRSRD RSAVLNLLEF LKDWSGHLQV
PTLDLEQLLT SELNIQNLAN MLSENKGRAG EFHEHLAAKL EACLPSLATK DAVRVDAGAK
MLAEIPQLAE SDDGKFDLEA ARRRLTDLLS GGDQEGEEGG GEPEDHSIYR GPHVDVPLVL
DDESWKRLLS LAEAARTAVA RQQAGVDEED VRFLALLTAI EYGAPPAASV PPFVHNVAVR
SKNAALHVRR CTADIRDKVA SAASDYLSYL EDPSLPTVMD FDDLLTHLRH TCQIIASLPL
LNIRYTSIEW DYRELLYLGT ALSDMSGIPW PLERVEEDDP SIAPLPEFET VAKKQKELET
TRENEKRLRT ILDDIEAMLG LAGVASAPGA PISPASPSAT PANHDNPEAT PPLADTAALT
IPVIEKYIAN AGSIVGAAKN PTYIRLRDTI QQIVRSKKYL MNILKSITFY TIDNYIASFE
ESIDHLYRDL PVLDPEVQDG IDRILDPMVS EALHTFEMGN RLTLEPARLV ALQNFATHST
LKETAAAVNL LPGLLAVYDA TVTGQAPEDA LRLLSGLQNQ LSQTLIPGKL KKRFLSYLQK
LKNNNNDQLR QKEVQAWRLE AEGFKPATEE QLEAFLDTAP NKELKRQYEK KLRQLMETGR
KEKEKLREQE DKERRERRAR EANEAWARIR KALGARPEPA PTSPDDWNTL LASLLPDNTD
SAAAAAAAVA RNTDILDSLT QILAAMLLGI TRVRRERLRS LLVDDGGAAE RMEAAEPGWF
TDIETGPLAR LDAWPATPAA TAKEGGGGRG AEEAAGALFR ARTAADAIRS ALAQTRQALQ
SPDMKSAVVN TDLEAPYAEY ERGLAGLLEK RRAAEAALTA IVSEYVDRTL PEATNDPGQA
NLPPPPTIPQ ATAPPRLASD LALWPKKPQL LTRRERDDLL QATGDFFSEL LTEAEAAEVR
ALEEQVRESQ TLMAKAHEMA ASTRRGFHTA LEAVLSRSRD EAPDDELRSL LPSPPKAPVQ
APLEAALARA AAGNGSWPYR KSLAAAKWIR GICEAVRGLS EGALALAGGA GAWLNLAAAA
DGEIHELTRL LEVEGMAQNS MDGMEELRLA LATLDPKRVA GGKETVADWK RRLSRLEAII
QEAQEESQLQ GTLQDLVTQA RGHTDPRQLK IVVEAARGLA LGASAGSQYA LLKDKLLRYA
SAKQSFLAFY ETAQPTVFVK HPLTNNLPLL ITISAPPTGW GNGAPTRRAQ FLAAAGPAKY
AGTLWLETES PCDPLNPAYV SADTQEPLNY IPVYHNFLEY VMPTVLENPE AFSLTPAGRP
QAIGPPQDDQ ERRRRTLASV ASARLSAAAA DSYWDTWPDV ESNAGELLRE YVSAPKALME
DLADNPIVAM TLLAHASLIA SRNHPPYPAP ATDREVILLE QREIMALLVG THPAYAAAFL
GAPSFYAGLG LVSALARDGG LGDLLSDSVL TYRLVRSPAS GRGGMPSTTR GSDDGEDARR
LTRHRIAGPP TGFIFFQDAW EEMDTRAALW PHPEFLGLVH NQSTARARAC MLLLARRCFA
PEALQQLWHS LRPLEGPVAF QDYLRDFVKQ AYTRGEELPR AEGLEVPRET PSSYGTVTGR
ALRNLMPYGT PITGPKRGSG DTIPVSVFEA AVAAAFLGRP LTLFVSSQYL FNLKTLGQVR
VVAPLLYCDG HSEPFRSLVE TISLNFLQDL DGYSESFEPE MSIFARQAVW LRELLTEARA
AKPKEARPPT VAILANRKNI IWKCFTYRHN LPDVQFYFNA AGASRWPTDV LNPSFYEHED
PPLPVGYQLP PNPRNVQELF SGFPPRVGHG LVSGDGFQSA DNTPASSDRL QQLGGGETDQ
GEEGSTTAES EASGPPSPQS PLLEKVAPGR PRDWLSPTSS PRDVTVTPGL AAPITLPGPR
LMARPYFGAE TRASESPDRS PGTSPRPWPK DSLELLPQPA PQQPPSSPWA SEQGPIVYTL
SPHSTPSTAS GSQKKHTIQI PGLVPSQKPS YPPSAPYKPG QSTGGIAPTP SAASLTTFGL
QPQDTQASSQ DPPYGHSIMQ REKKQQGGRE EAAEIRPSAT RLPTAVGLRP RAPVVAAGAA
ASATPAFDPG EAPSGLPIPQ APALGSGLAA PAHTPVGALA PSPQKTQAQR PQDAAALPTP
TIKAVGARPV PKATGALAAG ARPRGQPTAA PPSAASPPRV SLPVRSRQQQ SPAIPLPPMH
SGSEPGARPE VRLSQYRHAG PQTYTVQKEA PPSAASQLPK MPKCKDSMYY PPSGSARYPA
PFQALSFSQS VASPAPSSDQ TTLLWNTPSV VTQFLSIEDI IREVVTGGST SGDLVVPSGS
PSSLSTAAPE QDLRYSLTLS QASRVLSRFV SQLRRKLERS THRLIADLER LKFLYL
