LTP_EHV1B
ID LTP_EHV1B Reviewed; 3421 AA.
AC P28955; Q6DLI7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 OrderedLocusNames=24;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(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; AY665713; AAT67281.1; -; Genomic_DNA.
DR PIR; G36797; WZBEB6.
DR RefSeq; YP_053069.1; NC_001491.2.
DR PRIDE; P28955; -.
DR GeneID; 1487490; -.
DR KEGG; vg:1487490; -.
DR Proteomes; UP000001189; 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:0019784; F:deNEDDylase activity; IEA:InterPro.
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 GO; GO:0039693; P:viral DNA genome replication; IEA:InterPro.
DR HAMAP; MF_04044; HSV_LTP; 1.
DR InterPro; IPR005210; Herpes_LT_deneddylase.
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 Pfam; PF03586; Herpes_UL36; 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..3421
FT /note="Large tegument protein deneddylase"
FT /id="PRO_0000116036"
FT DOMAIN 19..238
FT /note="Peptidase C76"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 1..248
FT /note="Deubiquitination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 311..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..508
FT /note="Interaction with inner tegument protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT REGION 2407..2442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2479..3195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2412..2434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2621..2644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2661..2699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2776..2790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2865..2892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2951..2968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3024..3049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3101..3146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3168..3188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
FT SITE 26
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04044"
SQ SEQUENCE 3421 AA; 367083 MW; 5075EFE4739BB7AC CRC64;
MAQTLVPANK AGGAQADVVV IGYRNQYDSQ LGEGSHVSCL RSSLSFLRLI FTHGIDFALT
ADSIDGVLVE GRAWTVAGSK SGEAPCMVSI VELPNKITYA NSANALCCVF SRLYGDSGFY
MHPGDGFQST QIPARQFFDG VWKSRSESFA LITIGAIGLA VYRHGDVAYV FDPHGHGSVT
EAFVVRVLAR DVYAYLTGYA ATDPESDWAG ALVFFVTCGP TESEPGFLIS ATSLLYGISE
TYLSDEQYVE RSVATSHPGI STPPPLTDVA VGAVSEAWQY QELENGAATL DADMEGVAPA
AAQVRASVIR QPTEKRVSLP KRRRPPWTPP TSSENLTTSG NTHTVAGRPS QKVRNATANV
QNPTTGNGSA WAEALNDGGV DNASRPGQAV GAAGTLQNPA PGDALAMETT QASEEALRTR
RVFRLSGEDE APYDLGDAVG VLSAEINELA TRAEELDVLS STCVDSTVWV TRPHNSPDMD
ILEQFITMIF NRLLSFLVEN GARTRTDSPS VIAGLFPGVL AAIPTQSAVV NLLQATGMAL
SDVASYKSIL NMVSNEDSPV GELAVIKLEL VASEVIKSTQ KLVARVEELE RDVTSGSVNP
LGLYTYLTER LVAEMTKHGG DLFAREPKPG AVSLTERIGS LFRKARTREA RATRTNASLA
RDLNAIEAAV HAAHDKFDAI EIKPADPSDT TNMDELAKSL DLSAVPTRVA KVIKKVESMV
SDSIREYFLR GVQYSARAIA MDKTSGARFQ VASAAVSNLE RMLDSLPNFE KSLNSVVASA
GIQGPPPAQI SGSRKATLLG NLLRAGQNLT TDNALGAWAA LLSEAHTEGH IERRELEAVI
KEITSINDHA AKKASVEADM ERFRVLSAAV DQATSDMYNS NPHALDTIIR GAEEMIRQAK
VVEAHFDSGR ISREAASRVG VRKREVETLA NSARQRAAEI SAARDEIYSR LQSLLLPLAG
FVGLRAAPGV LEQLAKDAQR STSEELRNLM HEAPKQVVST VHSHLWSLFG QFREALEHPN
STTSSALAGV GPAFAIVVRS LLDPNKQRES VEFFITHADA LADTVGAVEA NPNSELAVAH
AVNSIAAAIQ TVSVGGRTIT EFAFLVPMLE RYQSRLTIVR ETQRLATAQR AVAASVSAAA
EVTTKLRAVA VPGVQEDVLK AAIAAAKHVS SEVTAAATAA ERELARLDSK ALSVAQVARA
HQDLQKQTAV AKQRVGEIEE VLANLNKQQR ELQDRAVHDR WKSDLLAALD KIETKSSFDV
SELSRLRDLG AARGYDSREF AKRAEQALAA NARAVIAVLD NVFKFNPYAP VNSKKETNPT
ISMLYNISWW DDFTLAAPIL NTLFAGVDVE ELMSLMRIST GMITFASTNG GRPKYNEAVN
SLSSDMLKVP QLAKYVDFYG KWYTEFNAEM DVLSKLRADV LQAVGVRSGE ISRALEEVTY
VRNAEVAEKV LADGVKLYIP SDALIAKAVK YLEEFNQKRF AGSAFEEAIA TTIRQDLSTA
REAATQAEAA RSEAMHRATH ILREVVEAAK AADRDASANL ANLKNLLRLT PPPQSVAAAL
DKATSSDDIV TQAALLLGTV ESTPELDIKA VEWLQQARSI IDSHPLTTKI DGKGPMDPYA
ERIEKLHTLR GELDELRRQL TATEVSWDEA WGNFSRAVPR ADVSMDGFVD AHQRARTLQA
SMGVISEMRA DNKYGRLPPK VIGAIESKFA ERHKNLETFN DTSTVLQTAI TQFDSLVQQI
PPEMEYDVLR SLLASFDQLA AVLPKWVGAE YAAYRSLLLM RIGLYDEYQK IAGIAAAGSR
PHLEAVEYRS AVEDANLRRA SRVSSLMGDK DVILSLREAK SSIDTAFPQV LLDAKGVPVE
YRVCYRAVGD KLAAMLCGKL GVSMRPAMPS DPIVESSSVS GINVTHDILQ LRFGLEKAYH
SGFSTFARFV RHKRADWSPT EPAQAAAEIY AAVLATTLTR EYGATWHRIR FMASSGLFVA
SPDSVCDTQG GRGKKSNNIV HLTLSDVVLS AMLRNSMHLV NFMRLDLTRQ HEYMARTITP
VLTKSLLSDI LINTLVPTDT STQWRSLPLA GDLEDLAQGM LFSIRMSDWK QNSFSTTSLL
DVWMRSPGES GRAAAAKIAS AIPGNPLATF TVLARMCIPP NALASLWEAL QPEAFSQQNL
SYDDVVTSRL DIASTVQTSV AVDPEMKSVD TKSRKQLYTT TGTSTTFTLA GSAPSAVKEV
SALDVATCAL MFGAPVVIAM ETPEMFSEAS GMSFCLKIFD SRPGATDHEI IQAVSSDLSS
WGTSLLALDP NAIENACLTT QLEILSGLVA SKLLAPAPPC LIVLDPSMRV IKVLWESESP
PNDLVITLAE DEIIAELPYL NADDDLLPPM NPDDPIYTRV ISGTNIPTAT TEGSLFADQQ
LEFLRPESNP FPFASHDSSQ SLDVPSSPSS GSDKYEEDPT GIVYDAPVDD MSDMAMNKAK
AWQEWLEDGF AEDDYRELSN AMPAPPKTTP VVESKQKSDS VDRAPTLPPK AAPLPPSDAS
AIMSGKPVFK YTPGNKSAVP PSVPAPPTLP PAPPLPQSTS KAASGPPPTL PPAPPLPQST
SKAASGPPPT LPPAPPLPQS TSKAASGPPP TLPPAPPLPQ STSKAASGAT QSDSGKTLTL
DVPKTQSKDK VVPVPPTDKP STTTPAALKQ SDASKPPTAA IQHQQKLGTP VTPKDSGDKP
TDNASAPVGV SPVTPDGTPG AKPPPKDAPP VDDTKQPVRK SLPSQVRGGR PYIRPSLGPF
KFTGPPGYTI PVHGLPPSDS NVTQSTKEPP KPAVETPAAA PAKSAAAPAA APAKSAAAPA
AAPAKSAAAP AAAPAKSAAA PAAAPAKSAA APAAAPAKDQ TKSAAEVPKP AKDQAKDQAK
DQAKDQAKDQ AKDQAKSTTG QKLAKDPKSD GLTDDVALEI VPEKTPLPDD SPIGAVPENT
PLPDDSPIGS PDLSASKNSH TTDAVSSDRF SVACKVPLPD SPEDDFYSYA VDVPLPDSPT
DDPSSGRSDA RAPTVGGVAS IHRKSDSRNN RQSDAWRRAF ADTLHGRPRN RSATKPCKSA
PYKVPHAISY TKIPSVPNDQ SGLAGKPCSE EPKRPTGRDT PVGSWNVSPS QAPADIPTAI
PQNQNTSESP RTTSLKSPTR TVQSSMPADD IDELAEYDLQ IARAVPVTKH PQPPPANQTP
PPQEPPAPID DRKNIRPPLS EEEIIAFLIN MDDDDAGNAS GPVDLHSVQA PKLPKQSKPT
TNQFVPLDWW TETEPVVDAD SLDLSPKQQR LFSWESTRDL LNINVRDRVY EEESDDEYTV
SWDQHLVPAV SPTSVSSYSS DTVTDSYTDI NDPRSVVCPL DGNAQNNVRE FLDTHSSRVR
VVPADELLSR RYFRSTSLSA MALLIAACRT IVRRLRATRR VLTDINRSLL LDLKQIRVLL
G
