ID Q8UZI9_9GAMA Unreviewed; 3105 AA. AC Q8UZI9; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=Large tegument protein deneddylase {ECO:0000256|HAMAP-Rule:MF_04044}; DE EC=3.4.19.12 {ECO:0000256|HAMAP-Rule:MF_04044}; DE EC=3.4.22.- {ECO:0000256|HAMAP-Rule:MF_04044}; OS Macacine gammaherpesvirus 4 (Rhesus lymphocryptovirus). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Gammaherpesvirinae; Lymphocryptovirus. OX NCBI_TaxID=45455 {ECO:0000313|EMBL:AAK95420.1}; RN [1] {ECO:0000313|EMBL:AAK95420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1}; RX PubMed=8892903; RA Franken M., Devergne O., Rosenzweig M., Annis B., Kieff E., Wang F.; RT "Comparative analysis identifies conserved tumor necrosis factor RT receptor-associated factor 3 binding sites in the human and simian RT Epstein-Barr virus oncogene LMP1."; RL J. Virol. 70:7819-7826(1996). RN [2] {ECO:0000313|EMBL:AAK95420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1}; RX PubMed=10482645; RA Rivailler P., Quink C., Wang F.; RT "Strong selective pressure for evolution of an Epstein-Barr virus RT LMP2B homologue in the rhesus lymphocryptovirus."; RL J. Virol. 73:8867-8872(1999). RN [3] {ECO:0000313|EMBL:AAK95420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1}; RX PubMed=10970361; RA Rao P., Jiang H., Wang F.; RT "Cloning of the rhesus lymphocryptovirus viral capsid antigen and RT Epstein-Barr virus-encoded small RNA homologues and use in diagnosis RT of acute and persistent infections."; RL J. Clin. Microbiol. 38:3219-3225(2000). RN [4] {ECO:0000313|EMBL:AAK95420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1}; RX PubMed=10846073; DOI=10.1128/JVI.74.13.5921-5932.2000; RA Jiang H., Cho Y.G., Wang F.; RT "Structural, functional, and genetic comparisons of Epstein-Barr virus RT nuclear antigen 3A, 3B, and 3C homologues encoded by the rhesus RT lymphocryptovirus."; RL J. Virol. 74:5921-5932(2000). RN [5] {ECO:0000313|EMBL:AAK95420.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1}; RX PubMed=11739708; DOI=10.1128/JVI.76.1.421-426.2002; RA Rivailler P., Jiang H., Cho Y.G., Quink C., Wang F.; RT "Complete nucleotide sequence of the rhesus lymphocryptovirus: genetic RT validation for an Epstein-Barr virus animal model."; RL J. Virol. 76:421-426(2002). CC -!- FUNCTION: Large tegument protein that plays multiple roles in the CC viral cycle. During viral entry, remains associated with the CC capsid while most of the tegument is detached and participates in CC the capsid transport toward the host nucleus. Plays a role in the CC routing of the capsid at the nuclear pore complex and subsequent CC uncoating. Within the host nucleus, acts as a deneddylase and CC promotes the degradation of nuclear CRLs (cullin-RING ubiquitin CC ligases) and thereby stabilizes nuclear CRL substrates, while CC cytoplasmic CRLs remain unaffected. These modifications prevent CC host cell cycle S-phase progression and create a favorable CC environment allowing efficient viral genome replication. CC Participates later in the secondary envelopment of capsids. CC Indeed, plays a linker role for the association of the outer viral CC tegument to the capsids together with the inner tegument protein. CC {ECO:0000256|HAMAP-Rule:MF_04044}. CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester, CC thioester, amide, peptide and isopeptide bonds formed by the C- CC terminal Gly of ubiquitin (a 76-residue protein attached to CC proteins as an intracellular targeting signal). CC {ECO:0000256|HAMAP-Rule:MF_04044}. CC -!- SUBUNIT: Interacts with host CUL1 and CUL4A; these interactions CC inhibit the E3 ligase activity of cullins. Interacts with inner CC tegument protein. Interacts with capsid vertex specific component CC CVC2. Interacts with the major capsid protein/MCP. CC {ECO:0000256|HAMAP-Rule:MF_04044}. CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP- CC Rule:MF_04044}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04044}. CC Host nucleus {ECO:0000256|HAMAP-Rule:MF_04044}. Note=Tightly CC associated with the capsid. {ECO:0000256|HAMAP-Rule:MF_04044}. CC -!- SIMILARITY: Belongs to the herpesviridae large tegument protein CC family. {ECO:0000256|PROSITE-ProRule:PRU00854}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04044}. 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; AY037858; AAK95420.1; -; Genomic_DNA. DR RefSeq; YP_067950.1; NC_006146.1. DR ProteinModelPortal; Q8UZI9; -. DR GeneID; 2949787; -. DR KEGG; vg:2949787; -. 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:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-HAMAP. DR HAMAP; MF_04044; HSV_LTP; 1. DR InterPro; IPR034702; HSV_LTP. DR InterPro; IPR006928; htUSP_central_domain. DR Pfam; PF04843; Herpes_teg_N; 1. DR PROSITE; PS51521; HTUSP; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04044}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04044}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04044}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04044}; KW Modulation of host ubiquitin pathway by viral deubiquitinase KW {ECO:0000256|HAMAP-Rule:MF_04044}; KW Modulation of host ubiquitin pathway by virus {ECO:0000256|HAMAP- KW Rule:MF_04044}; Protease {ECO:0000256|HAMAP-Rule:MF_04044}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_04044}; KW Thiol protease {ECO:0000256|HAMAP-Rule:MF_04044}; KW Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_04044}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04044, ECO:0000256|PROSITE- KW ProRule:PRU00854}; KW Virion tegument {ECO:0000256|HAMAP-Rule:MF_04044, ECO:0000256|PROSITE- KW ProRule:PRU00854}. FT DOMAIN 27 244 Peptidase C76. {ECO:0000259|PROSITE: FT PS51521}. FT REGION 1 267 Deubiquitination activity. FT {ECO:0000256|HAMAP-Rule:MF_04044}. FT COILED 1086 1113 {ECO:0000256|SAM:Coils}. FT COILED 1367 1404 {ECO:0000256|SAM:Coils}. FT COILED 1450 1487 {ECO:0000256|SAM:Coils}. FT COILED 1583 1610 {ECO:0000256|SAM:Coils}. FT ACT_SITE 47 47 {ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854}. FT ACT_SITE 179 179 {ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854}. FT ACT_SITE 181 181 {ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854}. FT SITE 34 34 Important for catalytic activity. FT {ECO:0000256|PROSITE-ProRule:PRU00854}. SQ SEQUENCE 3105 AA; 332895 MW; 7C6AE4D7D99FC7C3 CRC64; MRGSGRARTT DLEPPGGGGG GSALRILGTA SCNQSHCKFG RFAGIQCVSN CVLYLVKSFL AGRPLTSRPE LDDVLDEGAR LDALMRQSGI LRGHEMAQLT DVPSSVTLRA GGRVNIYRSA EIFGLVLFPA QISNSAVVQS LAEVLHGGYN GVAQFILYIC DIYAGAIIIE TDGSFYLFDP HCQKDAAPGT PAHVRVSTYA HDILQYVGAP GAQYTCVHLY FLPEAFEMED PRVFMLEHYG VYDFYEANGS GFDLVGPELV SSDGEQMASP APDRSPPVML PFQRQIIPYN LRPLPSRSLS SETRPARMPE TSPSAPVGAQ TAPGPPVGAS EAPADAASSP PLFIPIPGLG PGPEPPSTPP RGTGGLAPQT PKRKKGPGKD SPHKKPTSGR RLPMSSTTDT EDDQPPPRRP PSVLTRLPAP VVTVPQPQPA VPTQPASVPP SAAPPPHPSP VIPIPHSPTP KPPPDPTTSQ LPTPQPPPIS TPLVPPISTP LVPRTPTPQP PQAATPTPQP PQAATPTPQP PQAATPTPQP PQAATPTPQP PQAATPTPQP PQAATPTPQP PQATSHAPQL PRAASPAPQP TPTATATPQP PPVETSEPEQ IPSSTSPLPS VQRQSSGEDA SVGSGLVRYL SDVEEPFLSM SESEEDMDFA SDIPTSEEEE DDVFSNGRIR TSRRRTMANA SHPPPAWTPP GAATIKPPLT WPRPRWTLAR SSATFKRLPD TRTPTGPSSM TRPLTGKCRR DALSTIDHLL VTVVLEQGLI RSRSRSAALN LLEFLKDWSG NLQVPTRDLE RLLTSELNVQ NLAAMLSENK GRASEFHMHL AAKLAACLPS LAAEDASRVD AAAGLLAKIP RLAEAADGKF DLDKARRRLT DLLRPLAPTK DESPSRKNGW KRKGLTTHPP GLPEPAASAN APLVLDDERW RRLMSLAEVA GPRGRTSGAA VDEEDVRFLA LLTAIEYGAP SASVVPPFVH NVAAGPKPRA LHVRKYTADV RDRVASAASD YLSYLEDPSL PTVMDFDDLL TRLRHTCQII ASLSDLNIRH ASIERDYREL LYLGTALGDM TGIPWPLERV EEDDAAIAPL PEFETVAEKQ KELEATKENE KRLRVILEDI EAMLGLAGVA SAPRGAPGSP ADPDATPPLA DTAALTIPVM EKYIANAGSI VGAAKNPTYI RLRDTIQQIV RSKKYLMNIL KSITFYTVDN YISSFEESID HLYRGLPALD PEVQEGIDRI LDPMVSEALH TFETGNRLTL EPVRLVALQN FATHSTLRET AAAVNLLPGL LAVYDATVSG RAPENALRLL AGLQNQLSQT LIPGKLKKRF LSYLQKLKND NNDQLRQKEA QAWRLEADGF APASEEQLKA FLDTAPNKEL KRQYEKKLRR LLEAGRKEKE LLREREARER TERRAREAGE AWARIQKALG TRPEPAPTAP DDWNTLLASL TPEAPDDSKV EAATAKADAA ARNAEVLETL TRILAAMLSE ITRVKRERLR ALLGDGGGVE RMEAAEPGWF AELEAGPLAR LDAWPTTAST SDGGGRGAEE AGALFRARTA AGALRAALTQ ARQALQSPDA KSATVNTDLE APYEGYERGL AELQEKRRAA EAALSAAVSE YVDRTLPGAL DDPSRPAVPP PPSLPPPATS DPTLWPKKSQ LLTKRERDDL LQATGDFFSE LLTEAEAAQV RALEERVLES RALAARAHET AVGARRGFQT ALEAVLARAR EEAPDDELRA LLPTSSTPKS SIHETLAAAL GRAAARDGSW PYRRSLAAAE WIRDVCGAVR GLAEGALALA GGPATWLELA AAAEDQIGEL KRLLELESMA QNSMDGMEEL RLALATVDPR RVAGGKETVA DWKRRLARLE AIIQEAREES RLQDVLQDLV TRARGHVDPR QLKIVAEAAR GLALGAAAGS PQYALLRDRL VRYASAKQSF LAFYETAQPT VFVRRPLTDT GDRPLLAPRA PASPTGPLPV RRAQFLAAAG PAKYAGTLWL ETESPCDPLN PAYVSSDTQE PLNYIPVYHN FLEYVMPTVL ENPEAFALAP AGQPSARGRE ARTLASVASA RLGAAAADSY WDSWSDVEAN AGELLREYVS APKALMEDLA DNPIVAMTLL AHATLIASRN HPPFPTPATD REVILLEQRE IMTLLVGTHP AYAAAFLGAP SFYAGLGLVS ALARDGGLGE LLSDAVLTYR LVRSPAERKR GSSSTAATGA QNVGDAHRRF TGPPSGFIFL QEAWEEIETR AALWPHPEFL GLVHNQSTAR ARACLLLLAR RCFAPEALQQ LWHSLRPLEG PVAFQDYVRD FVRRAYTRGE ELPRAESVEV PRETPSTYGT VTGRALRNLM PYGTPITGPK RGSGDAIPVS VFEAAVAAAF LGRPLTLFVS SQYLFNVKTL GQVRVVAPLL YCDGRSEPFR SLAETVSLDF MKDLEGYSES FEPEMSVFAR QAAWLRELLA EARAAKPKEA QAPTVAVLAN RKNIVWKCFT YRHNLPDLQF HFNPAGASRW PTDVLNPSFY EHEDPPPVGY RPPPNPRNVQ ELFSGFPPRV GHGLVSGDGF QSADNTPASV RFQSPGGETE EDEEGSAAAD SEASVPPSPQ SPRLPAVTGR AGEWPAPSLS PRGTSAAPRE PAPASLPHSR GTVGPHRAGE KGPATAVESP GASPRPWPRE VQEIVPAPAA QGTIASPGAS QRGPAIYNLH PPPSPAAAGP QKHTIQIPGL GSPPAGPRQP QPPAATASGR PAGATATAAT PASSSVLGPR RPGLGDASPA PPHGHSIMQR ERQRPGGQEE HAKVQSTAAP HRPPPVSLKP RTPGVASTAQ ATLPAWDSTG GYGTGARPRE PLEEGAVPGP TRPPGGGLAP RPHQPPVQKP PAATAPAPTT GLAVVGGHTP GPAGAMDTAA RPEETVTKAP PPAAVQPRVP LPVKSKQQQT PAFPLTPMHP GSAPSARPEV EPPQSRHAGA PTYIAKKAGP SAAPSPPRKS QKYEDSIYYP PSGSIHYPAP FQTLSFSRDK ASPTPSSDQP ELLWNTPSVV TQFLSIEDII REVVSGGSTP GDLVVPSAAH SSLSAATPDQ DMRYSLTLAQ ARRVLTRFVT QLRHKLERST HRLITDLERL KFLYL //