ID Q8UZI9_9GAMA Unreviewed; 3105 AA. AC Q8UZI9; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 29-SEP-2021, entry version 70. 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; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus. OX NCBI_TaxID=45455 {ECO:0000313|EMBL:AAK95420.1, ECO:0000313|Proteomes:UP000201521}; RN [1] {ECO:0000313|EMBL:AAK95420.1, ECO:0000313|Proteomes:UP000201521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1, RC ECO:0000313|Proteomes:UP000201521}; RX PubMed=8892903; RA Franken M., Devergne O., Rosenzweig M., Annis B., Kieff E., Wang F.; RT "Comparative analysis identifies conserved tumor necrosis factor receptor- RT associated factor 3 binding sites in the human and simian Epstein-Barr RT virus oncogene LMP1."; RL J. Virol. 70:7819-7826(1996). RN [2] {ECO:0000313|EMBL:AAK95420.1, ECO:0000313|Proteomes:UP000201521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1, RC ECO:0000313|Proteomes:UP000201521}; RX PubMed=10482645; RA Rivailler P., Quink C., Wang F.; RT "Strong selective pressure for evolution of an Epstein-Barr virus LMP2B RT homologue in the rhesus lymphocryptovirus."; RL J. Virol. 73:8867-8872(1999). RN [3] {ECO:0000313|EMBL:AAK95420.1, ECO:0000313|Proteomes:UP000201521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1, RC ECO:0000313|Proteomes:UP000201521}; RX PubMed=10970361; RA Rao P., Jiang H., Wang F.; RT "Cloning of the rhesus lymphocryptovirus viral capsid antigen and Epstein- RT Barr virus-encoded small RNA homologues and use in diagnosis of acute and RT persistent infections."; RL J. Clin. Microbiol. 38:3219-3225(2000). RN [4] {ECO:0000313|EMBL:AAK95420.1, ECO:0000313|Proteomes:UP000201521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1, RC ECO:0000313|Proteomes:UP000201521}; 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, ECO:0000313|Proteomes:UP000201521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95420.1, RC ECO:0000313|Proteomes:UP000201521}; 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 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:0000256|ARBA:ARBA00004020, ECO:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_04044}. CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP- CC Rule:MF_04044}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04044}. Host CC nucleus {ECO:0000256|HAMAP-Rule:MF_04044}. Note=Tightly associated with CC the capsid. {ECO:0000256|HAMAP-Rule:MF_04044}. CC -!- SIMILARITY: Belongs to the herpesviridae large tegument protein family. CC {ECO:0000256|PROSITE-ProRule:PRU00854}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 GeneID; 2949787; -. DR KEGG; vg:2949787; -. DR Proteomes; UP000201521; 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:thiol-dependent deubiquitinase; IEA:UniProtKB-UniRule. DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-UniRule. 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP- KW Rule:MF_04044}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP- KW Rule:MF_04044}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04044}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04044}; KW Modulation of host ubiquitin pathway by viral deubiquitinase KW {ECO:0000256|ARBA:ARBA00022876, ECO:0000256|HAMAP-Rule:MF_04044}; KW Modulation of host ubiquitin pathway by virus KW {ECO:0000256|ARBA:ARBA00022662, ECO:0000256|HAMAP-Rule:MF_04044}; KW Protease {ECO:0000256|HAMAP-Rule:MF_04044}; KW Reference proteome {ECO:0000313|Proteomes:UP000201521}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, 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|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04044}; KW Virion tegument {ECO:0000256|ARBA:ARBA00022580, ECO:0000256|HAMAP- KW Rule:MF_04044}. FT DOMAIN 27..244 FT /note="Peptidase C76" FT /evidence="ECO:0000259|PROSITE:PS51521" FT REGION 1..267 FT /note="Deubiquitination activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04044" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 291..627 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 675..700 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 873..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1616..1645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2198..2219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2508..2977 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1086..1113 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1367..1404 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1450..1487 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1583..1610 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1849..1869 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 294..318 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 344..362 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..387 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 422..565 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 573..597 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 598..621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 683..697 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 873..889 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1623..1642 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2549..2563 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2803..2817 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2843..2863 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 47 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854" FT ACT_SITE 179 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854" FT ACT_SITE 181 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04044, FT ECO:0000256|PROSITE-ProRule:PRU00854" FT SITE 34 FT /note="Important for catalytic activity" FT /evidence="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 //