SCAF_HCMVM
ID SCAF_HCMVM Reviewed; 708 AA.
AC Q6SW62; D2K3N8; D2K3N9; Q6SW61;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid protein P40;
DE AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
DE Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assemblin {ECO:0000255|HAMAP-Rule:MF_04008};
DE EC=3.4.21.97 {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
GN Name=UL80; Synonyms=APNG;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
CC -!- FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by
CC binding major capsid protein in the cytoplasm, inducing the nuclear
CC localization of both proteins. Multimerizes in the nucleus such as
CC major capsid protein forms the icosahedral T=16 capsid. Autocatalytic
CC cleavage releases the assembly protein, and subsequently abolishes
CC interaction with major capsid protein. Cleavages products are evicted
CC from the capsid before or during DNA packaging. {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- FUNCTION: [Assemblin]: Protease that plays an essential role in virion
CC assembly within the nucleus. Catalyzes the cleavage of the assembly
CC protein after formation of the spherical procapsid. By that cleavage,
CC the capsid matures and gains its icosahedral shape. The cleavage sites
CC seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds.
CC Assemblin and cleavages products are evicted from the capsid before or
CC during DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- FUNCTION: [Assembly protein]: Plays a major role in capsid assembly.
CC Acts as a scaffold protein by binding major capsid protein.
CC Multimerizes in the nucleus such as major capsid protein forms the
CC icosahedral T=16 capsid. Cleaved by assemblin after capsid completion.
CC The cleavages products are evicted from the capsid before or during DNA
CC packaging. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold
CC protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008};
CC -!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts with
CC major capsid protein. Assemblin exists in a monomer-dimer equilibrium
CC with the dimer being the active species. Assembly protein
CC homomultimerizes and interacts with major capsid protein.
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=4;
CC Name=Capsid scaffolding protein; Synonyms=pPR, UL80a;
CC IsoId=Q6SW62-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, UL80.5;
CC IsoId=Q6SW62-2; Sequence=VSP_044019;
CC Name=UL80.4 protein;
CC IsoId=Q6SW62-3; Sequence=VSP_044018;
CC Name=UL80.3 protein;
CC IsoId=Q6SW62-4; Sequence=VSP_044017;
CC -!- DOMAIN: Region of interaction between pPR and pAP is called Amino
CC conserved domain (ACD). The region of interaction with major capsid
CC protein is called carboxyl conserved domain (CCD). {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- PTM: Capsid scaffolding protein is cleaved by assemblin after formation
CC of the spherical procapsid. As a result, the capsid obtains its mature,
CC icosahedral shape. Cleavages occur at two or more sites: release and
CC tail site. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR31633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY446894; AAR31632.1; -; Genomic_DNA.
DR EMBL; AY446894; AAR31633.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_081528.1; NC_006273.2.
DR RefSeq; YP_081529.1; NC_006273.2.
DR SMR; Q6SW62; -.
DR MEROPS; S21.002; -.
DR PRIDE; Q6SW62; -.
DR DNASU; 3077443; -.
DR GeneID; 3077443; -.
DR GeneID; 3077485; -.
DR KEGG; vg:3077443; -.
DR KEGG; vg:3077485; -.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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:0019028; C:viral capsid; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0039708; P:nuclear capsid assembly; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.16.10; -; 1.
DR HAMAP; MF_04008; HSV_SCAF; 1.
DR InterPro; IPR035443; Herpes_virus_sf.
DR InterPro; IPR001847; Peptidase_S21.
DR Pfam; PF00716; Peptidase_S21; 1.
DR PRINTS; PR00236; HSVCAPSIDP40.
PE 3: Inferred from homology;
KW Alternative promoter usage; Coiled coil; Host cytoplasm; Host nucleus;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..708
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000418270"
FT CHAIN 1..256
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000418271"
FT CHAIN 257..708
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000418272"
FT REGION 270..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..352
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 455..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..708
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 510..515
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 537..543
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 256..257
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 643..644
FT /note="Cleavage; by assemblin; Maturation site"
FT SITE 684..685
FT /note="Cleavage; by assemblin; Tail site"
FT VAR_SEQ 1..477
FT /note="Missing (in isoform UL80.3 protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_044017"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform UL80.4 protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_044018"
FT VAR_SEQ 1..335
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_044019"
SQ SEQUENCE 708 AA; 73838 MW; 28106DF482DB0521 CRC64;
MTMDEQQSQA VAPVYVGGFL ARYDQSPDEA ELLLPRDVVE HWLHAQGQGQ PSLSVALPLN
INHDDTAVVG HVAAMQSVRD GLFCLGCVTS PRFLEIVRRA SEKSELVSRG PVSPLQPDKV
VEFLSGSYAG LSLSSRRCDD VEAATSLSGS ETTPFKHVAL CSVGRRRGTL AVYGRDPEWV
TQRFPDLTAA DRDGLRAQWQ RCGSTAVDAS GDPFRSDSYG LLGNSVDALY IRERLPKLRY
DKQLVGVTER ESYVKASVSP EAACVIKAAS AERSGDSRSQ AATPAAGARV PSSSPSPPVE
PPSPVQPPAL PASPSVLPAE SPPSLSPSEP AEAASMSHPL SAAVPAATAP PGATVAGASP
AVSSLAWPHD GVYLPKDAFF SLLGASRSAA PVMYPGAVAA PPSASPAPLP LPSYPASYGA
PVVGYDQLAA RHFADYVDPH YPGWGRRYEP APSLHPSYPV PPPPSPAYYR RRDSPGGMDE
PPSGWERYDG GHRGQSQKQH RHGGSGGHNK RRKETAAASS SSSDEDLSFP GEAEHGRARK
RLKSHVNSDG GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPSAASS
SPTTTTVCTP TSELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA SGSEAATAGP
STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF VAALNKLE
