SCAF_HCMVA
ID SCAF_HCMVA Reviewed; 708 AA.
AC P16753; Q69030; Q7M6L0; Q7M6L1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [3]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [5]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [6]
RP MULTIMERIZATION, AND INTERACTION WITH UL86.
RX PubMed=8985337; DOI=10.1128/jvi.71.1.179-190.1997;
RA Wood L.J., Baxter M.K., Plafker S.M., Gibson W.;
RT "Human cytomegalovirus capsid assembly protein precursor (pUL80.5)
RT interacts with itself and with the major capsid protein (pUL86) through two
RT different domains.";
RL J. Virol. 71:179-190(1997).
RN [7]
RP REVIEW, AND ISOFORM UL80.4 PROTEIN AND UL80.3 PROTEIN.
RX PubMed=18637507; DOI=10.1007/978-3-540-77349-8_11;
RA Gibson W.;
RT "Structure and formation of the cytomegalovirus virion.";
RL Curr. Top. Microbiol. Immunol. 325:187-204(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PROTEASE.
RX PubMed=8805706; DOI=10.1038/383272a0;
RA Tong L., Qian C., Massariol M.-J., Bonneau P.R., Cordingley M.G.,
RA Lagace L.;
RT "A new serine-protease fold revealed by the crystal structure of human
RT cytomegalovirus protease.";
RL Nature 383:272-275(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PROTEASE.
RX PubMed=8805707; DOI=10.1038/383275a0;
RA Qiu X., Culp J.S., Dilella A.G., Hellmig B., Hoog S.S., Janson C.A.,
RA Smith W.W., Abdel-Meguid S.A.;
RT "Unique fold and active site in cytomegalovirus protease.";
RL Nature 383:275-279(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF PROTEASE.
RX PubMed=8805708; DOI=10.1038/383279a0;
RA Shieh H.-S., Kurumbail R.G., Stevens A.M., Stegeman R.A., Sturman E.J.,
RA Pak J.Y., Wittwer A.J., Palmier M.O., Wiegand R.C., Holwerda B.C.,
RA Stallings W.C.;
RT "Three-dimensional structure of human cytomegalovirus protease.";
RL Nature 383:279-282(1996).
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=P16753-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, UL80.5;
CC IsoId=P16753-2; Sequence=VSP_037423;
CC Name=UL80.4 protein;
CC IsoId=P16753-3; Sequence=VSP_037424;
CC Name=UL80.3 protein;
CC IsoId=P16753-4; Sequence=VSP_037425;
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=CAA35354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17403; CAA35353.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35354.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK000394; DAA00177.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00178.1; -; Genomic_DNA.
DR PIR; S09843; QQBEB8.
DR PDB; 1CMV; X-ray; 2.27 A; A/B=1-256.
DR PDB; 1ID4; X-ray; 2.20 A; A/B=1-256.
DR PDB; 1IEC; X-ray; 2.20 A; A/B=1-256.
DR PDB; 1IED; X-ray; 2.00 A; A/B=1-256.
DR PDB; 1IEF; X-ray; 2.30 A; A/B=1-256.
DR PDB; 1IEG; X-ray; 2.00 A; A/B=1-256.
DR PDB; 1JQ6; X-ray; 2.30 A; A=1-256.
DR PDB; 1JQ7; X-ray; 3.00 A; A/B=1-256.
DR PDB; 1LAY; X-ray; 2.50 A; A=1-256.
DR PDB; 1NJT; X-ray; 2.50 A; A/B/C/D=1-256.
DR PDB; 1NJU; X-ray; 2.70 A; A/B/C/D=1-256.
DR PDB; 1NKK; X-ray; 2.60 A; A/B/C/D=1-256.
DR PDB; 1NKM; X-ray; 2.70 A; A/B=1-256.
DR PDB; 1WPO; X-ray; 2.00 A; A/B=1-256.
DR PDB; 2WPO; X-ray; 2.70 A; A/B/C/D=1-256.
DR PDBsum; 1CMV; -.
DR PDBsum; 1ID4; -.
DR PDBsum; 1IEC; -.
DR PDBsum; 1IED; -.
DR PDBsum; 1IEF; -.
DR PDBsum; 1IEG; -.
DR PDBsum; 1JQ6; -.
DR PDBsum; 1JQ7; -.
DR PDBsum; 1LAY; -.
DR PDBsum; 1NJT; -.
DR PDBsum; 1NJU; -.
DR PDBsum; 1NKK; -.
DR PDBsum; 1NKM; -.
DR PDBsum; 1WPO; -.
DR PDBsum; 2WPO; -.
DR SMR; P16753; -.
DR BindingDB; P16753; -.
DR ChEMBL; CHEMBL3771; -.
DR DrugBank; DB07436; N-(1-PHENYL-PROPYL)-FORMAMIDE.
DR DrugBank; DB01973; O-Benzylsulfonyl-Serine.
DR DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DR MEROPS; S21.002; -.
DR EvolutionaryTrace; P16753; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; 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_0000027284"
FT CHAIN 1..256
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027285"
FT CHAIN 257..708
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027286"
FT REGION 269..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..619
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 MOTIF 537..543
FT /note="Nuclear localization signal 2"
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_037425"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform UL80.4 protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_037424"
FT VAR_SEQ 1..335
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_037423"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1IEG"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 64..78
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1LAY"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1LAY"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1JQ7"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:1IED"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1JQ7"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:1JQ6"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:1IED"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1IED"
SQ SEQUENCE 708 AA; 73852 MW; 32A993D6586824C9 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 EAACDIKAAS AERSGDSRSQ AATPAAGARV PSSSPSPPVE
PPSPVQPPAL PASPSVLPAE SPPSLSPSEP AEAASMSHPL SAAVPAATAP PGATVAGASP
AVSSLAWPHD GVYLPKDAFF SLLGASRSAV PVMYPGAVAA PPSASPAPLP LPSYPASYGA
PVVGYDQLAA RHFADYVDPH YPGWGRRYEP APSLHPSYPV PPPPSPAYYR RRDSPGGMDE
PPSGWERYDG GHRGQSQKQH RHGGSGGHNK RRKETAAASS SSSDEDLSFP GEAEHGRARK
RLKSHVNSDG GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPSAASS
SPTTTTVCTP TGELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA SGSEAATAGP
STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF VAALNKLE
