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Capsid scaffolding protein (Protease precursor) (pPR) [Cleaved into: Assembly protein (Capsid assembly protein); Assemblin (EC 3.4.21.97) (Protease)]

 A0A0G2TJS5_HCMV         Unreviewed;       708 AA.
A0A0G2TJS5;
16-SEP-2015, integrated into UniProtKB/TrEMBL.
16-SEP-2015, sequence version 1.
25-APR-2018, entry version 20.
RecName: Full=Capsid scaffolding protein {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Protease precursor {ECO:0000256|HAMAP-Rule:MF_04008};
Short=pPR {ECO:0000256|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assemblin {ECO:0000256|HAMAP-Rule:MF_04008};
EC=3.4.21.97 {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Protease {ECO:0000256|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Capsid assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
Name=UL80 {ECO:0000313|EMBL:AKI13478.1};
Human cytomegalovirus (HHV-5) (Human herpesvirus 5).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Betaherpesvirinae; Cytomegalovirus.
NCBI_TaxID=10359 {ECO:0000313|EMBL:AKI13478.1, ECO:0000313|Proteomes:UP000099255};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:AHJ82297.1}
NUCLEOTIDE SEQUENCE.
STRAIN=2CEN15 {ECO:0000313|EMBL:AHJ82297.1}, and
PAV6 {ECO:0000313|EMBL:AHJ84652.1};
Wilkie G.S., Zavattoni M., Davison A.J.;
"Diversity of human cytomegalovirus.";
Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AHJ83306.1}
NUCLEOTIDE SEQUENCE.
STRAIN=HAN32 {ECO:0000313|EMBL:AHJ83306.1};
Davison A.J.;
"Human cytomegalovirus RL11 gene family: variation, recombination and
transcription.";
Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000099255, ECO:0000313|Proteomes:UP000106410, ECO:0000313|Proteomes:UP000112015}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BE/10/2011 {ECO:0000313|EMBL:AKI08629.1},
BE/10/2012 {ECO:0000313|EMBL:AKI10311.1},
BE/18/2011 {ECO:0000313|EMBL:AKI13478.1},
BE/20/2011 {ECO:0000313|EMBL:AKI18492.1},
BE/26/2011 {ECO:0000313|EMBL:AKI19330.1},
BE/27/2011 {ECO:0000313|EMBL:AKI18156.1},
BE/32/2011 {ECO:0000313|EMBL:AKI19498.1},
BE/5/2012 {ECO:0000313|EMBL:AKI07962.1}, and
BE/6/2011 {ECO:0000313|EMBL:AKI12144.1};
PubMed=25972543;
Sijmons S., Thys K., Mbong Ngwese M., Van Damme E., Dvorak J.,
Van Loock M., Li G., Tachezy R., Busson L., Aerssens J., Van Ranst M.,
Maes P.;
"High-throughput analysis of human cytomegalovirus genome diversity
highlights the widespread occurrence of gene-disrupting mutations and
pervasive recombination.";
J. Virol. 0:0-0(2015).
[4] {ECO:0000313|EMBL:AKI24549.1}
NUCLEOTIDE SEQUENCE.
STRAIN=JER2002 {ECO:0000313|EMBL:AKI24549.1}, and
JER4559 {ECO:0000313|EMBL:AKI25733.1};
Wilkie G.S., Holton M.L., Ganzenmueller T., Kerr K., Cunningham C.,
Campanini G., Wilkinson G.W.G., Zavattoni M., Wolf D., Schulz T.F.,
Davison A.J.;
"High-throughput sequencing of complete human cytomegalovirus genomes
directly from clinical material.";
Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:AMJ54107.1}
NUCLEOTIDE SEQUENCE.
STRAIN=UK/Lon6/Urine/2011 {ECO:0000313|EMBL:AMJ54107.1}, and
UK/Lon9/Urine/2012 {ECO:0000313|EMBL:AMJ54774.1};
Lassalle F., Depledge D.P., Reeves M.B., Brown A.C.,
Christiansen M.T., Tutill H.J., Williams R.J., Einer-Jensen K.,
Holdstock J., Atkinson C., Brown J.R., van Loenen F.B., Clark D.A.,
Griffiths P.D., Verjans G.M.G.M., Schutten M., Milne R.S.B.,
Balloux F., Breuer J.;
"Islands of linkage in an ocean of pervasive recombination reveals
two-speed evolution of human cytomegalovirus genomes.";
Virus Evol 2:vew017-vew017(2016).
[6] {ECO:0000313|EMBL:AQN70197.1}
NUCLEOTIDE SEQUENCE.
STRAIN=PRA4 {ECO:0000313|EMBL:AQN70197.1};
Suarez N., Gerna G., Hage E., Hubacek P., Davison A.J.;
"The challenges of sequencing complete human cytomegalovirus genomes
directly from clinical material.";
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:AMJ54107.1}
NUCLEOTIDE SEQUENCE.
STRAIN=UK/Lon6/Urine/2011 {ECO:0000313|EMBL:AMJ54107.1}, and
UK/Lon9/Urine/2012 {ECO:0000313|EMBL:AMJ54774.1};
Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Assemblin: Protease that plays an essential role in
virion assembly within the nucleus. Catalyzes the cleavage of the
assembly protein after formation of the spherical procapsid. By
that cleavage, the capsid matures and gains its icosahedral shape.
The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well
as Ala-Thr bonds. Assemblin and cleavages products are evicted
from the capsid before or during DNA packaging.
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- FUNCTION: Assembly protein: Plays a major role in capsid assembly.
Acts as a scaffold protein by binding major capsid protein.
Multimerizes in the nucleus such as major capsid protein forms the
icosahedral T=16 capsid. Cleaved by assemblin after capsid
completion. The cleavages products are evicted from the capsid
before or during DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- FUNCTION: Capsid scaffolding protein: Acts as a scaffold protein
by binding major capsid protein in the cytoplasm, inducing the
nuclear localization of both proteins. Multimerizes in the nucleus
such as major capsid protein forms the icosahedral T=16 capsid.
Autocatalytic cleavage releases the assembly protein, and
subsequently abolishes interaction with major capsid protein.
Cleavages products are evicted from the capsid before or during
DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- CATALYTIC ACTIVITY: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in
the scaffold protein. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts
with major capsid protein. Assemblin exists in a monomer-dimer
equilibrium with the dimer being the active species. Assembly
protein homomultimerizes and interacts with major capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- DOMAIN: Region of interaction between pPR and pAP is called Amino
conserved domain (ACD). The region of interaction with major
capsid protein is called carboxyl conserved domain (CCD).
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- PTM: Capsid scaffolding protein is cleaved by assemblin after
formation of the spherical procapsid. As a result, the capsid
obtains its mature, icosahedral shape. Cleavages occur at two or
more sites: release and tail site. {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding
protein family. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04008}.
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EMBL; KJ361948; AHJ82297.1; -; Genomic_DNA.
EMBL; KJ361954; AHJ83306.1; -; Genomic_DNA.
EMBL; KJ361962; AHJ84652.1; -; Genomic_DNA.
EMBL; KP745635; AKI07962.1; -; Genomic_DNA.
EMBL; KP745639; AKI08629.1; -; Genomic_DNA.
EMBL; KP745649; AKI10311.1; -; Genomic_DNA.
EMBL; KP745660; AKI12144.1; -; Genomic_DNA.
EMBL; KP745668; AKI13478.1; -; Genomic_DNA.
EMBL; KP745696; AKI18156.1; -; Genomic_DNA.
EMBL; KP745698; AKI18492.1; -; Genomic_DNA.
EMBL; KP745703; AKI19330.1; -; Genomic_DNA.
EMBL; KP745704; AKI19498.1; -; Genomic_DNA.
EMBL; KR534201; AKI24549.1; -; Genomic_DNA.
EMBL; KR534208; AKI25733.1; -; Genomic_DNA.
EMBL; KT726949; AMJ54107.1; -; Genomic_DNA.
EMBL; KT726953; AMJ54774.1; -; Genomic_DNA.
EMBL; KY490066; AQN70197.1; -; Genomic_DNA.
Proteomes; UP000099255; Genome.
Proteomes; UP000106410; Genome.
Proteomes; UP000112015; Genome.
Proteomes; UP000139295; Genome.
Proteomes; UP000139920; Genome.
Proteomes; UP000156497; Genome.
Proteomes; UP000158879; Genome.
Proteomes; UP000161201; Genome.
Proteomes; UP000169355; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
Gene3D; 3.20.16.10; -; 1.
HAMAP; MF_04008; HSV_SCAF; 1.
InterPro; IPR035443; Herpes_virus_sf.
InterPro; IPR001847; Peptidase_S21.
Pfam; PF00716; Peptidase_S21; 1.
PRINTS; PR00236; HSVCAPSIDP40.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000099255,
ECO:0000313|Proteomes:UP000106410, ECO:0000313|Proteomes:UP000112015,
ECO:0000313|Proteomes:UP000139295};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04008};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04008};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04008};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04008};
Protease {ECO:0000256|HAMAP-Rule:MF_04008};
Serine protease {ECO:0000256|HAMAP-Rule:MF_04008};
Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04008};
Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04008}.
REGION 688 708 Interaction with major capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04008}.
COILED 559 586 {ECO:0000256|SAM:Coils}.
ACT_SITE 63 63 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
ACT_SITE 132 132 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
ACT_SITE 157 157 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
SITE 256 257 Cleavage; by assemblin; Release site.
{ECO:0000256|HAMAP-Rule:MF_04008}.
SEQUENCE 708 AA; 73904 MW; 6EC9A69DDCC1A8B8 CRC64;
MTMDEQQPQA VAPVYVGGFL ARYDQSPDEA ELLLPRDVVE HWLYAQSQGQ 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 AEASSMSHPL SAAVTAATAP PGTTVAGASP
AVPSLAWPHD GVYLPKDAFF SLLGASRSAA PVMYPGAVAA PPSASPAPLP LPSYPASYGA
PVVGYDQLAA RHFADYVDPH YPGWGRRYEP APSLHPSYPV PPPPSPAYYR RRDSPGGMDE
PPSGWERYDG GHRGQSQKQH RHGGSGGHNK RRKEAAAASS SSSDEDLSFP GEAEHGRARK
RLKSHVNSDG GSGGHAGSNQ QQQQRYDELR DAIHELKRDL FAARQSSTLL SAALPAAASS
SPTTTTVCTP TGELTSGGGE TPTALLSGGA KVAERAQAGV VNASCRLATA SGSEAATAGP
STAGSSSCPA SVVLAAAAAQ AAAASQSPPK DMVDLNRRIF VAALNKLE


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