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Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease); Assembly protein (Capsid assembly protein)]

 SCAF_SCMVC              Reviewed;         589 AA.
P16046;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 3.
23-MAY-2018, entry version 101.
RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
AltName: Full=Capsid protein P40;
AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assemblin {ECO:0000255|HAMAP-Rule:MF_04008};
EC=3.4.21.97 {ECO:0000255|HAMAP-Rule:MF_04008};
AltName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
AltName: Full=Capsid assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
Name=UL80; Synonyms=APNG;
Simian cytomegalovirus (strain Colburn).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Betaherpesvirinae; Cytomegalovirus.
NCBI_TaxID=50292;
NCBI_TaxID=9539; Macaca (macaques).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1649317;
Welch A.R., McNally L.M., Gibson W.;
"Cytomegalovirus assembly protein nested gene family: four 3'-
coterminal transcripts encode four in-frame, overlapping proteins.";
J. Virol. 65:4091-4100(1991).
[2]
SEQUENCE REVISION TO 501.
Brignole E., Gibson W.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF ISOFORM PAP.
PubMed=2536099;
Robson L., Gibson W.;
"Primate cytomegalovirus assembly protein: genome location and
nucleotide sequence.";
J. Virol. 63:669-676(1989).
[4]
CHARACTERIZATION OF ASSEMBLIN.
PubMed=1961747; DOI=10.1073/pnas.88.23.10792;
Welch A.R., Woods A.S., McNally L.M., Cotter R.J., Gibson W.;
"A herpesvirus maturational proteinase, assemblin: identification of
its gene, putative active site domain, and cleavage site.";
Proc. Natl. Acad. Sci. U.S.A. 88:10792-10796(1991).
[5]
SUBCELLULAR LOCATION.
PubMed=9733808;
Plafker S.M., Gibson W.;
"Cytomegalovirus assembly protein precursor and proteinase precursor
contain two nuclear localization signals that mediate their own
nuclear translocation and that of the major capsid protein.";
J. Virol. 72:7722-7732(1998).
-!- 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:0000255|HAMAP-Rule:MF_04008}.
-!- 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:0000255|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:0000255|HAMAP-Rule:MF_04008}.
-!- CATALYTIC ACTIVITY: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in
the scaffold protein. {ECO:0000255|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:0000255|HAMAP-Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Capsid scaffolding protein: Host cytoplasm
{ECO:0000255|HAMAP-Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Assemblin: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Assembly protein: Host nucleus
{ECO:0000255|HAMAP-Rule:MF_04008}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=4;
Name=Capsid scaffolding protein; Synonyms=pPR;
IsoId=P16046-1; Sequence=Displayed;
Name=APNG.7 protein;
IsoId=P16046-2; Sequence=VSP_037428;
Name=pAP; Synonyms=Assembly protein, APGN.5 protein;
IsoId=P16046-3; Sequence=VSP_037427;
Name=APNG.4 protein;
IsoId=P16046-4; Sequence=VSP_037426;
-!- 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:0000255|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:0000255|HAMAP-
Rule:MF_04008}.
-!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding
protein family. {ECO:0000255|HAMAP-Rule:MF_04008}.
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EMBL; M64627; AAA46065.2; -; Genomic_DNA.
EMBL; M24205; AAA85777.1; -; mRNA.
PIR; A40414; WMBECB.
ProteinModelPortal; P16046; -.
SMR; P16046; -.
PRIDE; P16046; -.
PMAP-CutDB; P16046; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0039708; P:nuclear capsid assembly; IDA:UniProtKB.
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.
1: Evidence at protein level;
Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
Phosphoprotein; Protease; Serine protease; Viral capsid assembly;
Viral release from host cell.
CHAIN 1 589 Capsid scaffolding protein.
/FTId=PRO_0000027289.
CHAIN 1 249 Assemblin. {ECO:0000255|HAMAP-
Rule:MF_04008}.
/FTId=PRO_0000027290.
CHAIN 250 589 Assembly protein. {ECO:0000255|HAMAP-
Rule:MF_04008}.
/FTId=PRO_0000027292.
REGION 307 326 Interaction with pAP. {ECO:0000255|HAMAP-
Rule:MF_04008}.
REGION 569 589 Interaction with major capsid protein.
{ECO:0000255|HAMAP-Rule:MF_04008}.
MOTIF 428 433 Nuclear localization signal 1.
MOTIF 453 459 Nuclear localization signal 2.
ACT_SITE 47 47 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_04008}.
ACT_SITE 118 118 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_04008}.
ACT_SITE 142 142 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_04008}.
SITE 249 250 Cleavage; by assemblin; Release site.
{ECO:0000255|HAMAP-Rule:MF_04008}.
SITE 556 557 Cleavage; by assemblin; Tail site.
VAR_SEQ 1 348 Missing (in isoform APNG.4 protein).
{ECO:0000305}.
/FTId=VSP_037426.
VAR_SEQ 1 280 Missing (in isoform pAP). {ECO:0000305}.
/FTId=VSP_037427.
VAR_SEQ 1 165 Missing (in isoform APNG.7 protein).
{ECO:0000305}.
/FTId=VSP_037428.
CONFLICT 501 501 A -> R (in Ref. 3; AAA85777).
{ECO:0000305}.
CONFLICT 537 537 A -> AS (in Ref. 3). {ECO:0000305}.
SEQUENCE 589 AA; 63715 MW; 247CBB9DCC4E5A23 CRC64;
MADPVYVGGF LVRYDEPPGE AELFLPSGVV DRWLRDCRGP LPLNVNHDES ATVGYVAGLQ
NVRAGLFCLG RVTSPKFLDI VQKASEKSEL VSRGPPSESS LRPDGVLEFL SGSYSGLSLS
SRRDINAADG AAGDAETACF KHVALCSVGR RRGTLAVYGR QPDWVMERFP DLTEADREAL
RNQLSGSGEV AAKESAESSA AAAVDPFQSD SYGLLGNSVD ALYIQERLPK LRYDKRLVGV
TARESYVKAS VSPAEQETCD IKVEKERPKE PEQSHVPTES MSHPMSAVAT PAASTVAPSQ
APLALAHDGV YLPKDAFFSL IGASRPLAEA AGARAAYPAV PPPPAYPVMN YEDPSSRHFD
YSAWLRRPAY DAVPPLPPPP VMPMPYRRRD PMMEEAERAA WERGYAPSAY DHYVNNGSWS
RSRSGALKRR RERDASSDEE EDMSFPGEAD HGKARKRLKA HHGRDNNNSG SDAKGDRYDD
IREALQELKR EMLAVRQIAP AALLAPAQLA TPVASPTTTT SHQAEASEPQ ASTAAAAPST
ASSHGSKSAE RGVVNASCRV APPLEAVNPP KDMVDLNRRL FVAALNKME


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