P10210 (PPR_HHV11) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protease precursor
Short name=pPR

Alternative name(s):
Capsid protein P40
Virion structural protein UL26

Cleaved into the following 2 chains:

1. Assemblin
   EC=3.4.21.97
   Alternative name(s):
   Capsid protein VP24
   Protease
2. Assembly protein
   Alternative name(s):
   Capsid protein VP22A

Gene names

Name:

UL26

Organism

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › Human herpesvirus 1

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protease precursor plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein VP5 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as VP5 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein VP5. Cleavages products are evicted from the capsid before or during DNA packaging By similarity. Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging By similarity. Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein VP5. Multimerizes in the nucleus such as VP5 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 By similarity.
Catalytic activity	Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
Subunit structure	Protease precursor homomultimerizes and interacts with major capsid protein VP5. Assemblin exists in a monomer-dimer equilibrium with the dimer being the active species. Assembly protein homomultimerizes and interacts with major capsid protein VP5 By similarity.
Subcellular location	Protease precursor: Host cytoplasm By similarity. Assemblin: Host nucleus By similarity. Assembly protein: Host nucleus By similarity.
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) By similarity.
Post-translational modification	Protease precursor is cleaved by assemblin after completion of icosahedral capsid formation. Cleavages occur at two or more sites: release and tail site By similarity. Assembly protein is phosphorylated.
Sequence similarities	Belongs to the peptidase S21 family.

Ontologies

Keywords
Cellular component	Host cytoplasm Host nucleus
Coding sequence diversity	Alternative promoter usage
Molecular function	Hydrolase Protease Serine protease Viral capsid scaffolding protein
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform Protease precursor (identifier: P10210-1)

Also known as: pPR; UL26;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform pAP (identifier: P10210-2)

Also known as: Assembly protein; UL26.5 protein;

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 635	635	Protease precursor		PRO_0000027244
	Chain	1 – 247	247	Assemblin		PRO_0000027245
	Chain	248 – 635	388	Assembly protein		PRO_0000027246
Regions
	Region	324 – 343	20	Interaction with pAP
	Region	618 – 635	18	Interaction with major capsid protein
	Motif	426 – 429	4	Nuclear localization signal Potential
	Compositional bias	514 – 590	77	Pro-rich
Sites
	Active site	61	1	Charge relay system By similarity
	Active site	129	1	Charge relay system By similarity
	Active site	148	1	Charge relay system By similarity
	Site	247 – 248	2	Cleavage; by assemblin; Release site By similarity
	Site	610 – 611	2	Cleavage; by assemblin; Tail site By similarity
Natural variations
	Alternative sequence	1 – 306	306	Missing in isoform pAP.		VSP_037414

Sequences

	Sequence		Length	Mass (Da)
	Isoform Protease precursor (pPR) (UL26) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: F3B3C7D42F3D062D	FASTA	635	66,471
	10 20 30 40 50 60 MAADAPGDRM EEPLPDRAVP IYVAGFLALY DSGDSGELAL DPDTVRAALP PDNPLPINVD 70 80 90 100 110 120 HRAGCEVGRV LAVVDDPRGP FFVGLIACVQ LERVLETAAS AAIFERRGPP LSREERLLYL 130 140 150 160 170 180 ITNYLPSVSL ATKRLGGEAH PDRTLFAHVA LCAIGRRLGT IVTYDTGLDA AIAPFRHLSP 190 200 210 220 230 240 ASREGARRLA AEAELALSGR TWAPGVEALT HTLLSTAVNN MMLRDRWSLV AERRRQAGIA 250 260 270 280 290 300 GHTYLQASEK FKMWGAEPVS APARGYKNGA PESTDIPPGS IAAAPQGDRC PIVRQRGVAL 310 320 330 340 350 360 SPVLPPMNPV PTSGTPAPAP PGDGSYLWIP ASHYNQLVAG HAAPQPQPHS AFGFPAAAGS 370 380 390 400 410 420 VAYGPHGAGL SQHYPPHVAH QYPGVLFSGP SPLEAQIAAL VGAIAADRQA GGQPAAGDPG 430 440 450 460 470 480 VRGSGKRRRY EAGPSESYCD QDEPDADYPY YPGEARGAPR GVDSRRAARH SPGTNETITA 490 500 510 520 530 540 LMGAVTSLQQ ELAHMRARTS APYGMYTPVA HYRPQVGEPE PTTTHPALCP PEAVYRPPPH 550 560 570 580 590 600 SAPYGPPQGP ASHAPTPPYA PAACPPGPPP PPCPSTQTRA PLPTEPAFPP AATGSQPEAS 610 620 630 NAEAGALVNA SSAAHVDVDT ARAADLFVSQ MMGAR
	Isoform pAP (Assembly protein) (UL26.5 protein) [UniParc]. Checksum: DF690388D0630F9D	FASTA	329	33,760
	10 20 30 40 50 60 MNPVPTSGTP APAPPGDGSY LWIPASHYNQ LVAGHAAPQP QPHSAFGFPA AAGSVAYGPH 70 80 90 100 110 120 GAGLSQHYPP HVAHQYPGVL FSGPSPLEAQ IAALVGAIAA DRQAGGQPAA GDPGVRGSGK 130 140 150 160 170 180 RRRYEAGPSE SYCDQDEPDA DYPYYPGEAR GAPRGVDSRR AARHSPGTNE TITALMGAVT 190 200 210 220 230 240 SLQQELAHMR ARTSAPYGMY TPVAHYRPQV GEPEPTTTHP ALCPPEAVYR PPPHSAPYGP 250 260 270 280 290 300 PQGPASHAPT PPYAPAACPP GPPPPPCPST QTRAPLPTEP AFPPAATGSQ PEASNAEAGA 310 320 LVNASSAAHV DVDTARAADL FVSQMMGAR

References

[1]	"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1." McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P. J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1." Davison M.D., Rixon F.J., Davison A.J. J. Gen. Virol. 73:2709-2713(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 11-29; 77-91 AND 223-241.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14112 Genomic DNA. Translation: CAA32318.1. X14112 Genomic DNA. Translation: CAA32319.1.
PIR	WMBEW6. H30084.
RefSeq	NP_044627.1. NC_001806.1. NP_044628.1. NC_001806.1.
3D structure databases
ProteinModelPortal	P10210.
SMR	P10210. Positions 17-247.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1096N.
MINT	MINT-6732542.
Protein family/group databases
MEROPS	S21.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2703453. 2703454.
Phylogenomic databases
ProtClustDB	CLSP2510154.
Family and domain databases
Gene3D	3.20.16.10. 1 hit.
InterPro	IPR001847. Peptidase_S21. [Graphical view]
Pfam	PF00716. Peptidase_S21. 1 hit. [Graphical view]
PRINTS	PR00236. HSVCAPSIDP40.
SUPFAM	SSF50789. Peptidase_S21. 1 hit.
ProtoNet	Search...
Other
BindingDB	P10210.
ChEMBL	CHEMBL3518.

Entry information

Entry name

PPR_HHV11

Accession

Primary (citable) accession number: P10210
Secondary accession number(s): O09798

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program