Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback. Take me to UniProt BETA

UniProtKB - A0A0X9ZXJ2 (A0A0X9ZXJ2_9ALPH)

Entry version 34 (25 May 2022)
Sequence version 1 (13 Apr 2016)
Previous versions | rss
Add a publicationFeedback
Protein

Capsid scaffolding protein

Gene

ORF35

Organism
Equid alphaherpesvirus 4 (Equine herpesvirus 4)
Status
Unreviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

UniRule annotation

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.

UniRule annotation

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.

UniRule annotation

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.UniRule annotation EC:3.4.21.97

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei55Charge relay systemUniRule annotation1
Active sitei123Charge relay systemUniRule annotation1
Active sitei142Charge relay systemUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine proteaseUniRule annotation
Biological processViral capsid assemblyUniRule annotationARBA annotation, Viral release from host cell

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Capsid scaffolding proteinUniRule annotation
Alternative name(s):
Protease precursorUniRule annotation
Short name:
pPRUniRule annotation
Cleaved into the following 2 chains:
AssemblinUniRule annotation (EC:3.4.21.97UniRule annotation)
Alternative name(s):
ProteaseUniRule annotation
Assembly proteinUniRule annotation
Alternative name(s):
Capsid assembly proteinUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ORF35Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEquid alphaherpesvirus 4 (Equine herpesvirus 4)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10331 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Duplodnaviria › Heunggongvirae › Peploviricota › Herviviricetes › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Host cytoplasmUniRule annotationARBA annotation, Host nucleusUniRule annotation

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_50345296881 – 647Capsid scaffolding proteinUniRule annotationAdd BLAST647
ChainiPRO_50345296871 – 242AssemblinUniRule annotationAdd BLAST242
ChainiPRO_5034529686243 – 647Assembly proteinUniRule annotationAdd BLAST405

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei242 – 243Cleavage; by assemblin; Release siteUniRule annotation2

Keywords - PTMi

PhosphoproteinUniRule annotationARBA annotation

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.

UniRule annotation

GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni290 – 321DisorderedSequence analysisAdd BLAST32
Regioni421 – 454DisorderedSequence analysisAdd BLAST34
Regioni627 – 647Interaction with major capsid proteinUniRule annotationAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi290 – 306Polar residuesSequence analysisAdd BLAST17
Compositional biasi422 – 441Polar residuesSequence analysisAdd BLAST20

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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).UniRule annotation

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the herpesviridae capsid scaffolding protein family.UniRule annotation

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.16.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_04008, HSV_SCAF, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035443, Herpes_virus_sf
IPR001847, Peptidase_S21

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00716, Peptidase_S21, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00236, HSVCAPSIDP40

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

A0A0X9ZXJ2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDAYATDSNV VSLPIYVAGY IALYDMGDGG ELTLTRETVA AALPPASRLP 
        60         70         80         90        100
INIDHRNGCV VGEVLSIVDD VRGPFFLGIV NCPQLGAVLA TAAGPDFFGE 
       110        120        130        140        150
MSEGLSEQER LLYLVSNYLP SASLSSRRLG PDEEPDETLF AHVSLCVIGR 
       160        170        180        190        200
RVGTIVTYDA TPENTVAPFK RLSPSVREEL LITAREAQSR LGDMATWHVS 
       210        220        230        240        250
EDTLTRVLLS TAVNNMLLRN RWNLVARRRR EAGIEGHTYL QASASFGITN 
       260        270        280        290        300
GCNKADFCGA ELVGTCGYKS GERVRDISYS RVTLGAKAFT SSGSSALPSS 
       310        320        330        340        350
DNSAGQIGER AKHPGAMASS NPQTLSAAGA PLVSGDYILV PAAQYNQLVV 
       360        370        380        390        400
GQHTSHPPIN AGQASATHAV PTQYIQPAYN SMVPTSMYQA PPYWSVPPST 
       410        420        430        440        450
NLEAQITALV GALAADRKAA KSSDSQAVQN SQCSPPLSPQ QERRYTRKRR 
       460        470        480        490        500
HDWDANTRDD IEGIYYPGER SPRPVERRAG RASTTIADLM GAVSSLQQEV 
       510        520        530        540        550
SQLRAIQTVT AQQQVAPAGL YKPVPPGVPQ QYSQYQYIHP QHAVSAIISP 
       560        570        580        590        600
QLSGIQAQPP QSVIATPVPA VETPGGAKVC AAPTATHQAV EHSKAVQPQF 
       610        620        630        640 
EAVTSAAVLP VNQPQASSQT VDASASTGLD FGRDDADIFV SQMMSAR
Length:647
Mass (Da):68,977
Last modified:April 13, 2016 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i69F45D5021492831
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
KT324737 Genomic DNA Translation: AMB16074.1
KT324738 Genomic DNA Translation: AMB16153.1
KT324739 Genomic DNA Translation: AMB16232.1
KT324741 Genomic DNA Translation: AMB16390.1
KT324742 Genomic DNA Translation: AMB16469.1
LC075584 Genomic DNA Translation: BAV93321.1
LC075585 Genomic DNA Translation: BAV93400.1
LC075587 Genomic DNA Translation: BAV93558.1
LC075588 Genomic DNA Translation: BAV93637.1

NCBI Reference Sequences

More...RefSeqi		NP_045252.1, NC_001844.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1487600

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:1487600

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KT324737 Genomic DNA Translation: AMB16074.1
KT324738 Genomic DNA Translation: AMB16153.1
KT324739 Genomic DNA Translation: AMB16232.1
KT324741 Genomic DNA Translation: AMB16390.1
KT324742 Genomic DNA Translation: AMB16469.1
LC075584 Genomic DNA Translation: BAV93321.1
LC075585 Genomic DNA Translation: BAV93400.1
LC075587 Genomic DNA Translation: BAV93558.1
LC075588 Genomic DNA Translation: BAV93637.1
RefSeqiNP_045252.1, NC_001844.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Genome annotation databases

GeneIDi1487600
KEGGivg:1487600

Family and domain databases

Gene3Di3.20.16.10, 1 hit
HAMAPiMF_04008, HSV_SCAF, 1 hit
InterProiView protein in InterPro
IPR035443, Herpes_virus_sf
IPR001847, Peptidase_S21
PfamiView protein in Pfam
PF00716, Peptidase_S21, 1 hit
PRINTSiPR00236, HSVCAPSIDP40

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiA0A0X9ZXJ2_9ALPH
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0A0X9ZXJ2
Secondary accession number(s): O39278
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/TrEMBL: April 13, 2016
Last sequence update: April 13, 2016
Last modified: May 25, 2022
This is version 34 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again