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Protein

Capsid scaffolding protein

Gene

17

Organism
Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever virus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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
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

Catalytic activityi

Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei47Charge relay systemUniRule annotation1
Active sitei116Charge relay systemUniRule annotation1
Active sitei137Charge relay systemUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Viral capsid assembly, Virus exit from host cell

Protein family/group databases

MEROPSiS21.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid scaffolding proteinUniRule annotation
Alternative name(s):
Capsid protein 17
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
Gene namesi
Name:17
OrganismiAlcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever virus)
Taxonomic identifieri654901 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeMacavirus
Virus hostiConnochaetes taurinus (Blue wildebeest) [TaxID: 9927]
Proteomesi
  • UP000000941 Componenti: Genome

Subcellular locationi

Capsid scaffolding protein :
  • Host cytoplasm UniRule annotation
Assemblin :
  • Host nucleus UniRule annotation
Assembly protein :
  • Host nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004057081 – 524Capsid scaffolding proteinAdd BLAST524
ChainiPRO_00004057091 – 230AssemblinUniRule annotationAdd BLAST230
ChainiPRO_0000405710231 – 524Assembly proteinUniRule annotationAdd BLAST294

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
Sitei230 – 231Cleavage; by assemblin; Release siteUniRule annotation2
Sitei498 – 499Cleavage; by assemblin; Tail siteBy similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO36367.

Interactioni

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

Structurei

3D structure databases

ProteinModelPortaliO36367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni268 – 287Interaction with pAPUniRule annotationAdd BLAST20
Regioni504 – 524Interaction with major capsid proteinUniRule annotationAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi359 – 365Nuclear localization signalBy similarity7

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

Sequence similaritiesi

Belongs to the herpesviridae capsid scaffolding protein family.UniRule annotation

Family and domain databases

HAMAPiMF_04008. HSV_SCAF. 1 hit.
InterProiIPR001847. Peptidase_S21.
[Graphical view]
PfamiPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSiPR00236. HSVCAPSIDP40.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O36367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRDSLFVAG FVDISTCPKE DPSLNLDAQT WSRYLPLSTS IPLTVEHFSE
60 70 80 90 100
AQVGWVTGLF SVAQGLFCTA VITAGEFLEL LDSLYLECTV AQHSPKADLP
110 120 130 140 150
RNPRAEVLHS WLPELSLSSV HPDLLGTKDE PGQVFHHISL CALGRRRGTV
160 170 180 190 200
AVYGDSLAWV LSRFQSLSRD DVAMIATNAL TPPSQAPEFT VKLGLLFAKA
210 220 230 240 250
IDAGFISNRI STLKLDRQAA GISPATYLKA SAVPQKLETA APLNQPEGAD
260 270 280 290 300
TLIDSTMSGP GAPPAPQDDL IPVPRSAFLN MLESTVSRTH PANGDAPALL
310 320 330 340 350
PFGRYNMVQV PKGLTPYVRP VGFIEPSDQD DYRYPSYTGP RPYDYFAPRQ
360 370 380 390 400
LCRNCCTSRP RKRAREDPED EVSFPGEEST VFRKDLTDLS KSLAELQSEI
410 420 430 440 450
RELKQMQNTP RPYPRPEHHY PAFDPLMYGL RPLPNPDKFP KEFICSDYFT
460 470 480 490 500
KDESASKKPE VVHIPNPEQH VPACAAQPEV KLVEEKDVAP KQPRVVNASF
510 520
QPKAETSKAA TLQKLFCDEM LSKQ
Length:524
Mass (Da):57,930
Last modified:January 1, 1998 - v1
Checksum:iBFA6D3976149177A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005370 Genomic DNA. Translation: AAC58064.1.
PIRiT03112.
RefSeqiNP_065516.1. NC_002531.1.

Genome annotation databases

GeneIDi911752.
KEGGivg:911752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005370 Genomic DNA. Translation: AAC58064.1.
PIRiT03112.
RefSeqiNP_065516.1. NC_002531.1.

3D structure databases

ProteinModelPortaliO36367.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS21.006.

Proteomic databases

PRIDEiO36367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi911752.
KEGGivg:911752.

Family and domain databases

HAMAPiMF_04008. HSV_SCAF. 1 hit.
InterProiIPR001847. Peptidase_S21.
[Graphical view]
PfamiPF00716. Peptidase_S21. 1 hit.
[Graphical view]
PRINTSiPR00236. HSVCAPSIDP40.
ProtoNetiSearch...

Entry informationi

Entry nameiSCAF_ALHV1
AccessioniPrimary (citable) accession number: O36367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.