ID A0A1P8VIX4_9BETA Unreviewed; 536 AA.
AC A0A1P8VIX4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Capsid scaffolding protein {ECO:0000256|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease precursor {ECO:0000256|HAMAP-Rule:MF_04008};
DE Short=pPR {ECO:0000256|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assemblin {ECO:0000256|HAMAP-Rule:MF_04008};
DE EC=3.4.21.97 {ECO:0000256|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease {ECO:0000256|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
GN Name=ORF67 {ECO:0000313|EMBL:APZ76282.1};
GN ORFNames=MRV_0071 {ECO:0000313|EMBL:APZ76282.1};
OS Murine roseolovirus.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=1940555 {ECO:0000313|EMBL:APZ76282.1};
RN [1] {ECO:0000313|EMBL:APZ76282.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOK1 {ECO:0000313|EMBL:APZ76282.1};
RA Patel S.J., Zhao G., Penna V.R., Park E., Lauron E.J., Harvey I.B.,
RA Beatty W.L., Plougastel-Douglas B., Poursine-Laurent J., Fremont D.H.,
RA Wang D., Yokoyama W.M.;
RT "A murine herpesvirus closely related to ubiquitous human herpesviruses
RT causes T-cell depletion.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Assemblin: Protease that plays an essential role in virion
CC assembly within the nucleus. Catalyzes the cleavage of the assembly
CC protein after formation of the spherical procapsid. By that cleavage,
CC the capsid matures and gains its icosahedral shape. The cleavage sites
CC seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds.
CC Assemblin and cleavages products are evicted from the capsid before or
CC during DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- FUNCTION: Assembly protein: Plays a major role in capsid assembly. Acts
CC as a scaffold protein by binding major capsid protein. Multimerizes in
CC the nucleus such as major capsid protein forms the icosahedral T=16
CC capsid. Cleaved by assemblin after capsid completion. The cleavages
CC products are evicted from the capsid before or during DNA packaging.
CC {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- FUNCTION: Capsid scaffolding protein: Acts as a scaffold protein by
CC binding major capsid protein in the cytoplasm, inducing the nuclear
CC localization of both proteins. Multimerizes in the nucleus such as
CC major capsid protein forms the icosahedral T=16 capsid. Autocatalytic
CC cleavage releases the assembly protein, and subsequently abolishes
CC interaction with major capsid protein. Cleavages products are evicted
CC from the capsid before or during DNA packaging. {ECO:0000256|HAMAP-
CC Rule:MF_04008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold
CC protein.; EC=3.4.21.97; Evidence={ECO:0000256|HAMAP-Rule:MF_04008};
CC -!- SUBUNIT: [Assemblin]: Exists in a monomer-dimer equilibrium with the
CC dimer being the active species. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SUBUNIT: [Assembly protein]: Homomultimer. Interacts with major capsid
CC protein. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SUBUNIT: [Capsid scaffolding protein]: Homomultimer. Interacts with
CC major capsid protein. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus
CC {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000256|HAMAP-
CC Rule:MF_04008}.
CC -!- DOMAIN: Region of interaction between pPR and pAP is called Amino
CC conserved domain (ACD). The region of interaction with major capsid
CC protein is called carboxyl conserved domain (CCD). {ECO:0000256|HAMAP-
CC Rule:MF_04008}.
CC -!- PTM: Capsid scaffolding protein is cleaved by assemblin after formation
CC of the spherical procapsid. As a result, the capsid obtains its mature,
CC icosahedral shape. Cleavages occur at two or more sites: release and
CC tail site. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC family. {ECO:0000256|HAMAP-Rule:MF_04008}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04008}.
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DR EMBL; KY355735; APZ76282.1; -; Genomic_DNA.
DR RefSeq; YP_009344898.1; NC_033620.1.
DR GeneID; 30999408; -.
DR KEGG; vg:30999408; -.
DR OrthoDB; 9131at10239; -.
DR Proteomes; UP000202182; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.16.10; Herpesvirus/Caudovirus protease domain; 1.
DR HAMAP; MF_04008; HSV_SCAF; 1.
DR InterPro; IPR035443; Herpes_virus_sf.
DR InterPro; IPR001847; Peptidase_S21.
DR Pfam; PF00716; Peptidase_S21; 1.
DR PRINTS; PR00236; HSVCAPSIDP40.
DR SUPFAM; SSF50789; Herpes virus serine proteinase, assemblin; 1.
PE 3: Inferred from homology;
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200, ECO:0000256|HAMAP-
KW Rule:MF_04008}; Host nucleus {ECO:0000256|HAMAP-Rule:MF_04008};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04008};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04008};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_04008};
KW Reference proteome {ECO:0000313|Proteomes:UP000202182};
KW Serine protease {ECO:0000256|HAMAP-Rule:MF_04008};
KW Viral capsid assembly {ECO:0000256|ARBA:ARBA00022950, ECO:0000256|HAMAP-
KW Rule:MF_04008};
KW Viral release from host cell {ECO:0000256|ARBA:ARBA00022612,
KW ECO:0000256|HAMAP-Rule:MF_04008}.
FT CHAIN 1..536
FT /note="Capsid scaffolding protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023304779"
FT CHAIN 1..226
FT /note="Assemblin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023304778"
FT CHAIN 227..536
FT /note="Assembly protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023304777"
FT REGION 423..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..536
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT SITE 226..227
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
SQ SEQUENCE 536 AA; 60999 MW; 6E0DF9AA7A6AFB23 CRC64;
MDPSTIYVGG FVYVYGKDRD ELYIPKDVIH KFIASGDAVS IPLNINHNDL ATIGYILNLF
DLKNGLFCIG KIDSSKFITI MSDISKKSQL IALGPNNSLR PNPLLECLSA FFPAFSLSSK
NLNNIDDINF FKHVSICGIG KRCGTVCVYG ETIRWIVDKF NIIDESEKDR VLNVKDSGRK
YDFNFDINLY DLLANTLDTS YIKDRLSKLR LDKKISGLSD TTYIKASKVL DFDNSMSESE
IDKKEHETNE ETTCIDKDKS AGVDNTIKST EKLTVEPLPI LENTSKVDIL IDIPKKTETN
TSISTSTVNT GLKEMSQTPI NSNQPGLLND GIYIPKDMFM SLLNMNNNYP NSHIAYNKPQ
IMDNYYGSQG MEFINRPMNG YVPSRYGNPY IDQNMHYGVP EYNRYDRHDY KYYQKMKRRY
ESDSDDDMAF PGDPDYIRKK QKRYDPTSSK SINREILDTL GSIKREIGNL RSTREHDIQN
TAQLMETENV DSSSKPHASK PIINASMTPT DSLSQNKNML NINKKLFVNA MKKLDI
//
