SCAF_BHV1C
ID SCAF_BHV1C Reviewed; 621 AA.
AC P54817; Q89855;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid protein P40;
DE AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
DE Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assemblin {ECO:0000255|HAMAP-Rule:MF_04008};
DE EC=3.4.21.97 {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04008};
DE Contains:
DE RecName: Full=Assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Capsid assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
GN Name=UL26;
OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7474173; DOI=10.1128/jvi.69.11.7375-7379.1995;
RA Haanes E.J., Thomsen D.R., Martin S., Homa F.L., Lowery D.E.;
RT "The bovine herpesvirus 1 maturational proteinase and scaffold proteins can
RT substitute for the homologous herpes simplex virus type 1 proteins in the
RT formation of hybrid type B capsids.";
RL J. Virol. 69:7375-7379(1995).
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:0000255|HAMAP-
CC Rule:MF_04008}.
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:0000255|HAMAP-Rule:MF_04008}.
CC -!- FUNCTION: [Assembly protein]: Plays a major role in capsid assembly.
CC Acts as a scaffold protein by binding major capsid protein.
CC Multimerizes in the nucleus such as major capsid protein forms the
CC icosahedral T=16 capsid. Cleaved by assemblin after capsid completion.
CC The cleavages products are evicted from the capsid before or during DNA
CC packaging. {ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_04008};
CC -!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts with
CC major capsid protein. Assemblin exists in a monomer-dimer equilibrium
CC with the dimer being the active species. Assembly protein
CC homomultimerizes and interacts with major capsid protein.
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-
CC Rule:MF_04008}.
CC -!- SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04008}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Capsid scaffolding protein; Synonyms=pPR, UL26;
CC IsoId=P54817-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, UL26.5;
CC IsoId=P54817-2; Sequence=VSP_018864;
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:0000255|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:0000255|HAMAP-Rule:MF_04008}.
CC -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04008}.
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DR EMBL; U31809; AAA91999.1; -; Genomic_DNA.
DR EMBL; U31809; AAA92000.1; -; Genomic_DNA.
DR EMBL; Z78205; CAB01599.1; -; Genomic_DNA.
DR EMBL; AJ004801; CAA06107.1; -; Genomic_DNA.
DR RefSeq; NP_045332.1; NC_001847.1.
DR SMR; P54817; -.
DR MEROPS; S21.001; -.
DR GeneID; 4783434; -.
DR KEGG; vg:4783434; -.
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:0016032; P:viral process; IMP:AgBase.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.16.10; -; 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.
PE 3: Inferred from homology;
KW Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
KW Phosphoprotein; Protease; Serine protease; Viral capsid assembly;
KW Viral release from host cell.
FT CHAIN 1..621
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000027249"
FT CHAIN 1..254
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027250"
FT CHAIN 255..621
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027251"
FT REGION 258..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 420..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..621
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 439..442
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 299..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 254..255
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 596..597
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT VAR_SEQ 1..313
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_018864"
SQ SEQUENCE 621 AA; 63712 MW; AEF6D7C9BDE69003 CRC64;
MADAPDGGSA DARVDAEPSA LARASMPVYV GGYLALYGMG DEGELVLTRE QVARALPPAA
PLPINIDHAS ACEVGAVLAL ADDDAGLFFV GVINCPQLAD TLAGVAHPAF FGADAPSLTP
RERFLYLVSN YLPSVSLSSR RLAPDEEADG TLFAHVALCV LGRRVGTIVT YDATPDACVA
PFRRLSPRAR AALLANAEAA RAALGDRAWP VPREALAQTL LSTAVNNMLV RDKWDTVSRR
RREAGIAGHT YLQASAVFPL PTGGEGPERT GGRERAQKSA VAGGVCIALP VAGGRARQPE
LPPAPPPPPP PPAMSAAHQA GAASAHPLPA GDYVYVPTAQ YNQLVVSQAR GAAMTAAPPP
APYFLPAAAA AAAAPPPMPG WYGAAGAAPW HPGYGFPPPG LESQIMALAG AIADGRRVQA
HGADGSGYDG PLDRRPLAKR RRYNWDHPRG RSGGGDDDEA YYPGEGAPAE LPPHHHSPPP
PHPPPSHALS KLASAVSSLQ QEVSQLRAGY PYGPAFAAAQ HPPAAHLPCL PQQYTAPPRV
GAGPAQVPTL APAQAPAQAL SVPAVAAAPA TVAAAAAVGP PEEPGVAATV DASAMASLPP
AQPPQACDPA EIFVAQMMRQ R
