SCAF_PSHV1
ID SCAF_PSHV1 Reviewed; 726 AA.
AC Q6UDK6; Q6UDK5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 65.
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 Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
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;
CC IsoId=Q6UDK6-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein;
CC IsoId=Q6UDK6-2; Sequence=VSP_040857;
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}.
CC -!- CAUTION: The sequence corresponding to the ORFs UL26 and UL26.5 have
CC been constructed manually and may not be correct. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ73704.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAQ73705.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY372243; AAQ73704.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY372243; AAQ73705.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_944398.1; NC_005264.1.
DR RefSeq; NP_944399.1; NC_005264.1.
DR SMR; Q6UDK6; -.
DR MEROPS; S21.001; -.
DR PRIDE; Q6UDK6; -.
DR GeneID; 2656956; -.
DR GeneID; 2656997; -.
DR KEGG; vg:2656956; -.
DR KEGG; vg:2656997; -.
DR Proteomes; UP000006840; 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; -; 1.
DR HAMAP; MF_04008; HSV_SCAF; 1.
DR InterPro; IPR035443; Herpes_virus_sf.
DR InterPro; IPR001847; Peptidase_S21.
DR Pfam; PF00716; Peptidase_S21; 2.
DR PRINTS; PR00236; HSVCAPSIDP40.
PE 3: Inferred from homology;
KW Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
KW Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..726
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000406804"
FT CHAIN 1..257
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000406805"
FT CHAIN 258..726
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000406806"
FT REGION 321..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..384
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 385..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..726
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT COMPBIAS 397..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 257..258
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 697..698
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..341
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_040857"
FT UNSURE 471..497
SQ SEQUENCE 726 AA; 77135 MW; A8B7879C2A7A6830 CRC64;
MVVAEQLEDV FVGGYLVIYA SQDGAGEEYR LPKEVVARAL PVEPGRVPVN INHDASCRVG
SVISIVDVEK GLFFLGVVSG SLALAMFKYV ARDLFRADDG DSPGGGAESE TRSDEALPAN
TLSEREKFLY LLSNVLPSLS LSSARLADGY SPADDFFAHV ALCELGKRDG TIAIYGSSPP
EVLDAFSGLD DAAKRELARS AEEWTTSSRR EEPVDEAMVS ECLLRKFMNN AFLMDRGEYL
RARRHLADVR RPKYLQAAET TCLSSANPRS SGKAAFSCEA RGLDEAGAGA IGRAPESGMA
ASADQHAQDG IKIRLERSRS QIGPGAMSSV SQPAAAPYSG AMADSAAQVP SAQPPRIPCP
PTGQTEMIYV PLGTYNDLVV SAAQARRGED RRQQLSAPPP QHAQQIVQRE TGINSSSPAL
APAGRGSYAS ASHIMHQPAF QTQQPCWPQQ QQYVQAPCGG HGIGYYGQAV SRRGGSSGDG
APTTRSTGAP GAGGLSMFGM QHAGPQTHFT APLHGLPTGF PAHGSFLHAP GYLGAMPPIQ
VYAPQPQQHP PSLDTRIEAL LAALEKERAS EQGAAEGPQQ SLVAGQNKKK ALLKRSMEHQ
REEEEDDESA PEAPYFPGEA AASCKRQAKR QRAAAEGEEQ VAPSFSDLIQ GLAALHKDVA
EMKASVAGIG APQASQPTPV AQPEHEEPKQ APATVDASSS KKLKDSRRAA EKRRAADEFA
RIMSTE
