SCAF_SUHVK
ID SCAF_SUHVK Reviewed; 524 AA.
AC Q83417;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 AltName: Full=Virion structural protein UL26;
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=Capsid protein VP24;
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};
DE AltName: Full=Capsid protein VP22A;
OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8806172; DOI=10.1016/0168-1702(96)01293-2;
RA Dezelee S., Bras F., Vende P., Simonet B., Nguyen X., Flamand A.,
RA Masse M.J.;
RT "The BamHI fragment 9 of pseudorabies virus contains genes homologous to
RT the UL24, UL25, UL26, and UL 26.5 genes of herpes simplex virus type 1.";
RL Virus Res. 42:27-39(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=22022263; DOI=10.1371/journal.ppat.1002282;
RA Szpara M.L., Tafuri Y.R., Parsons L., Shamim S.R., Verstrepen K.J.,
RA Legendre M., Enquist L.W.;
RT "A wide extent of inter-strain diversity in virulent and vaccine strains of
RT alphaherpesviruses.";
RL PLoS Pathog. 7:E1002282-E1002282(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=22491460; DOI=10.1128/jvi.00068-12;
RA Grimm K.S., Klupp B.G., Granzow H., Muller F.M., Fuchs W.,
RA Mettenleiter T.C.;
RT "Analysis of viral and cellular factors influencing herpesvirus-induced
RT nuclear envelope breakdown.";
RL J. Virol. 86:6512-6521(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-224.
RX PubMed=26161660; DOI=10.1371/journal.ppat.1005045;
RA Zuehlsdorf M., Werten S., Klupp B.G., Palm G.J., Mettenleiter T.C.,
RA Hinrichs W.;
RT "Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate
RT the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease.";
RL PLoS Pathog. 11:E1005045-E1005045(2015).
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=Q83417-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, UL26.5 protein;
CC IsoId=Q83417-2; Sequence=VSP_057942;
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; JF797218; AEM64057.1; -; Genomic_DNA.
DR EMBL; JQ809328; AFI70810.1; -; Genomic_DNA.
DR EMBL; KJ717942; AID18746.1; -; Genomic_DNA.
DR EMBL; X95710; CAA65015.1; -; Genomic_DNA.
DR RefSeq; YP_068348.1; NC_006151.1.
DR PDB; 4CX8; X-ray; 2.53 A; A/B=1-224.
DR PDB; 4V07; X-ray; 2.10 A; A/B=1-224.
DR PDB; 4V08; X-ray; 2.03 A; A/B=1-224.
DR PDB; 4V0T; X-ray; 2.05 A; A/B=1-224.
DR PDBsum; 4CX8; -.
DR PDBsum; 4V07; -.
DR PDBsum; 4V08; -.
DR PDBsum; 4V0T; -.
DR SASBDB; Q83417; -.
DR SMR; Q83417; -.
DR MEROPS; S21.001; -.
DR GeneID; 2952508; -.
DR KEGG; vg:2952508; -.
DR BRENDA; 3.4.21.97; 5212.
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; 1.
DR PRINTS; PR00236; HSVCAPSIDP40.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Host cytoplasm; Host nucleus;
KW Hydrolase; Phosphoprotein; Protease; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..524
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000434531"
FT CHAIN 1..225
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000434532"
FT CHAIN 226..524
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000434533"
FT REGION 256..275
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..524
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT COMPBIAS 290..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 225..226
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 502..503
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..246
FT /note="Missing (in isoform pAP)"
FT /id="VSP_057942"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:4V08"
FT TURN 83..88
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:4V08"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:4V08"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:4V08"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:4V0T"
SQ SEQUENCE 524 AA; 54645 MW; 6C8210F747315BB0 CRC64;
MGPVYVSGYL ALYDRDGGEL ALTREIVAAA LPPAGPLPIN IDHRPRCDIG AVLAVVDDDR
GPFFLGVVNC PQLGAVLARA VGPDFFGDMR LSDEERLLYL LSNYLPSASL SSRRLAPGEA
PDETLFAHVA LCVIGRRVGT IVVYDASPEA AVAPFRQLSA RARSELLARA AESPDRERVW
HMSEEALTRA LLSTAVNNML LRDRWELVAA RRREAGVRGH TYLQATMWAG LLPKSGASPA
PGPSAAMAAP PSAAPGDYIF VPAAQYNQLV VNQRPAPSLE SQLGAIVSAA MDRRHRRSPS
PEPRPPARKR RYDDYAQDNA YYPGEAPPPA SDLAAVVSSL QREISHLRAQ QLRYPTPYYA
PAAPPQLLPP GAVVGHPHPH HAAGALYPPM YAPQPGLHAP PPSPVAHAVP ALPGLPGLQG
LAAPVAHVPA QVVPQQPVVV QAQPVAVPAA AAAAPAPAPA AAAAAAAPVQ AAAPAAPASA
PQPPVQASVS APADVSAGTI DASSAAVACQ RGADIFVSQM MSQR
