ID Q785G2_9ALPH Unreviewed; 639 AA.
AC Q785G2; Q782R9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=ORF 33 {ECO:0000313|EMBL:BAA82921.1};
OS Marek's disease virus serotype 2 MDV2.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus gallidalpha3; Gallid alphaherpesvirus 3.
OX NCBI_TaxID=36353 {ECO:0000313|EMBL:BAA82921.1, ECO:0000313|Proteomes:UP000133659};
RN [1] {ECO:0000313|EMBL:BAA82921.1, ECO:0000313|Proteomes:UP000133659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPRS24 {ECO:0000313|EMBL:BAA82921.1};
RA Jang H., Cai J., Izumiya Y., Murakami Y., Mochizuki M., Song C., Lee Y.,
RA Kai C., Takahashi E., Mikami T.;
RT "The complete DNA sequence and transcription map of the unique long genome
RT region of Marek's disease virus type 2.";
RL Submitted (FEB-1999) 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; AB024414; BAA82921.1; -; Genomic_DNA.
DR MEROPS; S21.001; -.
DR Proteomes; UP000133659; 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:UP000133659};
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..639
FT /note="Capsid scaffolding protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023462799"
FT CHAIN 1..235
FT /note="Assemblin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023462795"
FT CHAIN 236..639
FT /note="Assembly protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023462797"
FT REGION 432..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..639
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT COMPBIAS 432..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 50
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT SITE 235..236
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
SQ SEQUENCE 639 AA; 69394 MW; E17B08849EA58600 CRC64;
MNPTEKYSSV YVAGYLFLYG ADDGSELHID REDIRAAIPT PAPLPINIDH IRNCTVGAVL
ALTDDEHGLF FLGKINCPVM IRTLETAASQ EIFSEFDNLK TEERVLYLIT NYLPSVSLSS
KRLEPGEKAD KSFLAHVALC LLGKRIGTIV TYDLTPENAI EPFRKLSPTT KTALLSEGQE
TERLLGDKVW HPSKEAMSTA LLGTALNNML LRDRWRTISS RRRMAGISGQ KYLQASAWTA
LAESMTSNNA STIHPIGETA NSDGIQKDDR IEVCATSPQT NKTLESRAFS GGSGFAGTHA
ISPPPQMSAQ SPTEMSMNTK SHFPPGDDFI WVPMKSYNEL VSRQATHAIN APEAAVGSQA
PYSSSPLMIP AHLGQHAHIG GYGHASNPQF ASGAINYMGG FPYALPIHPV PTGQSSLETK
LSALLDCMTR EKKSVDGDRG RDDMFSGQEE RGRRGRKRPY NCDKSPEQEP YYPGEFQQSE
HRNLRCEDGI EYGRDATQTR PALAGLVNAV TSLQKEVERL NGRAQAHSIP AVQHMQGMGT
GFQAPVYYAY PPLPIPHVFS RPPEDGRPIS SGEGRASLGS ATGTPPSGSV PPNASQERVD
AAPKSDTVQS QDTVNASTIA NVHRADDAGA DIFIKQMMA
//