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Database: UniProt
Entry: Q785G2_9ALPH
LinkDB: Q785G2_9ALPH
Original site: Q785G2_9ALPH 
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
//
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