SCAF_HHV8P
ID SCAF_HHV8P Reviewed; 534 AA.
AC Q2HRB6; D0UZM9; Q2HRB5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=ORF17;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 3-196.
RX PubMed=24977643; DOI=10.1021/bi5003234;
RA Gable J.E., Lee G.M., Jaishankar P., Hearn B.R., Waddling C.A.,
RA Renslo A.R., Craik C.S.;
RT "Broad-spectrum allosteric inhibition of herpesvirus proteases.";
RL Biochemistry 53:4648-4660(2014).
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=Q2HRB6-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein;
CC IsoId=Q2HRB6-2; Sequence=VSP_053272;
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; AF148805; ABD28867.1; -; Genomic_DNA.
DR EMBL; AF148805; ABD28868.1; -; Genomic_DNA.
DR RefSeq; YP_001129369.1; NC_009333.1.
DR RefSeq; YP_001129370.1; NC_009333.1.
DR PDB; 4P2T; X-ray; 2.15 A; A/B=3-196.
DR PDBsum; 4P2T; -.
DR SMR; Q2HRB6; -.
DR BioGRID; 1776981; 5.
DR BioGRID; 1776985; 12.
DR ChEMBL; CHEMBL4296290; -.
DR MEROPS; S21.006; -.
DR PRIDE; Q2HRB6; -.
DR DNASU; 4961478; -.
DR GeneID; 4961478; -.
DR GeneID; 4961482; -.
DR KEGG; vg:4961478; -.
DR KEGG; vg:4961482; -.
DR Proteomes; UP000000942; 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; 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; Reference proteome; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..534
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000423879"
FT CHAIN 1..230
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000435878"
FT CHAIN 231..534
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000435879"
FT REGION 253..272
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 337..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..534
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 336..342
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 338..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 230..231
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 512..513
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..246
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_053272"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4P2T"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4P2T"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:4P2T"
SQ SEQUENCE 534 AA; 57866 MW; EEA75DF8146B0791 CRC64;
MAQGLYVGGF VDVVSCPKLE QELYLDPDQV TDYLPVTEPL PITIEHLPET EVGWTLGLFQ
VSHGIFCTGA ITSPAFLELA SRLADTSHVA RAPVKNLPKE PLLEILHTWL PGLSLSSIHP
RELSQTPSGP VFQHVSLCAL GRRRGTVAVY GHDAEWVVSR FSSVSKSERA HILQHVSSCR
LEDLSTPNFV SPLETLMAKA IDASFIRDRL DLLKTDRGVA SILSPAYLKA SQFPVGIQAV
TPPRPAMNSS GQEDIISIPK SAFLSMLQSS IDGMKTTAAK MSHTLSGPGL MGCGGQMFPT
DHHLPSYVSN PAPPYGYAYK NPYDPWYYSP QLPGYRTGKR KRGAEDDEGH LFPGEEPAYH
KDILSMSKNI AEIQSELKEM KLNGWHAGPP PSSSAAAAAV DPHYRPHANS AAPCQFPTMK
EHGGTYVHPP IYVQAPHGQF QQAAPILFAQ PHVSHPPVST GLAVVGAPPA EPTPASSTQS
IQQQAPETTH TPCAAVEKDA PTPNPTSNRV EASSRSSPKS KIRKMFCEEL LNKQ
