SCAF_HHV6U
ID SCAF_HHV6U Reviewed; 528 AA.
AC P24433;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=U53; Synonyms=0R, XKRF1;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-528.
RX PubMed=2152817; DOI=10.1128/jvi.64.1.287-299.1990;
RA Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA Barrell B.G.;
RT "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL J. Virol. 64:287-299(1990).
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=P24433-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein;
CC IsoId=P24433-2; Sequence=VSP_037418;
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; X83413; CAA58387.1; -; Genomic_DNA.
DR EMBL; M68963; AAA65563.1; -; Genomic_DNA.
DR RefSeq; NP_042946.1; NC_001664.2.
DR SMR; P24433; -.
DR BindingDB; P24433; -.
DR ChEMBL; CHEMBL4010; -.
DR MEROPS; S21.004; -.
DR PRIDE; P24433; -.
DR DNASU; 1487933; -.
DR GeneID; 1487933; -.
DR KEGG; vg:1487933; -.
DR Proteomes; UP000009295; 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:0039708; P:nuclear capsid assembly; IDA:UniProtKB.
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 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..528
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000376801"
FT CHAIN 1..230
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027265"
FT CHAIN 231..528
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027266"
FT REGION 270..288
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 394..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..528
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 416..422
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 135
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 491..492
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_037418"
SQ SEQUENCE 528 AA; 58636 MW; 3C043B8224D285CB CRC64;
MSKVWVGGFL CVYGEEPSEE CLALPRDTVQ KELGSGNIPL PLNINHNEKA TIGMVRGLFD
LEHGLFCVAQ IQSQTFMDII RNIAGKSKLI TAGSVIEPLP PDPEIECLSS SFPGLSLSSK
VLQDENLDGK PFFHHVSVCG VGRRPGTIAI FGREISWILD RFSCISESEK RQVLEGVNVY
SQGFDENLFS ADLYDLLADS LDTSYIRKRF PKLQLDKQLC GLSKCTYIKA SEPPVEIIVA
ATKVAGDQVQ LTTEPGSELA VETCDVPVVH GNYDAVESAT ATTAMSNQNL PNTTPLLSSP
PFSDCVFLPK DAFFSLLNVT TGQQPKIVPP VSVHPPVTEQ YQMLPYSESA AKIAEHESNR
YHSPCQAMYP YWQYSPVPQY PAALHGYRQS KTLKKRHFQS DSEDELSFPG DPEYTKKRRR
HRVDNDDDKE MAREKNDLRE LVDMIGMLRQ EISALKHVRA QSPQRHIVPM ETLPTIEEKG
AASPKPSILN ASLAPETVNR SLAGQNESTD LLKLNKKLFV DALNKMDS
