SCAF_SCMVC
ID SCAF_SCMVC Reviewed; 589 AA.
AC P16046;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 110.
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=UL80; Synonyms=APNG;
OS Simian cytomegalovirus (strain Colburn).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=50292;
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1649317; DOI=10.1128/jvi.65.8.4091-4100.1991;
RA Welch A.R., McNally L.M., Gibson W.;
RT "Cytomegalovirus assembly protein nested gene family: four 3'-coterminal
RT transcripts encode four in-frame, overlapping proteins.";
RL J. Virol. 65:4091-4100(1991).
RN [2]
RP SEQUENCE REVISION TO 501.
RA Brignole E., Gibson W.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF ISOFORM PAP.
RX PubMed=2536099; DOI=10.1128/jvi.63.2.669-676.1989;
RA Robson L., Gibson W.;
RT "Primate cytomegalovirus assembly protein: genome location and nucleotide
RT sequence.";
RL J. Virol. 63:669-676(1989).
RN [4]
RP CHARACTERIZATION OF ASSEMBLIN.
RX PubMed=1961747; DOI=10.1073/pnas.88.23.10792;
RA Welch A.R., Woods A.S., McNally L.M., Cotter R.J., Gibson W.;
RT "A herpesvirus maturational proteinase, assemblin: identification of its
RT gene, putative active site domain, and cleavage site.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10792-10796(1991).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9733808; DOI=10.1128/jvi.72.10.7722-7732.1998;
RA Plafker S.M., Gibson W.;
RT "Cytomegalovirus assembly protein precursor and proteinase precursor
RT contain two nuclear localization signals that mediate their own nuclear
RT translocation and that of the major capsid protein.";
RL J. Virol. 72:7722-7732(1998).
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=4;
CC Name=Capsid scaffolding protein; Synonyms=pPR;
CC IsoId=P16046-1; Sequence=Displayed;
CC Name=APNG.7 protein;
CC IsoId=P16046-2; Sequence=VSP_037428;
CC Name=pAP; Synonyms=Assembly protein, APGN.5 protein;
CC IsoId=P16046-3; Sequence=VSP_037427;
CC Name=APNG.4 protein;
CC IsoId=P16046-4; Sequence=VSP_037426;
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; M64627; AAA46065.2; -; Genomic_DNA.
DR EMBL; M24205; AAA85777.1; -; mRNA.
DR PIR; A40414; WMBECB.
DR SMR; P16046; -.
DR PRIDE; P16046; -.
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 1: Evidence at protein level;
KW Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
KW Phosphoprotein; Protease; Serine protease; Viral capsid assembly;
KW Viral release from host cell.
FT CHAIN 1..589
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000027289"
FT CHAIN 1..249
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027290"
FT CHAIN 250..589
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027292"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..326
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 421..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 428..433
FT /note="Nuclear localization signal 1"
FT MOTIF 453..459
FT /note="Nuclear localization signal 2"
FT COMPBIAS 425..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 249..250
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 556..557
FT /note="Cleavage; by assemblin; Tail site"
FT VAR_SEQ 1..348
FT /note="Missing (in isoform APNG.4 protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_037426"
FT VAR_SEQ 1..280
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_037427"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform APNG.7 protein)"
FT /evidence="ECO:0000305"
FT /id="VSP_037428"
FT CONFLICT 501
FT /note="A -> R (in Ref. 3; AAA85777)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="A -> AS (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 63715 MW; 247CBB9DCC4E5A23 CRC64;
MADPVYVGGF LVRYDEPPGE AELFLPSGVV DRWLRDCRGP LPLNVNHDES ATVGYVAGLQ
NVRAGLFCLG RVTSPKFLDI VQKASEKSEL VSRGPPSESS LRPDGVLEFL SGSYSGLSLS
SRRDINAADG AAGDAETACF KHVALCSVGR RRGTLAVYGR QPDWVMERFP DLTEADREAL
RNQLSGSGEV AAKESAESSA AAAVDPFQSD SYGLLGNSVD ALYIQERLPK LRYDKRLVGV
TARESYVKAS VSPAEQETCD IKVEKERPKE PEQSHVPTES MSHPMSAVAT PAASTVAPSQ
APLALAHDGV YLPKDAFFSL IGASRPLAEA AGARAAYPAV PPPPAYPVMN YEDPSSRHFD
YSAWLRRPAY DAVPPLPPPP VMPMPYRRRD PMMEEAERAA WERGYAPSAY DHYVNNGSWS
RSRSGALKRR RERDASSDEE EDMSFPGEAD HGKARKRLKA HHGRDNNNSG SDAKGDRYDD
IREALQELKR EMLAVRQIAP AALLAPAQLA TPVASPTTTT SHQAEASEPQ ASTAAAAPST
ASSHGSKSAE RGVVNASCRV APPLEAVNPP KDMVDLNRRL FVAALNKME
