ID H2A2B1_MUHV1 Unreviewed; 700 AA.
AC H2A2B1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=M80 {ECO:0000313|EMBL:CCE57080.1};
OS Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Muromegalovirus;
OC Muromegalovirus muridbeta1.
OX NCBI_TaxID=10366 {ECO:0000313|EMBL:CCE57080.1, ECO:0000313|Proteomes:UP000122533};
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1] {ECO:0000313|EMBL:CCE57080.1, ECO:0000313|Proteomes:UP000122533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1 {ECO:0000313|EMBL:CCE57080.1};
RX PubMed=23107009; DOI=10.1016/j.virol.2012.08.041;
RA Smith L.M., McWhorter A.R., Shellam G.R., Redwood A.J.;
RT "The genome of murine cytomegalovirus is shaped by purifying selection and
RT extensive recombination.";
RL Virology 435:258-268(2013).
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; HE610454; CCE57080.1; -; Genomic_DNA.
DR IntAct; H2A2B1; 1.
DR MINT; H2A2B1; -.
DR MEROPS; S21.002; -.
DR Proteomes; UP000122533; 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; 2.
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 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..700
FT /note="Capsid scaffolding protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023516028"
FT CHAIN 1..271
FT /note="Assemblin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023516029"
FT CHAIN 272..700
FT /note="Assembly protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023516027"
FT REGION 143..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..700
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT COMPBIAS 272..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT SITE 271..272
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
SQ SEQUENCE 700 AA; 74244 MW; E77F4B744A6223BC CRC64;
MTGDAARAPD AGSMIYVGGF LTLYDEDPQD ERLRLPRDVV ARELRRAAAG GPAVPLNINH
DESSTVGTVR LFDAEAGLFC LGRLSSPAFL GIVEKAAGKS KLVARGPAKG LEADPVVEYL
SAGFPALSLS SFSPDAVAAA AAAAAADTSE NPGEEAEGQP RRQTTDSGGF FRHVSLCGLG
RRRGTLAVYG RDRDWIVGRF AALTPDERAE IARVDDAALG GWDGDADPFG SDSYGLLAST
VDDGYIAERL CRLRYDKRLL GLQSKETYVK ASELPAEADD GPEPQSIRRD ASRDSEERAA
GREEMAQSSH GLTPAAVSVP GTANPAASAF PADCVYLSRD ALMSILAAAA KQNAVPGALT
SPQQALPQVP SYYGMPPDGV QYHLPPPPPP PPSHHRGGGG TFDPPLPHGG YGPPYHHPDA
YRGGYHHPDR DPRGGVPYEG WYRPRYDPAG DDHPSYNNRR GDRYRADRPP QQQPLYRGER
NRRRSPPDSD DDDDDDDEDL EAGERTGGKR TRQRGSADSG RKRRRRGAAP DDDGGDLSLP
GERGYPKRTA GDHHQSAPPA SRTDEFGEVR ATLNEIRKDI SQIRAAARAE GNGAREDAAS
VGSSDQKCAA PPPGATEMMA SEPPAGGTVV ARMALDPAVA AATGHTAGLL TAGKLVNASC
EPTPMEVGEP SGGGTSRKGG EASMLEVNKR MFVSLLNKME
//
