ID A0A1R3T5F5_9ALPH Unreviewed; 621 AA.
AC A0A1R3T5F5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=UL26 {ECO:0000313|EMBL:SCO83555.1};
OS Spheniscid alphaherpesvirus 1.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus spheniscidalpha1.
OX NCBI_TaxID=2560777 {ECO:0000313|EMBL:SCO83555.1};
RN [1] {ECO:0000313|EMBL:SCO83555.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lib01004 {ECO:0000313|EMBL:SCO83555.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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; LT608135; SCO83555.1; -; Genomic_DNA.
DR OrthoDB; 8407at10239; -.
DR Proteomes; UP000203542; Segment.
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:UP000203542};
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..621
FT /note="Capsid scaffolding protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023336240"
FT CHAIN 1..255
FT /note="Assemblin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023336238"
FT CHAIN 256..621
FT /note="Assembly protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT /id="PRO_5023336239"
FT REGION 417..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..621
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT COMPBIAS 417..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
FT SITE 255..256
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04008"
SQ SEQUENCE 621 AA; 68011 MW; 411DA5507BF78C9A CRC64;
MAGQREAIVV EEPYPSNAYT TKLEFQPIYV AGYLALYDMG DGGDLTLTRD VVRAALPPAT
SPLPINIDHK TNCEIGAVLA IVDDERGPFF LGKINCPQLG DVLASAASSE VFGSKSSSLT
DGEKLLYLVT NYLPSASLSS RRLAPGDVPD DTLLSHVALC VIGRRVGTIV TYDLTASSVV
EPFKFLSKQS RDEILREAQI TDDMLAGRMW SPGEEVLARA LLATAVNNML LRDRWEVVSR
RRKQAGISGH TYLQASAKFG FGWNNDVLTE QKKEVREGLS ENAAFQEHLK KLTDDTERAI
DKSDISKHRS NSFTCADMST PPPPPSRVQG DGDYMWVPCS QYNQLLNGAG VARPQSTVGS
TTPLIQQPYM QPMQYVGAVP QMQSMYGYVP NASWGSSPLE TQLAAFLCAM AADRRASSNQ
TSTQPPVQQH NYQQTPAVSL ERRSCRKRRA DWDLYEDDHD ETYFPGEMRD SRQVAGTKTQ
PDNLAGQSTA RAVGAISGLI EAVSSLQQEI GQLRNIHNQQ AQLPTQQMIW TPPAAQPAYL
PQPMQVPVVQ ANVKPAQSQI QEPVQNKDDQ QVAVVAAQSA ATQPSSSSTT TVDASLVTGL
DRDRGRRDDA DIFVTQMMSQ R
//
