CAPSD_BPPAJ
ID CAPSD_BPPAJ Reviewed; 667 AA.
AC P85500; B5WZR9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Capsid polyprotein {ECO:0000303|PubMed:19010363, ECO:0000312|EMBL:BAG74987.1};
DE AltName: Full=ORF3 protein {ECO:0000303|PubMed:19010363};
DE EC=3.4.-.- {ECO:0000269|PubMed:19010363};
DE Contains:
DE RecName: Full=Capsid protein {ECO:0000303|PubMed:19010363};
OS Pseudomonas phage PAJU2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=504346;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 349-362, FUNCTION
RP (CAPSID PROTEIN), AND PROTEOLYTIC CLEAVAGE.
RX PubMed=19010363; DOI=10.1016/j.virusres.2008.10.005;
RA Uchiyama J., Rashel M., Matsumoto T., Sumiyama Y., Wakiguchi H.,
RA Matsuzaki S.;
RT "Characteristics of a novel Pseudomonas aeruginosa bacteriophage, PAJU2,
RT which is genetically related to bacteriophage D3.";
RL Virus Res. 139:131-134(2009).
CC -!- FUNCTION: [Capsid polyprotein]: The C-terminus contains the capsid
CC protein. The N-terminal region may act as a prohead protease.
CC {ECO:0000269|PubMed:19010363}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000269|PubMed:19010363}.
CC -!- PTM: The prohead protease may be autocatalytically cleaved giving rise
CC to the mature capsid protein. {ECO:0000305|PubMed:19010363}.
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DR EMBL; AP009624; BAG74987.1; -; Genomic_DNA.
DR RefSeq; YP_002284337.1; NC_011373.1.
DR GeneID; 6989668; -.
DR KEGG; vg:6989668; -.
DR Proteomes; UP000001041; Genome.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR InterPro; IPR024455; Phage_capsid.
DR InterPro; IPR006433; Prohead_protease.
DR Pfam; PF04586; Peptidase_S78; 1.
DR Pfam; PF05065; Phage_capsid; 1.
DR TIGRFAMs; TIGR01554; major_cap_HK97; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Capsid protein; Direct protein sequencing;
KW Hydrolase; Protease; Reference proteome; T=7 icosahedral capsid protein;
KW Viral capsid assembly; Viral capsid maturation;
KW Viral release from host cell; Virion.
FT CHAIN 1..667
FT /note="Capsid polyprotein"
FT /id="PRO_0000363886"
FT CHAIN 349..667
FT /note="Capsid protein"
FT /evidence="ECO:0000269|PubMed:19010363"
FT /id="PRO_0000326456"
FT REGION 8..154
FT /note="Prohead protease activity"
FT /evidence="ECO:0000305|PubMed:19010363"
FT SITE 348..349
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:19010363"
FT CONFLICT 352
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="W -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 71389 MW; 5FB908548F8D9811 CRC64;
MKTNRAYSTL EVKALDDEKR VITGIASTPS PDRMQDVVEP KGAQFKLPIP FLWQHNHDEP
IGHVTEAKVT QKGIEVSVQL TQVEEPGKLK DRLDEAWQSI KSGLVRGLSI GFSAKEFEQI
PGSWGLRFLS WEWFELSAVT IPANAEATIT SVKSIDREQR AALGIKSVPV VRVTPAGASA
IKTKTIKVPK PQEGNDMKTT AEQIAEFEAT RVTKAAEMEA IMTKAAEAGE TLDAEQSEQF
DTLEAEIAAI DKHIGRLKQM QKAQAANAKP VTEEAGAQRM ANVKALDFKE VQVRAKNTQK
LEPGIAFARA AKCLALGHLE HRDAIGIAKS LYDGQDSIIA ATQRLVTKAA VAAATTSDAT
WAGPLVGDET SVFADFVEYL RPQTILGRFG TNGIPSLRRV PFRVPLIGQT SGGDGYWVGE
GQAKPLTKFD FERKTLEPLK VANIAVATME VIRDSSPSAD VIIRDQLAAA LRERLDIDFI
DPAKAAVAGV SPASILNGVA GIPSSGNTAD DVRADIRALF NAFIAANNAP TSGVWLMPAT
TALALSLMQN PLGQAEFPGI SMTGGTLFGL PVIVSEYIPT ASAGAVVALV NASDIYLGDE
GGVDLSMSTE ASLQMDNAPD NPTTASTVLV SLWQRNLVGF RAERAINWAR RRASAVAYLT
GVNWGAA