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VPM_BPP2
ID   VPM_BPP2                Reviewed;         247 AA.
AC   P25476;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-JUN-2021, entry version 75.
DE   RecName: Full=Terminase, endonuclease subunit;
DE   AltName: Full=GpM;
GN   Name=M;
OS   Escherichia phage P2 (Bacteriophage P2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Peduovirinae; Peduovirus.
OX   NCBI_TaxID=10679;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1837355; DOI=10.1093/nar/19.25.7207;
RA   Linderoth N.A., Ziermann R., Haggaard-Ljungquist E., Christie G.E.,
RA   Calendar R.;
RT   "Nucleotide sequence of the DNA packaging and capsid synthesis genes of
RT   bacteriophage P2.";
RL   Nucleic Acids Res. 19:7207-7214(1991).
CC   -!- FUNCTION: M protein is probably an endonuclease which directs cos
CC       cleavage. The Q, P and M proteins are needed to package DNA into
CC       proheads and for the conversion of proheads to capsids.
CC   -!- SIMILARITY: To phage HP1 protein ORF19. {ECO:0000305}.
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DR   EMBL; AF063097; AAD03272.1; -; Genomic_DNA.
DR   PIR; S22800; S22800.
DR   RefSeq; NP_046761.1; NC_001895.1.
DR   SMR; P25476; -.
DR   GeneID; 1261513; -.
DR   KEGG; vg:1261513; -.
DR   Proteomes; UP000009092; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
DR   InterPro; IPR010270; Phage_P2_GpM.
DR   Pfam; PF05944; Phage_term_smal; 1.
PE   4: Predicted;
KW   DNA-binding; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..247
FT                   /note="Terminase, endonuclease subunit"
FT                   /id="PRO_0000165256"
FT   DNA_BIND        214..245
FT                   /evidence="ECO:0000255"
FT   REGION          209..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..247
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  27439 MW;  D5B6AE3A39C3CB9F CRC64;
     MTSPAQRHMM RVSAAMTAQR EAAPLRHATV YEQMLVKLAA DQRTLKAIYS KELKAAKKRE
     LLPFWLPWVN GVLELGKGAQ DDILMTVMLW RLDTGDIAGA LEIARYALKY GLTMPGKHRR
     TPPYMFTEEV ALAAMRAHAA GESVDTRLLT ETLELTATAD MPDEVRAKLH KITGLFLRDG
     GDAAGALAHL QRATQLDCQA GVKKEIERLE RELKPKPEPQ PKAATRAPRK TRSVTPAKRG
     RPKKKAS
 
 
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