VGA_BPAL3
ID VGA_BPAL3 Reviewed; 494 AA.
AC P25243;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=A protein;
DE AltName: Full=GPA;
GN Name=A;
OS Escherichia phage alpha3 (Bacteriophage alpha-3).
OC Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX NCBI_TaxID=10849;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1532908; DOI=10.1016/0167-4781(92)90440-b;
RA Kodaira K., Nakano K., Okada S., Taketo A.;
RT "Nucleotide sequence of the genome of the bacteriophage alpha 3:
RT interrelationship of the genome structure and the gene products with those
RT of the phages, phi X174, G4 and phi K.";
RL Biochim. Biophys. Acta 1130:277-288(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-257.
RX PubMed=2785817; DOI=10.1016/0167-4781(89)90180-2;
RA Kodaira K., Miyata T., Suzuki K., Nakano K., Taketo A.;
RT "Possible finger structure in gene A protein of Microviridae.";
RL Biochim. Biophys. Acta 1008:123-124(1989).
CC -!- FUNCTION: The A protein is a specific endonuclease that cleaves the
CC viral strand of supertwisted, closed circular DNA at a unique site in
CC the A gene. The A protein also causes relaxation of supertwisted DNA
CC and forms a complex with viral DNA that has a discontinuity in gene A
CC of the viral strand.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X60322; CAA42874.1; -; Genomic_DNA.
DR EMBL; X12611; CAA31130.1; -; Genomic_DNA.
DR PIR; S22324; S22324.
DR RefSeq; NP_039590.1; NC_001330.1.
DR GeneID; 1260690; -.
DR KEGG; vg:1260690; -.
DR Proteomes; UP000002137; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR InterPro; IPR008766; Replication_gene_A.
DR Pfam; PF05840; Phage_GPA; 1.
PE 4: Predicted;
KW DNA replication; DNA-binding; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Reference proteome; Viral DNA replication; Zinc; Zinc-finger.
FT CHAIN 1..494
FT /note="A protein"
FT /id="PRO_0000164865"
FT ZN_FING 230..252
FT /evidence="ECO:0000255"
FT ACT_SITE 327
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 331
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 494 AA; 57368 MW; 002FCD85A4C11699 CRC64;
MATEIFSDVV KSVWSHATAK HAHLRMAVQV DNRSRLLSDL VYQLEKRLSE ETHLDDETLA
IYESQTALLE DHMALVRKCA AQLDNSNTID HRTPLDAECV FLFEMICPGV RYGKTLNSLW
TKYVVQWPEK LIRQELDMVK PLSFKDEVAK YMEKMQEKTR KNRMTQKVIN EMRIAHQKGW
FFVFDTLTLA DDRLQAFNEN PNALRDYFRT VGRAVLRAEG RSVKDSYNDC YRYLCVPEFG
GQHGRLHWHV VHMVRTLPLG SHDPNFGRKV RNYRQINSFR GMWPYGFTQP IAVRYQHDAY
SRKGWLWPVD KTGKAMQSKP YQAVAWYVTK YVAKQSDQRQ KAITERQKKC KNPLMAICLK
KEFRVRSSRK LGMELPSMAH LSNKVLLELS RISFDSSPLY QIVKENAKKQ LTLNIGALPL
HVILDVRPEV RSMLKTIRRL MKKTPEFNWQ SSIASMTVTL KNGDISDEAR QYIIDAGITP
TDLRAKATQT FGGK