ID   REP_SPV4                Reviewed;         320 AA.
AC   P11334;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Replication-associated protein ORF2;
DE            EC=3.1.21.-;
DE            EC=6.5.1.1;
DE   AltName: Full=Rep;
GN   ORFNames=ORF2;
OS   Spiroplasma virus 4 (SpV4).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Gokushovirinae; Spiromicrovirus.
OX   NCBI_TaxID=10855;
OH   NCBI_TaxID=2134; Spiroplasma melliferum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2822658; DOI=10.1128/jb.169.11.4950-4961.1987;
RA   Renaudin J., Pascarel M.-C., Bove J.-M.;
RT   "Spiroplasma virus 4: nucleotide sequence of the viral DNA, regulatory
RT   signals, and proposed genome organization.";
RL   J. Bacteriol. 169:4950-4961(1987).
CC   -!- FUNCTION: Plays an essential role in viral DNA replication. Binds the
CC       origin of replication and cleaves the dsDNA replicative form I (RFI)
CC       and becomes covalently bound to it via phosphotyrosine bond, generating
CC       the dsDNA replicative form II (RFII). In turn, viral DNA replication
CC       initiates at the 3'-OH of the cleavage site. After one round of rolling
CC       circle synthesis, protein ORF2 is linked to the newly synthesized ssDNA
CC       and joins the ends of the displaced strand to generate a circular
CC       single-stranded molecule ready to be packed into a virion.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1;
CC   -!- SIMILARITY: Belongs to the microviridae Rep protein family.
CC       {ECO:0000305}.
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; M17988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H29825; G2BPSV.
DR   RefSeq; NP_598335.1; NC_003438.1.
DR   GeneID; 935173; -.
DR   KEGG; vg:935173; -.
DR   Proteomes; UP000002101; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   ATP-binding; Endonuclease; Hydrolase; Ligase; Nuclease; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..320
FT                   /note="Replication-associated protein ORF2"
FT                   /id="PRO_0000065792"
FT   ACT_SITE        188
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT   ACT_SITE        192
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
SQ   SEQUENCE   320 AA;  38090 MW;  B4C1B2BCAC1A2058 CRC64;
     MACLRPLQVH NLKKGEKVNF KHYSNGDVAR YDMNKNYIVN DSVPCRKCVG CRLDNSAEWG
     VRASLEIKSN PKHNWFVTLT YSDEHLVYNA LGRPNCVPEH ITKFIKSLRK YFERRGHIGI
     KYLASNEYGT KRMRPHYHIC FFNLPLDDLE KTIDSQKGYQ QWTSKTISRF WDKGFHTIGE
     LTYHSANYTA RYTTKKLGVK DYKALQLVPE KLRMSKGIGL KYFMENKERI YKEDSVLIST
     DKGIKRFKVP KYFDRRMERE WQDEFYLDYI KEKREKVAKR TLFQRQIVSS RSYTDYLGDE
     QKKLNNIVKR LTRPLKTGKK