REP_CACV
ID REP_CACV Reviewed; 290 AA.
AC Q912W1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Replication-associated protein;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE EC=3.6.1.-;
DE AltName: Full=ATP-dependent helicase Rep;
DE AltName: Full=RepP;
GN Name=Rep; ORFNames=ORF1;
OS Canary circovirus (CaCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Circovirus.
OX NCBI_TaxID=142661;
OH NCBI_TaxID=9134; Serinus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Todd D., Weston J., Ball N.W., Borghmans B.J., Smyth J.A., Gelmini L.,
RA Lavazza A.;
RT "Nucleotide sequence-based identification of a novel circovirus of
RT canaries.";
RL Avian Pathol. 30:321-325(2001).
CC -!- FUNCTION: Essential for the replication of viral ssDNA. The closed
CC circular ssDNA genome is first converted to a superhelical dsDNA. Rep
CC and/or Rep' binds a specific hairpin at the genome origin of
CC replication. Introduces an endonucleolytic nick within the conserved
CC sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby
CC initiating the rolling circle replication (RCR). Following cleavage,
CC binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The
CC cleavage gives rise to a free 3'-OH that serves as a primer for the
CC cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA
CC by rolling circle mechanism. After one round of replication, a Rep-
CC catalyzed nucleotidyl transfer reaction releases a circular single-
CC stranded virus genome, thereby terminating the replication. Displays
CC origin-specific DNA cleavage, nucleotidyl transferase, ATPase and
CC helicase activities. ATPase activity is probably carried by the isoform
CC Rep (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000250};
CC -!- SUBUNIT: Interacts with the capsid protein; this interaction relocates
CC Rep into the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 is
CC probably involved in metal coordination. RCR-3 is required for
CC phosphodiester bond cleavage for initiation of RCR.
CC -!- SIMILARITY: Belongs to the nanoviruses/circoviruses replication-
CC associated protein family. {ECO:0000305}.
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DR EMBL; AJ301633; CAC44748.2; -; Genomic_DNA.
DR RefSeq; NP_573442.1; NC_003410.1.
DR SMR; Q912W1; -.
DR PRIDE; Q912W1; -.
DR GeneID; 935131; -.
DR KEGG; vg:935131; -.
DR Proteomes; UP000007621; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003365; Viral_rep_N.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF02407; Viral_Rep; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Replication-associated protein"
FT /id="PRO_0000319863"
FT MOTIF 4..13
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 14..17
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 51..56
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 60..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 89..92
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 33372 MW; 98095B2736B6B4C8 CRC64;
MAPVRAAAAK RWCFTLNNYT AEEEAKVRAL LPGEFHFAIC GKERGEQGTP HLQGFLHFKK
KQRLSALKKL LARAHWEKAR GSDHDNEEYC SKENDVILTI GEPVQGNRSD LAGAVAAVKA
GRRMVDIARE FSEIYVKYGR GLRDLALMIG QKPRDFKTEV VVITGPSGVG KSRLASEMEG
SKFYKMKGDW WDGYSNEDIV IMDDFYGWLP FCEMLRLMDR YPHKVPVKGS YVEFTSKKIV
ITSNTHPESW YCPDKCYLPA LFRRINKWMY WDGLRFEDVP DAMKKHPINY
