REP_PICV
ID REP_PICV Reviewed; 317 AA.
AC Q9IG45;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
OS Pigeon circovirus (PiCV) (Columbid circovirus).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Circovirus.
OX NCBI_TaxID=126070;
OH NCBI_TaxID=8932; Columba livia (Rock dove).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11205099; DOI=10.1007/s007050070002;
RA Mankertz A., Hattermann K., Ehlers B., Soike D.;
RT "Cloning and sequencing of columbid circovirus (coCV), a new circovirus
RT from pigeons.";
RL Arch. Virol. 145:2469-2479(2000).
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:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000305};
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; AF252610; AAF74196.1; -; Genomic_DNA.
DR RefSeq; NP_059527.1; NC_002361.1.
DR SMR; Q9IG45; -.
DR GeneID; 1460801; -.
DR KEGG; vg:1460801; -.
DR Proteomes; UP000000473; 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..317
FT /note="Replication-associated protein"
FT /id="PRO_0000319865"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..40
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 41..44
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 78..83
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 87..107
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 116..119
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 36254 MW; 988D75198E300EE6 CRC64;
MAPCKPGSNP PKGRVSAAEG GARREATRRP PREAAAKRWC FTLNNPTEEE IKSLETWLVS
DFHYAIVGKE VGEQGTPHLQ GFVHLKQKKR LPQLKQLFKR AHWEKARGSD EDNEKYCSKE
GNVLLTLGIP AKGNRSDLSE AVAAVKAGRA MTEVARDFSE IYVKYGRGLR DLKLLIGQQP
RDFKTEVIVI TGPPGCGKSR WAADYPGSKF YKMKGEWWDG YDHQEVVIID DFYGWLPFCE
LLRVTDRYPH KVPVKGAFVE FTSRVIIVTS NSPPDAWYSE ERCCVQALFR RINKWLVWNH
DKFEDAPDCM KKYPINY
