REP9_FBNY2
ID REP9_FBNY2 Reviewed; 281 AA.
AC P0CK61; O91252; P0CAX6; Q9WIK2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Para-Rep C9;
DE Short=Rep9;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE EC=3.6.1.-;
DE AltName: Full=ATP-dependent helicase C9;
DE AltName: Full=Replication-associated protein of non-essential DNA C9;
GN Name=C9;
OS Faba bean necrotic yellows virus (isolate SV292-88) (FBNYV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291604;
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9880028; DOI=10.1099/0022-1317-79-12-3101;
RA Katul L., Timchenko T., Gronenborn B., Vetten H.J.;
RT "Ten distinct circular ssDNA components, four of which encode putative
RT replication-associated proteins, are associated with the faba bean necrotic
RT yellows virus genome.";
RL J. Gen. Virol. 79:3101-3109(1998).
CC -!- FUNCTION: Initiates and terminates the replication only of its own
CC subviral DNA molecule. The closed circular ssDNA genome is first
CC converted to a superhelical dsDNA. Rep binds a specific hairpin at the
CC genome origin of replication. Introduces an endonucleolytic nick within
CC the intergenic region of the genome, thereby initiating the rolling
CC circle replication (RCR). Following cleavage, binds covalently to the
CC 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a
CC free 3'-OH that serves as a primer for the cellular DNA polymerase. The
CC polymerase synthesizes the (+) strand DNA by rolling circle mechanism.
CC After one round of replication, a Rep-catalyzed nucleotidyl transfer
CC reaction releases a circular single-stranded virus genome, thereby
CC terminating the replication. Displays origin-specific DNA cleavage,
CC nucleotidyl transferase, ATPase and helicase activities (By
CC 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: Homooligomer (Potential). Rep binds to repeated DNA motifs
CC (iterons) (By similarity). {ECO:0000250, ECO:0000305}.
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 -!- MISCELLANEOUS: The genome of nanoviruses is composed of six to eight
CC segments. In addition, some isolates contain subviral DNAs.
CC -!- SIMILARITY: Belongs to the nanoviridea/circoviridae replication-
CC associated protein family. {ECO:0000305}.
CC -!- CAUTION: This protein is encoded by a subviral DNA that is not present
CC in all isolates of the virus. {ECO:0000305}.
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DR EMBL; AJ005966; CAA06789.1; -; Genomic_DNA.
DR SMR; P0CK61; -.
DR Proteomes; UP000008666; 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; IPR003365; Viral_rep_N.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF02407; Viral_Rep; 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..281
FT /note="Para-Rep C9"
FT /id="PRO_0000378527"
FT MOTIF 8..11
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 39..44
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 48..69
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 78..81
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT MOTIF 95..101
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 78
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 172..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 32708 MW; BE746CEFB41A8CA9 CRC64;
MSAVNWVFTL NFAGEVPVLS FDERVQYAVW QHERVNHDHI QGVIQLKKKA KMNTVKNIIG
GNPHLEKMKG SIEEASAYAQ KEESRVAGPW SYGELLKKGS HKRKIMELIK DPENELEEPQ
KYRRAMAWSA MDESRKLAEE EGFPYMFYSW QETVLGLLEE EPNDRTIIWV YGPNGNEGKS
QFGKFLGLKK DYLYLPGGKT QDMTYMLMKN PKANVVMDIP RCNSEYLNYQ FMELIKNRTI
YSYKYEPVGC IINNKIHVIV LANVLPDYEK ISQDRIKIIY C
