ID   REP1_FBNY1              Reviewed;         282 AA.
AC   O91254;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-NOV-2023, entry version 81.
DE   RecName: Full=Para-Rep C1;
DE            Short=Rep1;
DE            EC=2.7.7.-;
DE            EC=3.1.21.-;
DE            EC=3.6.1.-;
DE   AltName: Full=ATP-dependent helicase C1;
DE   AltName: Full=Replication-associated protein of non-essential DNA C1;
GN   Name=C1; ORFNames=ORF1;
OS   Faba bean necrotic yellows virus (isolate Egyptian EV1-93) (FBNYV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC   Mulpavirales; Nanoviridae; Nanovirus; Faba bean necrotic yellows virus.
OX   NCBI_TaxID=291603;
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.
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}.
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; AJ005968; CAA06791.1; -; Genomic_DNA.
DR   SMR; O91254; -.
DR   Proteomes; UP000008665; 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   Gene3D; 3.40.1310.20; -; 1.
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.
DR   PROSITE; PS52020; CRESS_DNA_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..282
FT                   /note="Para-Rep C1"
FT                   /id="PRO_0000378518"
FT   DOMAIN          1..99
FT                   /note="CRESS-DNA virus Rep endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           7..10
FT                   /note="RCR-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           47..49
FT                   /note="RCR-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   MOTIF           56..77
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           86..89
FT                   /note="RCR-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   ACT_SITE        86
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01364"
FT   BINDING         38
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         47
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255"
FT   BINDING         174..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  32677 MW;  EFC5C1368AE261D7 CRC64;
     MASKRWCFTL NYKTAVERES FISLFSRDEL NYFVCGDETA PTTNQKHLQG YVSLKKMIRL
     GGLKKKFGYR AHWEIAKGDD FQNRDYCTKE TLISEIGAPV KKGSNQRKIM DLYLQDPEEM
     QLKDPDTALR CNAKRLRIEY CSSFAVISLR PWQSELHRVL MAEPDDRTII WVYGSDGGEG
     KSTFAKELIK YGWFYTAGGK TQDILYMYAQ DPERNIAFDV PRCSSEMMNY QAMEMLKNRV
     FASTKYRPVD LCVRKKVHLI VFANVSPDPT KISEDRIVII NC
//