REP1_FBNY2
ID REP1_FBNY2 Reviewed; 278 AA.
AC Q66862;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 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=7844570; DOI=10.1099/0022-1317-76-2-475;
RA Katul L., Maiss E., Vetten V.J.;
RT "Sequence analysis of a faba bean necrotic yellows virus DNA component
RT containing a putative replicase gene.";
RL J. Gen. Virol. 76:475-479(1995).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF TYR-78 AND LYS-177.
RX PubMed=10559333; DOI=10.1128/jvi.73.12.10173-10182.1999;
RA Timchenko T., de Kouchkovsky F., Katul L., David C., Vetten H.J.,
RA Gronenborn B.;
RT "A single Rep protein initiates replication of multiple genome components
RT of faba bean necrotic yellows virus, a single-stranded DNA virus of
RT plants.";
RL J. Virol. 73:10173-10182(1999).
RN [3]
RP REVIEW.
RX PubMed=14741122; DOI=10.1016/j.vetmic.2003.10.015;
RA Gronenborn B.;
RT "Nanoviruses: genome organisation and protein function.";
RL Vet. Microbiol. 98:103-109(2004).
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 {ECO:0000269|PubMed:10559333}.
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; X80879; CAA56847.1; -; Genomic_DNA.
DR SMR; Q66862; -.
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; IDA:CACAO.
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; IDA:CACAO.
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 GO; GO:0019071; P:viral DNA cleavage involved in viral genome maturation; IDA:CACAO.
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 1: Evidence at protein level;
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..278
FT /note="Para-Rep C1"
FT /id="PRO_0000222439"
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 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 176..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 78
FT /note="Y->F: Complete loss of DNA cleavage and nucleotidyl
FT transfer activity."
FT /evidence="ECO:0000269|PubMed:10559333"
FT MUTAGEN 177
FT /note="K->A: Complete loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:10559333"
SQ SEQUENCE 278 AA; 32382 MW; 4D9F4451F4EA2DED CRC64;
MACSNWVFTR NFQGALPLLS FDERVQYAVW QHERGTHDHI QGVIQLKKKA RFSTVKEIIG
GNPHVEKMKG TIEEASAYVQ KEETRVAGPW SYGDLLKRGS HRRKTMERYL EDPEEMQLKD
PDTALRCNAK RLKEDFMKEK TKLQLRPWQK ELHDLILTEP DDRTIIWVYG PDGGEGKSMF
AKELIKYGWF YTAGGKTQDI LYMYAQDPER NIAFDVPRCS SEMMNYQAME MMKNRCFAST
KYRSVDLCCN KNVHLVVFAN VAYDPTKISE DRIVIINC
