REP1_MDV1
ID REP1_MDV1 Reviewed; 281 AA.
AC Q9Z0D5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Replication-associated protein of non-essential DNA C1;
GN Name=C1;
OS Milk vetch dwarf virus (isolate N) (MDV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291605;
OH NCBI_TaxID=47065; Astragalus sinicus (Chinese milk vetch).
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9880029; DOI=10.1099/0022-1317-79-12-3111;
RA Sano Y., Wada M., Hashimoto Y., Matsumoto T., Kojima M.;
RT "Sequences of ten circular ssDNA components associated with the milk vetch
RT dwarf virus genome.";
RL J. Gen. Virol. 79:3111-3118(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; AB000920; BAA33980.1; -; Genomic_DNA.
DR SMR; Q9Z0D5; -.
DR Proteomes; UP000008236; 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; Transferase.
FT CHAIN 1..281
FT /note="Para-Rep C1"
FT /id="PRO_0000378519"
FT MOTIF 11..14
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 42..47
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 51..71
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 80..83
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT MOTIF 97..103
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 80
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 173..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 32870 MW; 3D3AAE74F3A38A06 CRC64;
MPTLQGTFWC FTLNFSGDAP SLSFNERVQY ACWQHERVSH DHLQGYIQMK KRSTLKMMKE
LLPGAHLEVS KGTPEEASDY AMKEETRVAG PWTYGELLKK GSNKRKLLDR YKENPEDMEL
EDPAKARRCR AKIDKEKFIA EFKVEDDEQE WKKILEKEIE KIASPRSILW VYGPQGGEGK
TSKAKELITR GWFYTRGGKK DDVAYSYVED PTRHVVFDIP RDMQEYCNYS LIEMLKDRII
ISNKYEPITN CQVYNIHVIV MANFLPDVTK ISEDRIKIIY C
