REP2_SCSVF
ID REP2_SCSVF Reviewed; 280 AA.
AC Q87009;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Para-Rep C2;
DE Short=Rep2;
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 C2;
GN Name=C2;
OS Subterranean clover stunt virus (strain F) (SCSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Mulpavirales; Nanoviridae; Nanovirus.
OX NCBI_TaxID=291607;
OH NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7886939; DOI=10.1006/viro.1995.1094;
RA Boevink P.C., Chu P.W.G., Keese P.K.;
RT "Sequence of subterranean clover stunt virus DNA: affinities with the
RT geminiviruses.";
RL Virology 207:354-361(1995).
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; U16731; AAA68018.1; -; Genomic_DNA.
DR SMR; Q87009; -.
DR Proteomes; UP000006543; 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..280
FT /note="Para-Rep C2"
FT /id="PRO_0000378523"
FT MOTIF 7..10
FT /note="RCR-1"
FT /evidence="ECO:0000250"
FT MOTIF 45..50
FT /note="RCR-2"
FT /evidence="ECO:0000250"
FT MOTIF 54..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 84..87
FT /note="RCR-3"
FT /evidence="ECO:0000250"
FT MOTIF 97..103
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 84
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 45
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 280 AA; 32473 MW; BAE273C64B04D6E3 CRC64;
MARRYCFTLN YATEIERETF LSLFSQDELN YFVVGDETAT TGQKHLQGFV SFKNKIRLGG
LKKKFGNRAH WEIARGSDSQ NRDYCCKETL ISEIGIPVMK GSNKRKTMEI YEEDPEEMQL
KDPDTALRCK AKKLKEEYCS CYDFQKLRPW QIELHAALMA EPDDRSIIWV YGSDGGEGKT
SFAKELIRYG WFYTAGGKTQ DVLYMYAQDP ERNIAFDVPR CSSEMMNYQA MEMLKNRVFA
STKYRPVDLC IRKLVHLIVF ANVAPDPTRI SEDRLVIINC
