REP_ABMVW
ID REP_ABMVW Reviewed; 356 AA.
AC P21947; O11842;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=Protein AC1;
DE AltName: Full=Protein AL1;
GN ORFNames=AC1, AL1;
OS Abutilon mosaic virus (isolate West India) (AbMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=10816;
OH NCBI_TaxID=3630; Abutilon.
OH NCBI_TaxID=3635; Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OH NCBI_TaxID=47605; Hibiscus.
OH NCBI_TaxID=96479; Malva.
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=108335; Sida.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2219703; DOI=10.1016/0042-6822(90)90343-p;
RA Frischmuth T., Zimmat G., Jeske H.;
RT "The nucleotide sequence of abutilon mosaic virus reveals prokaryotic as
RT well as eukaryotic features.";
RL Virology 178:461-468(1990).
RN [2]
RP SEQUENCE REVISION.
RA Jeske H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the replication of viral ssDNA. The closed
CC circular ssDNA genome is first converted to a superhelical dsDNA. Rep
CC binds a specific region at the genome origin of replication. It
CC introduces an endonucleolytic nick within the conserved sequence 5'-
CC TAATATTAC-3' in the intergenic region of the genome present in all
CC geminiviruses, thereby initiating the rolling circle replication (RCR).
CC Following cleavage, binds covalently to the 5'-phosphate of DNA as a
CC tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a
CC primer for the cellular DNA polymerase. The polymerase synthesizes the
CC (+) strand DNA by rolling circle mechanism. After one round of
CC replication, a Rep-catalyzed nucleotidyl transfer reaction releases a
CC circular single-stranded virus genome, thereby terminating the
CC replication. Displays origin-specific DNA cleavage, nucleotidyl
CC transferase, ATPase and helicase activities (By similarity).
CC {ECO:0000250}.
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. Interacts with the replication enhancer protein
CC (REn). Interacts with host retinoblastoma-related protein 1 (RBR1), and
CC may thereby induce the transcription of host replicative enzymes even
CC if the cell is not dividing anymore. Interacts with host PCNA.
CC Interacts with host SCE1 protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000305}.
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DR EMBL; X15983; CAA34111.2; -; Genomic_DNA.
DR PIR; A36214; QQCVW1.
DR RefSeq; NP_047218.2; NC_001928.2.
DR SMR; P21947; -.
DR GeneID; 956371; -.
DR KEGG; vg:956371; -.
DR Proteomes; UP000006885; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR001301; Gemini_AL1_CLV.
DR InterPro; IPR001191; Gemini_AL1_REP.
DR InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR InterPro; IPR022692; Gemini_AL1_REP_central.
DR Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00228; GEMCOATCLVL1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; Helicase; Host nucleus; Host-virus interaction; Hydrolase;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..356
FT /note="Replication-associated protein"
FT /id="PRO_0000222200"
FT REGION 143..153
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 156..176
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 15..19
FT /note="RCR-1"
FT MOTIF 57..62
FT /note="RCR-2"
FT MOTIF 103..106
FT /note="RCR-3"
FT ACT_SITE 103
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 40247 MW; 3AA732F65867352A CRC64;
MPPPKKFRVQ AKNYFLTYPQ CSLTKDEALS QLQNLETPVN KKFIKICREL HENGEPHLHV
LIQFEGKYQC TNNRFFDLVS PTRSAHFHPN IQGAKSSSDV KSYIDKDGDT AEWGEFQIDG
RSARGGQQTA NDSYAKALNA GDVQSALNIL KEEQPKDYVL QNHNIRSNLE RIFAKAPEPW
VPRFPLSSFT AVPEEMQEWA DDYFGSGSAA RPDRPLSLIV EGDSRTGKTM WARALGPHNY
LSGHLDFNGR VYSNEVEYNV IDDVAPHYLK LKHWKELLGA QKDWQSNCKY GKPVQIKGGI
PAIVLCNPGE GSSYKEYLDK EENTGLRNWT LKNAIFITLT APLYQEGTQA GQEEGH
