REP_SLCV
ID REP_SLCV Reviewed; 347 AA.
AC P29048;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Squash leaf curl virus (SLCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=10829;
OH NCBI_TaxID=3662; Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var. moschata).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1984668; DOI=10.1016/0042-6822(91)90009-z;
RA Lazarowitz S.G., Lazdins I.B.;
RT "Infectivity and complete nucleotide sequence of the cloned genomic
RT components of a bipartite squash leaf curl geminivirus with a broad host
RT range phenotype.";
RL Virology 180:58-69(1991).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M38183; AAC32410.1; ALT_INIT; Genomic_DNA.
DR PIR; C36785; QQCVS1.
DR RefSeq; NP_047243.2; NC_001936.1.
DR SMR; P29048; -.
DR GeneID; 956394; -.
DR KEGG; vg:956394; -.
DR Proteomes; UP000009151; 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; Reference proteome; Transferase.
FT CHAIN 1..347
FT /note="Replication-associated protein"
FT /id="PRO_0000222212"
FT REGION 141..151
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 154..174
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 16..20
FT /note="RCR-1"
FT MOTIF 59..64
FT /note="RCR-2"
FT MOTIF 105..108
FT /note="RCR-3"
FT ACT_SITE 105
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 51
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 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 39110 MW; AFDAEBDDE122110E CRC64;
MPRNPNSFRL TARNIFLTYP RCDVPKEEVL EMLLHLSWSV VKPNYVRVAR EEHSDGSPHL
HCLIQLSGKS NIKDAGFFDL THPRRSARFH PNIQAAKDTN AVKNYITKEG DYCESGQYKV
SGGSKSNKDD VYHNAVNAGS AGEALDIIKA GDPKTFIVNY HNLLANVERL FQKPPEPWVP
PFELSSFTSV PEELQDWADD YFNECSAAAR PTSIIIEGGS RTGKTMWARS LGPHNYLSGH
LDFNSRVFSN DVKYNVIDDV APHYLKLKHW KELIGAQRDW QSNCKYGKPV QIKGGIPSIV
LCNPGEGSSY KDFLDKAENS ALREWTEKNA KFIFLEGPLY QSTAQDC
