REP_CLVK
ID REP_CLVK Reviewed; 358 AA.
AC P14982;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
DE AltName: Full=40.4 kDa protein;
DE AltName: Full=Protein AC1;
DE AltName: Full=Protein AL1;
GN ORFNames=AC1, AL1;
OS African cassava mosaic virus (isolate West Kenyan 844) (ACMV) (Cassava
OS latent virus (isolate West Kenyan 844)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=10818;
OH NCBI_TaxID=197394; Hewittia sublobata.
OH NCBI_TaxID=3996; Jatropha multifida (Coralbush).
OH NCBI_TaxID=194268; Laportea.
OH NCBI_TaxID=3983; Manihot esculenta (Cassava) (Jatropha manihot).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stanley J., Gay M.R.;
RT "Nucleotide sequence of cassava latent virus DNA.";
RL Nature 301:260-262(1983).
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; J02057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P14982; -.
DR Proteomes; UP000008452; 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..358
FT /note="Replication-associated protein"
FT /id="PRO_0000222203"
FT REGION 142..152
FT /note="Binding to RBR1"
FT /evidence="ECO:0000250"
FT REGION 155..175
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT MOTIF 14..18
FT /note="RCR-1"
FT MOTIF 56..61
FT /note="RCR-2"
FT MOTIF 102..105
FT /note="RCR-3"
FT ACT_SITE 102
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 40346 MW; ED173E753EE92D69 CRC64;
MRTPRFRIQA KNVFLTYPKC SIPKEHLLSF IQTLSLQSNP KFIKICRELH QNGEPHLHAL
IQFEGKITIT NNRLFDCVHP SCSTSFHPNI QGAKSSSDVK SYLDKDGDTV EWGQFQIDGR
SARGGQQSAN DAYAKALNSG SKSEALNVIR ELVPKDFVLQ FHNLNSNLDR IFQEPPAPYV
SPFPCSSFDQ VPVEIEEWVA DNVRDSAARP WRPNSIVIEG DSRTGKTIWA RSLGPHNYLC
GHLDLSPKVF NNAAWYNVID DVDPHYLKHF KEFMGSQRDW QSNTKYGKPV QIKGGIPTIF
LCNPGPTSSY KEFLAEEKQE ALKAWALKNA IFITLTEPLY SGSNQSHSQT SQEASHPA
