REP_CSMV
ID REP_CSMV Reviewed; 361 AA.
AC P18919;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Chloris striate mosaic virus (CSMV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=10820;
OH NCBI_TaxID=4498; Avena sativa (Oat).
OH NCBI_TaxID=110876; Chloris gayana.
OH NCBI_TaxID=4509; Dactylis glomerata (Orchard grass) (Cock's-foot grass).
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=279312; Ixophorus unisetus.
OH NCBI_TaxID=4564; Triticum.
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3369088; DOI=10.1016/0042-6822(88)90558-2;
RA Andersen M.T., Richardson K.A., Harbison S.A., Morris B.A.M.;
RT "Nucleotide sequence of the geminivirus chloris striate mosaic virus.";
RL Virology 164:443-449(1988).
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. Acts as an inhibitor of C-
CC sense gene transcription (By similarity). {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. Rep binds to repeated DNA motifs (iterons).
CC Forms the O-complex, which is a Rep-DNA complex involved in the
CC initiation of RCR. Part of the C- and V-complexes which are RepA-Rep-
CC DNA complexes involved in the c-sense and v-sense transcription.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Rep;
CC IsoId=P18919-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=P18921-1; Sequence=External;
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 -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000305}.
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DR EMBL; M20021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JU0044; JU0044.
DR SMR; P18919; -.
DR Proteomes; UP000203767; 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 InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00228; GEMCOATCLVL1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Covalent protein-DNA linkage;
KW DNA replication; DNA-binding; Endonuclease; Helicase; Host nucleus;
KW Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repressor;
KW Transferase.
FT CHAIN 1..361
FT /note="Replication-associated protein"
FT /id="PRO_0000222283"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..204
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 266..285
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 42..46
FT /note="RCR-1"
FT MOTIF 84..89
FT /note="RCR-2"
FT MOTIF 124..127
FT /note="RCR-3"
FT MOTIF 307..317
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 243..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 41426 MW; 54CF1B5CD2D303E8 CRC64;
MSSLPVSESE GEGSGTSVQV PSRGGQVTPG EKAFSLRTKH VFLTYPRCPI SPEEAGQKIA
DRLKNKKCNY IYISREFHAD GEPHLHAFVQ LEANFRTTSP KYFDLDEFHP NIQAARQPAS
TLKYCMKHPE SSWEFGKFLK PKVNRSPTQS ASRDKTMKQI MANATSRDEY LSMVRKSFPF
EWAVRLQQFQ YSANALFPDP PQTYSAPYAS RDMSDHPVIG EWLQQELYTW SPGVRRRSLY
ICGPTRTGKT SWARSLGTHH YWQHSVNFLE EWNCQAQFNI IDDIPFKFVP CWKGLVGSQY
DLTVNPKYGK KKRIPNGIPC IILVNEDEDW LQSMSTQQVD WFHGNAVVYH LLPGETFIPS
E
