ID   REPA_CSMV               Reviewed;         295 AA.
AC   P18921;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Replication-associated protein A;
DE            Short=RepA;
DE            EC=3.1.21.-;
GN   ORFNames=C1;
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: Implicated in enhancement of V-sense gene expression. Acts a
CC       an inhibitor of C-sense gene transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Part of the C- and V-complexes which are RepA-
CC       Rep-DNA complexes involved in the c-sense and v-sense transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=RepA;
CC         IsoId=P18921-1; Sequence=Displayed;
CC       Name=Rep;
CC         IsoId=P18919-1; Sequence=External;
CC   -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 may
CC       be involved in metal coordination. RCR-3 is required for phosphodiester
CC       bond cleavage for initiation of RCR.
CC   -!- MISCELLANEOUS: [Isoform RepA]: Produced from the unspliced transcript.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M20021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JU0043; JU0043.
DR   SMR; P18921; -.
DR   Proteomes; UP000203767; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   InterPro; IPR001146; Gemini_AL1_MSV.
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; PR00229; GEMCOATMSVL1.
PE   3: Inferred from homology;
KW   Activator; Alternative splicing; DNA-binding; Endonuclease;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Host cytoplasm;
KW   Host nucleus; Host-virus interaction; Hydrolase; Metal-binding;
KW   Modulation of host cell cycle by virus; Nuclease; Reference proteome;
KW   Repressor.
FT   CHAIN           1..295
FT                   /note="Replication-associated protein A"
FT                   /id="PRO_0000222205"
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   MOTIF           42..46
FT                   /note="RCR-1"
FT   MOTIF           84..89
FT                   /note="RCR-2"
FT   MOTIF           124..127
FT                   /note="RCR-3"
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"
SQ   SEQUENCE   295 AA;  33156 MW;  3386AD9080610B34 CRC64;
     MSSLPVSESE GEGSGTSVQV PSRGGQVTPG EKAFSLRTKH VFLTYPRCPI SPEEAGQKIA
     DRLKNKKCNY IYISREFHAD GEPHLHAFVQ LEANFRTTSP KYFDLDEFHP NIQAARQPAS
     TLKYCMKHPE SSWEFGKFLK PKVNRSPTQS ASRDKTMKQI MANATSRDEY LSMVRKSFPF
     EWAVRLQQFQ YSANALFPDP PQTYSAPYAS RDMSDHPVIG EWLQQELYTV SPQALSLHAG
     ISEEQARIDL QWMSDLTRSG ALESGDEACT SVGQQELERL LGPEVLELIT TGSTQ