REP_MISV9
ID REP_MISV9 Reviewed; 348 AA.
AC Q67590;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Miscanthus streak virus (isolate 91) (MiSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268776;
OH NCBI_TaxID=183675; Miscanthus sacchariflorus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1919519; DOI=10.1099/0022-1317-72-10-2325;
RA Chatani M., Matsumoto Y., Mizuta H., Ikegami M., Boulton M.I., Davies J.W.;
RT "The nucleotide sequence and genome structure of the geminivirus miscanthus
RT streak virus.";
RL J. Gen. Virol. 72:2325-2331(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. 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=Q67590-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=Q67591-1; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA00835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D01030; BAA00834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D01030; BAA00835.1; ALT_SEQ; Genomic_DNA.
DR PIR; JQ1359; JQ1359.
DR RefSeq; NP_569146.1; NC_003379.1.
DR RefSeq; NP_569147.1; NC_003379.1.
DR SMR; Q67590; -.
DR GeneID; 932215; -.
DR GeneID; 932216; -.
DR KEGG; vg:932215; -.
DR KEGG; vg:932216; -.
DR Proteomes; UP000008874; 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..348
FT /note="Replication-associated protein"
FT /id="PRO_0000316940"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..188
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 251..269
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 29..33
FT /note="RCR-1"
FT MOTIF 71..76
FT /note="RCR-2"
FT MOTIF 111..114
FT /note="RCR-3"
FT MOTIF 291..301
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 111
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 71
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 40318 MW; 3DBC09D1D4EEC444 CRC64;
MRAPASSAAS NRPGPSNHPT PRWNSKQFFL TYPHCNLTPS ELMKELFSRL TEKIPGYIKV
SQEFHKDGDP HLHVLIQLNT KLCTRNPKFF DVQGFHPNIQ PVRDAEKVFG YISKTNGDSD
EMGELQLRIK KPEKPTRDQR MAMIIASSTN RNEYLSMVRK EFPFDWAIRL QQFEYSAAAL
FTEPPPVYQS PFPNEQIVCP PELVDIIDQE WNQQPNGPRR PRSIYICGPS RTGKTTWARN
IGRHNYYNST VDFTHYDKDA IYNVIDDVPF KFLPQWKALV GAQRDYIVNP KYGKKKKIPG
GIPSIILTND DEDWIKDMKP AQVEYLHANA HVHYMYEGQK FYVLPAEE
