REP_PASVK
ID REP_PASVK Reviewed; 359 AA.
AC P0C647;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Panicum streak virus (isolate Kenya) (PanSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268780;
OH NCBI_TaxID=59788; Megathyrsus maximus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1588314; DOI=10.1099/0022-1317-73-5-1041;
RA Briddon R.W., Lunness P., Chamberlain L.C., Brundish H., Pinner M.S.,
RA Markham P.G.;
RT "The nucleotide sequence of an infectious insect-transmissible clone of the
RT geminivirus Panicum streak virus.";
RL J. Gen. Virol. 73:1041-1047(1992).
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=P0C647-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=Q00338-1; 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; X60168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C647; -.
DR Proteomes; UP000007896; 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; 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 InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00229; GEMCOATMSVL1.
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; Repressor; Transferase.
FT CHAIN 1..359
FT /note="Replication-associated protein"
FT /id="PRO_0000316942"
FT REGION 181..193
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 258..276
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 25..29
FT /note="RCR-1"
FT MOTIF 67..72
FT /note="RCR-2"
FT MOTIF 107..110
FT /note="RCR-3"
FT MOTIF 298..309
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 107
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 69
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 42004 MW; A8007D732C37FCF7 CRC64;
MSTVGSSSEG RHSVRCFRHR NANTFLTYSK CPLEPEFIGE HLFRLTREYE PAYILVVRET
HTDGTWHCHA LLQCIKPCTT RDERYFDIDR YHGNIQSAKS TDKVREYILK DPKDKWEKGT
YIPRKKSFVP PGKEPAEKKP TKDEVMREIM THATSREEYL SLVQSSLPYD WATKLNYFEY
SASRLFPDIA EPYTNPHPTT EYDLHCNETI EDWLKPNIYQ QNAPGERKRS LYICGPTRTG
KTSWARSLGR HNYWQNNIDW SSYDEEAQYN VVDDIPFKFC PCRKRLVGCQ KDYIVNPKYG
KRRKVASKSI PTIILANEDE DWLKDMTPAH VEYFEANCDQ YILLPGEKFY KTGEAGGSI
