REP_WDVS
ID REP_WDVS Reviewed; 351 AA.
AC Q67622;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Wheat dwarf virus (isolate Sweden) (WDV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268789;
OH NCBI_TaxID=4498; Avena sativa (Oat).
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=4521; Lolium multiflorum (Italian ryegrass) (Lolium perenne subsp. multiflorum).
OH NCBI_TaxID=4550; Secale cereale (Rye).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15938050; DOI=10.1002/j.1460-2075.1985.tb03912.x;
RA McDowell S.W., McDonald H., Hamilton W.D.O., Coutts R.H.A., Buck K.W.;
RT "The nucleotide sequence of cloned wheat dwarf virus DNA.";
RL EMBO J. 4:2173-2180(1985).
RN [2]
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=10891420; DOI=10.1006/viro.2000.0412;
RA Missich R., Ramirez-Parra E., Gutierrez C.;
RT "Relationship of oligomerization to DNA binding of Wheat dwarf virus RepA
RT and Rep proteins.";
RL Virology 273:178-188(2000).
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 {ECO:0000269|PubMed:10891420}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Rep;
CC IsoId=Q67622-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=P06847-1; 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=CAA26624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA26625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X02869; CAA26624.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X02869; CAA26625.1; ALT_SEQ; Genomic_DNA.
DR PDB; 6Q1M; X-ray; 1.24 A; A=1-137.
DR PDB; 6WE0; X-ray; 1.80 A; A=1-137.
DR PDB; 6WE1; X-ray; 2.61 A; A/D=1-137.
DR PDBsum; 6Q1M; -.
DR PDBsum; 6WE0; -.
DR PDBsum; 6WE1; -.
DR SMR; Q67622; -.
DR Proteomes; UP000007629; 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 GO; GO:0039684; P:rolling circle single-stranded viral DNA replication; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding;
KW Covalent protein-DNA linkage; DNA replication; DNA-binding; Endonuclease;
KW Helicase; Host nucleus; Hydrolase; Metal-binding; Multifunctional enzyme;
KW Nuclease; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Repressor; Transferase.
FT CHAIN 1..351
FT /note="Replication-associated protein"
FT /id="PRO_0000316945"
FT REGION 173..185
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 246..264
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 17..21
FT /note="RCR-1"
FT MOTIF 59..64
FT /note="RCR-2"
FT MOTIF 106..109
FT /note="RCR-3"
FT MOTIF 286..296
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 106
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:6Q1M"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6Q1M"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6Q1M"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6Q1M"
FT STRAND 58..72
FT /evidence="ECO:0007829|PDB:6Q1M"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6Q1M"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6Q1M"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:6Q1M"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6WE0"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:6Q1M"
SQ SEQUENCE 351 AA; 40511 MW; 51664B5AD96A2463 CRC64;
MASSSAPRFR VYSKYLFLTY PECTLEPQYA LDSLRTLLNK YEPLYIAAVR ELHEDGSPHL
HVLVQNKLRA SITNPNALNL RMDTSPFSIF HPNIQAAKDC NQVRDYITKE VDSDVNTAEW
GTFVAVSTPG RKDRDADMKQ IIESSSSREE FLSMVCNRFP FEWSIRLKDF EYTARHLFPD
PVATYTPEFP TESLICHETI ESWKNEHLYS ESPGRHKSIY ICGPTRTGKT SWARSLGTHN
YYNSLVDFTT YDVNAKYNII DDIPFKFTPN WKCFVGAQRD FTVNPKYGKR KVIRGGIPCI
ILVNPDEDWL KDMTPEQSDY MYSNTVVHYM YEGETFINYS FASGEDVTAS Q
