REPA_WDVS
ID REPA_WDVS Reviewed; 264 AA.
AC P06847;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Replication-associated protein A;
DE Short=RepA;
DE EC=3.1.21.-;
GN ORFNames=C1;
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 MUTAGENESIS OF CYS-196 AND GLU-198.
RX PubMed=7664747; DOI=10.1002/j.1460-2075.1995.tb00079.x;
RA Xie Q., Suarez-Lopez P., Gutierrez C.;
RT "Identification and analysis of a retinoblastoma binding motif in the
RT replication protein of a plant DNA virus: requirement for efficient viral
RT DNA replication.";
RL EMBO J. 14:4073-4082(1995).
RN [3]
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).
RN [4]
RP INTERACTION WITH ZEA MAYS RBR1.
RX PubMed=14741123; DOI=10.1016/j.vetmic.2003.10.012;
RA Gutierrez C., Ramirez-Parra E., Mar Castellano M., Sanz-Burgos A.P.,
RA Luque A., Missich R.;
RT "Geminivirus DNA replication and cell cycle interactions.";
RL Vet. Microbiol. 98:111-119(2004).
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. Interacts (via LXCXE domain) with host
CC retinoblastoma-related protein 1 (RBR1), and may thereby deregulate the
CC host cell cycle. Part of the C- and V-complexes which are RepA-Rep-DNA
CC complexes involved in the c-sense and v-sense transcription.
CC {ECO:0000269|PubMed:10891420, ECO:0000269|PubMed:14741123}.
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=P06847-1; Sequence=Displayed;
CC Name=Rep;
CC IsoId=Q67622-1; 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 -!- DOMAIN: The LXCXE motif specifically binds to host RBR1.
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; X02869; CAA26625.1; -; Genomic_DNA.
DR SMR; P06847; -.
DR ELM; P06847; -.
DR Proteomes; UP000007629; 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; 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 Pfam; PF00799; Gemini_AL1; 1.
DR Pfam; PF08283; Gemini_AL1_M; 1.
DR PRINTS; PR00227; GEMCOATAL1.
DR PRINTS; PR00228; GEMCOATCLVL1.
PE 1: Evidence at protein level;
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..264
FT /note="Replication-associated protein A"
FT /id="PRO_0000222220"
FT REGION 173..185
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 237..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 194..198
FT /note="LXCXE motif, interaction with host RBR1"
FT /evidence="ECO:0000305"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MUTAGEN 196
FT /note="C->G: Loss of interaction with the human
FT retinoblastoma-like protein 2."
FT /evidence="ECO:0000269|PubMed:7664747"
FT MUTAGEN 198
FT /note="E->K: Loss of interaction with the human
FT retinoblastoma-like protein 2."
FT /evidence="ECO:0000269|PubMed:7664747"
SQ SEQUENCE 264 AA; 30157 MW; 8137A357E6503A7E CRC64;
MASSSAPRFR VYSKYLFLTY PECTLEPQYA LDSLRTLLNK YEPLYIAAVR ELHEDGSPHL
HVLVQNKLRA SITNPNALNL RMDTSPFSIF HPNIQAAKDC NQVRDYITKE VDSDVNTAEW
GTFVAVSTPG RKDRDADMKQ IIESSSSREE FLSMVCNRFP FEWSIRLKDF EYTARHLFPD
PVATYTPEFP TESLICHETI ESWKNEHLYS VSLESYILCT STPADQAQSD LEWMDDYSRS
HRGGISPSTS AGQPEQERLP GQGL
