REPA_BEYDV
ID REPA_BEYDV Reviewed; 292 AA.
AC O39521; A4K7Q4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Replication-associated protein A;
DE Short=RepA;
DE EC=3.1.21.-;
GN ORFNames=C1;
OS Bean yellow dwarf virus (BeYDV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=57119;
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9267015; DOI=10.1099/0022-1317-78-8-2113;
RA Liu L., van Tonder T., Pietersen G., Davies J.W., Stanley J.;
RT "Molecular characterization of a subgroup I geminivirus from a legume.";
RL J. Gen. Virol. 78:2113-2117(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Mild;
RX PubMed=17347772; DOI=10.1007/s00705-006-0933-6;
RA Halley-Stott R.P., Tanzer F., Martin D.P., Rybicki E.P.;
RT "The complete nucleotide sequence of a mild strain of Bean yellow dwarf
RT virus.";
RL Arch. Virol. 152:1237-1240(2007).
RN [3]
RP INTERACTION WITH ZEA MAYS RBR1, AND MUTAGENESIS OF LEU-181; CYS-183 AND
RP GLU-185.
RX PubMed=10191192; DOI=10.1006/viro.1999.9616;
RA Liu L., Saunders K., Thomas C.L., Davies J.W., Stanley J.;
RT "Bean yellow dwarf virus RepA, but not rep, binds to maize retinoblastoma
RT protein, and the virus tolerates mutations in the consensus binding
RT motif.";
RL Virology 256:270-279(1999).
RN [4]
RP FUNCTION, INTERACTION WITH ZEA MAYS RBR1, AND MUTAGENESIS OF GLU-185.
RX PubMed=14645928; DOI=10.1099/vir.0.19494-0;
RA Hefferon K.L., Dugdale B.;
RT "Independent expression of Rep and RepA and their roles in regulating bean
RT yellow dwarf virus replication.";
RL J. Gen. Virol. 84:3465-3472(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16972938; DOI=10.1111/j.1742-4658.2006.05454.x;
RA Hefferon K.L., Moon Y.-S., Fan Y.;
RT "Multi-tasking of nonstructural gene products is required for bean yellow
RT dwarf geminivirus transcriptional regulation.";
RL FEBS J. 273:4482-4494(2006).
CC -!- FUNCTION: Implicated in enhancement of V-sense gene expression. Acts a
CC an inhibitor of C-sense gene transcription.
CC {ECO:0000269|PubMed:14645928, ECO:0000269|PubMed:16972938}.
CC -!- SUBUNIT: Homooligomer. Interacts with host retinoblastoma-related
CC protein 1 (RBR1), and may thereby deregulate the host cell cycle. Part
CC of the C- and V-complexes which are RepA-Rep-DNA complexes involved in
CC the c-sense and v-sense transcription (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16972938}. Host
CC cytoplasm {ECO:0000269|PubMed:16972938}. Note=distributed equally
CC throughout both the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RepA;
CC IsoId=O39521-1; Sequence=Displayed;
CC Name=Rep;
CC IsoId=O39522-1; Sequence=External;
CC -!- DOMAIN: There are three rolling circle replication (RCR) motifs. RCR-2
CC may be involved in metal coordination. RCR-3 is required for
CC phosphodiester 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}.
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DR EMBL; Y11023; CAA71907.1; -; Genomic_DNA.
DR EMBL; DQ458791; ABE67103.1; -; Genomic_DNA.
DR RefSeq; NP_612222.1; NC_003493.2. [O39521-1]
DR SMR; O39521; -.
DR PRIDE; O39521; -.
DR GeneID; 935291; -.
DR KEGG; vg:935291; -.
DR Proteomes; UP000007453; 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 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..292
FT /note="Replication-associated protein A"
FT /id="PRO_0000318770"
FT REGION 160..172
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 181..185
FT /note="Binding to RBR1"
FT REGION 230..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..20
FT /note="RCR-1"
FT MOTIF 58..63
FT /note="RCR-2"
FT MOTIF 98..101
FT /note="RCR-3"
FT COMPBIAS 255..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 102
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT VARIANT 63
FT /note="I -> L (in strain: Mild)"
FT VARIANT 171
FT /note="Q -> P (in strain: Mild)"
FT VARIANT 189
FT /note="N -> S (in strain: Mild)"
FT VARIANT 205
FT /note="F -> Y (in strain: Mild)"
FT VARIANT 212
FT /note="D -> Q (in strain: Mild)"
FT VARIANT 227..228
FT /note="MR -> TM (in strain: Mild)"
FT VARIANT 231..232
FT /note="LG -> ME (in strain: Mild)"
FT VARIANT 256
FT /note="G -> D (in strain: Mild)"
FT VARIANT 260
FT /note="T -> I (in strain: Mild)"
FT VARIANT 263
FT /note="G -> V (in strain: Mild)"
FT VARIANT 266
FT /note="T -> I (in strain: Mild)"
FT MUTAGEN 181
FT /note="L->I: 20% loss of ability to bind RBR."
FT /evidence="ECO:0000269|PubMed:10191192"
FT MUTAGEN 183
FT /note="C->S: 50% loss of ability to bind RBR."
FT /evidence="ECO:0000269|PubMed:10191192"
FT MUTAGEN 185
FT /note="E->Q: 95% loss of ability to bind RBR. Reduced
FT replication efficiency."
FT /evidence="ECO:0000269|PubMed:10191192,
FT ECO:0000269|PubMed:14645928"
SQ SEQUENCE 292 AA; 33354 MW; 31C4DCA03607F3BF CRC64;
MPSASKNFRL QSKYVFLTYP KCSSQRDDLF QFLWEKLTPF LIFFLGVASE LHQDGTTHYH
ALIQLDKKPC IRDPSFFDFE GNHPNIQPAR NSKQVLDYIS KDGDIKTRGD FRDHKVSPRK
SDARWRTIIQ TATSKEEYLD MIKEEFPHEW ATKLQWLEYS ANKLFPPQPE QYVSPFTESD
LRCHEDLHNW RETHLYHVSI DAYTFIHPVS YDQAQSDLEW MADLTRMREG LGSDTPASTS
ADQLVPERPP GLEVSGDTTT GTGPSTSPTT MNTPPIISST TSPSSSSHCG SN
