REP_MSVPA
ID REP_MSVPA Reviewed; 354 AA.
AC Q91MG2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Maize streak virus genotype E (isolate Pat) (MSV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268331;
OH NCBI_TaxID=4498; Avena sativa (Oat).
OH NCBI_TaxID=217170; Axonopus compressus.
OH NCBI_TaxID=240436; Brachiaria deflexa.
OH NCBI_TaxID=4543; Cenchrus americanus (Pearl millet) (Pennisetum glaucum).
OH NCBI_TaxID=281129; Cenchrus polystachios.
OH NCBI_TaxID=4505; Coix lacryma-jobi (Job's tears).
OH NCBI_TaxID=270102; Dactyloctenium aegyptium.
OH NCBI_TaxID=66017; Digitaria.
OH NCBI_TaxID=90396; Echinochloa colona.
OH NCBI_TaxID=4511; Eleusine coracana (Indian finger millet) (Ragi).
OH NCBI_TaxID=29674; Eleusine indica (Goosegrass) (Cynosurus indicus).
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
OH NCBI_TaxID=59788; Megathyrsus maximus.
OH NCBI_TaxID=29709; Melinis repens (Natal redtop) (Rhynchelytrum repens).
OH NCBI_TaxID=4538; Oryza glaberrima (African rice).
OH NCBI_TaxID=4530; Oryza sativa (Rice).
OH NCBI_TaxID=158143; Paspalum conjugatum (Hilo grass).
OH NCBI_TaxID=147272; Paspalum notatum (Bahia grass).
OH NCBI_TaxID=173849; Paspalum scrobiculatum.
OH NCBI_TaxID=300125; Rottboellia cochinchinensis.
OH NCBI_TaxID=4547; Saccharum officinarum (Sugarcane).
OH NCBI_TaxID=192628; Setaria barbata.
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11601896; DOI=10.1006/viro.2001.1075;
RA Martin D.P., Willment J.A., Billharz R., Velders R., Odhiambo B.,
RA Njuguna J., James D., Rybicki E.P.;
RT "Sequence diversity and virulence in Zea mays of Maize streak virus
RT isolates.";
RL Virology 288:247-255(2001).
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=Q91MG2-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=Q91MG1-1; 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; AF329888; AAK73470.1; -; Genomic_DNA.
DR SMR; Q91MG2; -.
DR Proteomes; UP000007780; 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 Gene3D; 3.40.50.300; -; 1.
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; Reference proteome; Repressor;
KW Transferase.
FT CHAIN 1..354
FT /note="Replication-associated protein"
FT /id="PRO_0000316938"
FT REGION 174..186
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 251..269
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 18..22
FT /note="RCR-1"
FT MOTIF 60..65
FT /note="RCR-2"
FT MOTIF 100..103
FT /note="RCR-3"
FT MOTIF 291..302
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 100
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 52
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 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 104
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 354 AA; 41135 MW; C661AE8C83FA1B46 CRC64;
MASSSSNRSF LHRNANTFLT YPHCPENPEI ISQKLWDLVA RWNPLYIVCA REAHRDGNMH
LHALLQTDKP VRTTDARIFD IEGFHPNIQS AKSVNKVRDY ILKEPLAVFE RGTFIPRKSC
FQGNTPPFPK KNPNKDEIMA HIISHATSKQ EYLCLVRKEF PYDWATKLQY FEYSANKLFP
DIQEEFISPH PPSSPDLLCN ESIKDWLQPN IYQPADEGSR KQSLYIVGPT RTGKSTWARS
LGLHNYWQNN VDWSSYNEDA IYNIVDDIPF KYCPCWKQLV GCQKEFVVNP KYGKKKKVQM
KSKPTIILAN SDEDWMKEMT PGQLEYFEAN CMIYVMSPGE KWYSPPQLPP TEEV
