REP_TYDVA
ID REP_TYDVA Reviewed; 337 AA.
AC P31618;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Tobacco yellow dwarf virus (strain Australia) (TYDV).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=31599;
OH NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
OH NCBI_TaxID=239686; Datura stramonium var. tatula.
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1546458; DOI=10.1016/0042-6822(92)90466-3;
RA Morris B.A.M., Richardson K.A., Haley A., Zhan X., Thomas J.E.;
RT "The nucleotide sequence of the infectious cloned DNA component of tobacco
RT yellow dwarf virus reveals features of geminiviruses infecting
RT monocotyledonous plants.";
RL Virology 187:633-642(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=P31618-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=P31617-1; 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=AAA47949.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA47950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M81103; AAA47949.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M81103; AAA47950.1; ALT_SEQ; Genomic_DNA.
DR PIR; C42452; C42452.
DR RefSeq; NP_620726.1; NC_003822.1.
DR RefSeq; NP_620727.1; NC_003822.1.
DR SMR; P31618; -.
DR GeneID; 944385; -.
DR GeneID; 944386; -.
DR KEGG; vg:944385; -.
DR KEGG; vg:944386; -.
DR Proteomes; UP000007548; 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; 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 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..337
FT /note="Replication-associated protein"
FT /id="PRO_0000222301"
FT REGION 163..175
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 239..257
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 19..23
FT /note="RCR-1"
FT MOTIF 61..66
FT /note="RCR-2"
FT MOTIF 101..104
FT /note="RCR-3"
FT MOTIF 279..289
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 101
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000250"
FT BINDING 53
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 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 337 AA; 39390 MW; 469649E22BC1F983 CRC64;
MPSAPQKTKS FRLQTKYVFL TYPRCSSSAE NLRDFLWDKL SRFAIFFIAI ATELHQDGTP
HLHCLIQLDK RSNIRDPSFF DLEGNHPNIQ PAKNSEQVLE YISKDGNVIT KGEFKKHRVS
PSKSDERWRT IIQTATSKEE YLDMIKDEFP HEWATKLQWL EYSANKLFPP QPEIYQATFT
EEDLQCHEDL QLWRDQHLYH EPRRAGTRIP SLYICGPSRT GKTTWARSLG RHNYWNGTID
FTVYDDHATY NVIDDIPFKF VPLWKQLIGC QSDFTVNPKY GKKKKIKGGV PCIILCNDDE
DWLKNMSPAQ IEYFEANCIT HFMYAAETFF APESSSH
