REP_SSVN
ID REP_SSVN Reviewed; 364 AA.
AC Q80GM6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Replication-associated protein;
DE Short=Rep;
DE EC=2.7.7.-;
DE EC=3.1.21.-;
GN ORFNames=C1/C2;
OS Sugarcane streak virus (isolate South Africa) (SSV) (Sugarcane streak virus
OS (isolate Natal)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=268781;
OH NCBI_TaxID=173841; Cenchrus echinatus.
OH NCBI_TaxID=4547; Saccharum officinarum (Sugarcane).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8352656; DOI=10.1007/bf01309851;
RA Hughes F.L., Rybicki E.P., Kirby R.;
RT "Complete nucleotide sequence of sugarcane streak Monogeminivirus.";
RL Arch. Virol. 132:171-182(1993).
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=Q80GM6-1; Sequence=Displayed;
CC Name=RepA;
CC IsoId=Q89822-1; 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=AAA47830.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAP13956.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAP13957.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; S64567; AAP13956.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S64567; AAP13957.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M82918; AAA47830.1; ALT_SEQ; Genomic_DNA.
DR SMR; Q80GM6; -.
DR Proteomes; UP000007230; Genome.
DR Proteomes; UP000204673; 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; 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 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..364
FT /note="Replication-associated protein"
FT /id="PRO_0000316943"
FT REGION 180..192
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 257..275
FT /note="Transactivation"
FT /evidence="ECO:0000250"
FT MOTIF 24..28
FT /note="RCR-1"
FT MOTIF 66..71
FT /note="RCR-2"
FT MOTIF 106..109
FT /note="RCR-3"
FT MOTIF 297..308
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 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 364 AA; 41819 MW; A9B513B3708F483B CRC64;
MSTVGSTVSS TPSRRFKHRN VNTFLTYSRC PLEPEAVGLH IWSLIAHWTP VYVLSVRETH
EDGGYHIHVL AQSAKPVYTT DSGFFDIDGF HPNIQSAKSA NKVRAYAMKN PVTYWERGTF
IPRKTSFLGD STEPNSKKQS KDDIVRDIIE HSTNKQEYLS MIQKALPYEW ATKLQYFEYS
ANKLFPDIQE IYTSPFPQST PALLDPTAIN TWLENNLYQQ NSNSNRKLSL YILGPTRTGK
SSWARSLGRH NYWQNNVDWS SYDEDAEYNI IDDIPFKYCP CWKQLIGCQK DYIVNPKYGK
RKKVASKSIP TIVLANEDED WLRDMTPAQQ DYFNANCETY MLEPGERFFS LPAVSATAHP
SSEV
