GenomeNet

Database: UniProt
Entry: A7DXH1_9GEMI
LinkDB: A7DXH1_9GEMI
Original site: A7DXH1_9GEMI 
ID   A7DXH1_9GEMI            Unreviewed;       362 AA.
AC   A7DXH1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   08-NOV-2023, entry version 48.
DE   RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531, ECO:0000256|RuleBase:RU361249};
DE            Short=Rep {ECO:0000256|RuleBase:RU361249};
DE            EC=3.1.21.- {ECO:0000256|RuleBase:RU361249};
GN   Name=rep {ECO:0000313|EMBL:CAM91890.1};
OS   Bean leaf curl Madagascar virus.
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=439420 {ECO:0000313|EMBL:CAM91890.1, ECO:0000313|Proteomes:UP000241504};
RN   [1] {ECO:0000313|EMBL:CAM91890.1, ECO:0000313|Proteomes:UP000241504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lefeuvre P., Martin D.P., Hoareau M., Naze F., Becker N., Delatte H.,
RA   Reynaud B., Lett J.M.;
RT   "Begomovirus "melting pot" in the South West Indian Ocean Islands:
RT   molecular diversity and evolution through recombination.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00024923, ECO:0000256|RuleBase:RU361249}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601191-2};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601191-2};
CC       Note=Divalent metal cations, possibly Mg(2+) or Mn(2+).
CC       {ECO:0000256|PIRSR:PIRSR601191-2};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361249};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|RuleBase:RU361249}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC       ECO:0000256|RuleBase:RU361249}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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       {ECO:0000256|RuleBase:RU361249}.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000256|ARBA:ARBA00006240, ECO:0000256|RuleBase:RU361249}.
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; AM701757; CAM91890.1; -; Genomic_DNA.
DR   Proteomes; UP000241504; 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; 3.40.1310.20; -; 1.
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.
DR   SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361249};
KW   Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124,
KW   ECO:0000256|RuleBase:RU361249};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU361249};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|RuleBase:RU361249};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU361249};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562,
KW   ECO:0000256|RuleBase:RU361249};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361249};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601191-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|RuleBase:RU361249};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU361249};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361249};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU361249};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361249}.
FT   DOMAIN          7..119
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00799"
FT   DOMAIN          126..230
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   central"
FT                   /evidence="ECO:0000259|Pfam:PF08283"
FT   ACT_SITE        103
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT   BINDING         49
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   BINDING         57
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   BINDING         107
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ   SEQUENCE   362 AA;  40866 MW;  C19993219CB1F1CA CRC64;
     MAPPKKFRIN AKHYFLTFPK CSLSKEEALE QLKTLNTPTN KKYIKICREL HEDGQPHLHV
     LLQFEGKFNC QNQRFFDLVS PNRSAHFHPN IQGAKSSSDV KSYIDKDGDT LEWGEFQVDG
     RSARGGQQTA NDAYATALNS GSKQEALRVI RELAPKDFVL QYHNLVNNLD RIFQEPPVPY
     SCPFLSSSFD QVPEELEEWA AENVVEAAAR PSRPISIVVE GESRTGKTVW ARSLGPHNYL
     CGHLDLSPKV FSNDAWYNVI DDVDPHYLKH FKEFMGAQKD WQSNTKYGKP VQIKGGIPTI
     FLCNPGPNSS YKEFLDEDKN AHLKSWALKN AVFVTLSEPL FSNTNQGSAS GGQEESNQET
     QD
//
DBGET integrated database retrieval system