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Database: UniProt
Entry: C7FF73_9GEMI
LinkDB: C7FF73_9GEMI
Original site: C7FF73_9GEMI 
ID   C7FF73_9GEMI            Unreviewed;       361 AA.
AC   C7FF73;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   08-NOV-2023, entry version 30.
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=AC1 {ECO:0000313|EMBL:ACU28781.1};
OS   Sida golden mosaic virus - Florida [Phaseolus].
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus; Sida golden mosaic virus.
OX   NCBI_TaxID=587624 {ECO:0000313|EMBL:ACU28781.1};
RN   [1] {ECO:0000313|EMBL:ACU28781.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Florida {ECO:0000313|EMBL:ACU28781.1};
RA   Jones L.A.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACU28781.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Florida {ECO:0000313|EMBL:ACU28781.1};
RX   AGRICOLA=IND44357620; DOI=10.1094/PDIS-94-4-0487B;
RA   Durham T.C., Baker C., Jones L., Snyder L.U.;
RT   "First Report of Sida golden mosaic virus Infecting Snap Bean (Phaseolus
RT   vulgaris) in Florida.";
RL   Plant Dis. 94:487-487(2010).
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}.
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DR   EMBL; GQ357649; ACU28781.1; -; Genomic_DNA.
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          128..231
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   361 AA;  40807 MW;  C282057D6641CFA8 CRC64;
     MPPPKKFRVQ SKNYFLTYPQ CSLTKEEALS QLQSLNTPVN KKFIKICREL HQNGEPHLHV
     LIQFEGKYQC KNNRFFDLVS PTRSAHFHPN IQGAKSSSDV KSYIDKDGDT LEWGEFQIDG
     RSARGGPQTA NDSYAKALNA DSVQSALAVL REEQPKDFVL QNHNIRSNLE RIFAKVPEPW
     VPPFQLSSFT NVPDEMQEWA DEFFGTGSAA RPDRPLSLIV EGDSRTGKTM WARALGPHNY
     LSGHLDFNGR VYSNEVEYNV IDDVAPQYLK LKHWKELLGA QKDWQSNCKY GKPVQIKGGI
     PAIVLCNPGE GASYKEFLDK EENTGLRNWT IKNAIFITLT APLYQEGTQA GQEEGNQEAE
     D
//
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