ID A9YC19_9GEMI Unreviewed; 102 AA. AC A9YC19; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 19-JAN-2022, entry version 22. DE RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531}; DE Flags: Fragment; OS Tomato yellow leaf curl virus. OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes; OC Geplafuvirales; Geminiviridae; Begomovirus. OX NCBI_TaxID=10832 {ECO:0000313|EMBL:ABX60436.1}; RN [1] {ECO:0000313|EMBL:ABX60436.1} RP NUCLEOTIDE SEQUENCE. RA Anfoka G.H., Abhary M.K., Haj Ahmad F.W.; RT "Cucurbits are natural hosts for viruses that cause Tomato yellow leaf curl RT disease."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABX60436.1} RP NUCLEOTIDE SEQUENCE. RX AGRICOLA=IND44235486; DOI=10.1111/j.1365-3059.2009.02060.x; RA Anfoka G., Haj Ahmad F., Abhary M., Hussein A.; RT "Detection and molecular characterization of viruses associated with tomato RT yellow leaf curl disease in cucurbit crops in Jordan."; RL Plant Pathol. 58:754-762(2009). 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}. 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|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family. CC {ECO:0000256|ARBA:ARBA00006240}. 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; EU143755; ABX60436.1; -; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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 Pfam; PF00799; Gemini_AL1; 1. DR PRINTS; PR00227; GEMCOATAL1. DR PRINTS; PR00228; GEMCOATCLVL1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601191-2}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 5..102 FT /note="Gemini_AL1" FT /evidence="ECO:0000259|Pfam:PF00799" FT ACT_SITE 101 FT /note="For DNA cleavage activity" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1" FT METAL 47 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT METAL 55 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT METAL 57 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT NON_TER 102 FT /evidence="ECO:0000313|EMBL:ABX60436.1" SQ SEQUENCE 102 AA; 11976 MW; E211C6EC9CBB425A CRC64; MPRLFKIYAK NYFLTYPNCS LSKEEALSQL KNLETPTNKK YIKVCRELHE NGEPHLHVLI QFEGKYQCKN QRFFDLVSPN RSAHFHPNIQ AAKSSTDVKT YV //