ID A0A089FUV9_9GEMI Unreviewed; 352 AA. AC A0A089FUV9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 18-SEP-2019, entry version 9. DE RecName: Full=Replication-associated protein {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:AIP89857.1}; OS East African cassava mosaic Cameroon virus. OC Viruses; Geminiviridae; Begomovirus. OX NCBI_TaxID=223262 {ECO:0000313|EMBL:AIP89857.1}; RN [1] {ECO:0000313|EMBL:AIP89857.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MG:MG704B1:11 {ECO:0000313|EMBL:AIP89857.1}; RA Hoareau M., Harimalala M., Zinga I., De Bruyn A., Lett J.-M., RA Lefeuvre P.; RT "Divergent evolutionary histories of Cassava Mosaic Geminiviruses in RT Madagascar."; RL Submitted (MAY-2014) 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. CC Rep binds a specific region at the genome origin of replication. CC It introduces an endonucleolytic nick within the conserved CC sequence 5'-TAATATTAC-3' in the intergenic region of the genome CC present in all geminiviruses, thereby initiating the rolling CC circle replication (RCR). Following cleavage, binds covalently to CC the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives CC rise to a free 3'-OH that serves as a primer for the cellular DNA CC polymerase. The polymerase synthesizes the (+) strand DNA by CC rolling circle mechanism. After one round of replication, a Rep- CC catalyzed nucleotidyl transfer reaction releases a circular CC single-stranded virus genome, thereby terminating the replication. CC Displays origin-specific DNA cleavage, nucleotidyl transferase, CC ATPase and helicase activities. {ECO:0000256|RuleBase:RU361249}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361249}; 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 CC {ECO:0000256|RuleBase:RU361249}. CC -!- DOMAIN: There are 3 rolling circle replication (RCR) motifs. RCR-2 CC is 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|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; KJ888092; AIP89857.1; -; Genomic_DNA. 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:InterPro. 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU361249}; KW Covalent protein-DNA linkage {ECO:0000256|RuleBase:RU361249}; KW DNA-binding {ECO:0000256|RuleBase:RU361249}; KW Endonuclease {ECO:0000256|RuleBase:RU361249}; KW Helicase {ECO:0000256|RuleBase:RU361249}; KW Host nucleus {ECO:0000256|RuleBase:RU361249}; KW Hydrolase {ECO:0000256|RuleBase:RU361249}; KW Metal-binding {ECO:0000256|RuleBase:RU361249}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU361249}; KW Nuclease {ECO:0000256|RuleBase:RU361249}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU361249}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU361249}; KW Transferase {ECO:0000256|RuleBase:RU361249}. FT DOMAIN 7 119 Gemini_AL1. {ECO:0000259|Pfam:PF00799}. FT DOMAIN 134 230 Gemini_AL1_M. {ECO:0000259|Pfam:PF08283}. SQ SEQUENCE 352 AA; 39915 MW; 662BEFE24BDD1177 CRC64; MPRAGRFQIN AKNYFITYPR CSLTKEEALS QLKALSYPTN IKFVRVCREL HQDGVPHLHV LIQFEGKFQC TNPRFFDLIS PSRSTHFHPN IQGAKSSSDV KAYIEKGGEF LDDGIFQVDA RSARGEGQHL AQVYADALNA SSKSEALNII KEKDPKSFFL QFHNISANAD RIFQAPPQTY VSPFLSSSFT QIPEEIEVWV SENICRPAAR PWRPISIVLE GDSRTGKTMW ARSLGPHNYL CGHLDLSPKI YSNDAWYNVI DDVDPHYLKH FKEFMGAQRD WQSNTKYGKP IQIKGGIPTI FLCNPGPNSS YKEYLDEDKN SNLKNWAIKN ALFISLTEPL FSSTDQSQAQ AS //