ID A0A089FUV9_9GEMI Unreviewed; 352 AA. AC A0A089FUV9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-AUG-2020, entry version 12. 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:AIP89857.1}; OS East African cassava mosaic Cameroon virus. OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes; OC Geplafuvirales; 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., 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. 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|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|ARBA:ARBA00001936, CC 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; 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|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, ECO:0000256|RuleBase:RU361249}; 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="Gemini_AL1" FT /evidence="ECO:0000259|Pfam:PF00799" FT DOMAIN 134..230 FT /note="Gemini_AL1_M" FT /evidence="ECO:0000259|Pfam:PF08283" FT ACT_SITE 103 FT /note="For DNA cleavage activity" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1" FT METAL 49 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 METAL 59 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" 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 //