ID A0A6B9PT99_9GEMI Unreviewed; 195 AA. AC A0A6B9PT99; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-OCT-2020, entry version 3. 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}; DE Flags: Fragment; OS Euphorbia yellow mosaic virus. OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes; OC Geplafuvirales; Geminiviridae; Begomovirus. OX NCBI_TaxID=598494 {ECO:0000313|EMBL:QHD59442.1}; RN [1] {ECO:0000313|EMBL:QHD59442.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BR-Am-03 {ECO:0000313|EMBL:QHD59442.1}; RA Catarino A.M., Lima E.E.J.S.P., Hanada R.E., Sousa T.F., Cruz J.C., RA Nascimento A.R., Costa C.A., Silva G.F.; RT "Molecular detection of Euphorbia yellow mosaic virus infecting Capsicum RT chinense in Amazonas."; RL Submitted (JAN-2018) 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; MG773280; QHD59442.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C: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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. 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 8..120 FT /note="Gemini_AL1" FT /evidence="ECO:0000259|Pfam:PF00799" FT DOMAIN 124..195 FT /note="Gemini_AL1_M" FT /evidence="ECO:0000259|Pfam:PF08283" FT ACT_SITE 105 FT /note="For DNA cleavage activity" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1" FT METAL 51 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" FT METAL 61 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT METAL 109 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT NON_TER 195 FT /evidence="ECO:0000313|EMBL:QHD59442.1" SQ SEQUENCE 195 AA; 21999 MW; 335315B68A8FD7F5 CRC64; MPRNPNSFRL TAKNIFLTYP RCDIPKDEVL QLLRDLPWAV VKPTYIRVAR ELHADGFPHL HCLIQLSGKS NIKDARFFNL THPRRSAEFH PNAQSAKDAN AVKNYITKEG DYCESGQYKV SGGSKSNKDD VYHNAVNAAT AGEALDIIRA GDPKTFIVNY HNVKANVERL FIKPPLPWVP PFQLSSFNNV PSDLQ //