ID Q96612_9GEMI Unreviewed; 361 AA. AC Q96612; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 05-JUN-2019, entry version 58. 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:AAB18173.1}; OS Abutilon mosaic virus-HW. OC Viruses; Geminiviridae; Begomovirus. OX NCBI_TaxID=222059 {ECO:0000313|EMBL:AAB18173.1}; RN [1] {ECO:0000313|EMBL:AAB18173.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hawaii {ECO:0000313|EMBL:AAB18173.1}; RX DOI=10.1094/Phyto-86-608; RA Wu Z.C., Hu J.S., Pollston J.E., Ullman D.E., Hiebert E.; RT "Complete nucleotide sequence of a nonvector-transmissible strain of RT Abutilon mosaic geminivirus in Hawaii."; RL Phytopathology 86:608-613(1996). RN [2] {ECO:0000313|EMBL:AAB18173.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hawaii {ECO:0000313|EMBL:AAB18173.1}; RA Wu Z.C.Hu.J.S.Polston.J.E., Ullman D.E., Hiebert E.; RL Submitted (MAR-1996) 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; U51137; AAB18173.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:InterPro. 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 126 231 Gemini_AL1_M. {ECO:0000259|Pfam:PF08283}. SQ SEQUENCE 361 AA; 40887 MW; 034D5A7608253CDC CRC64; MPPPEKFRVQ AKNYFLTYPQ YSLAKEVALS QLQNLETPVN KKFIEICREL HENGEPHLHV LIQFEGKFQC TNYRFFDLVS PTRAAHFHPN IQGAKSSSDV KSYIDKDGDT AEWGEFQIDG RSTRGGQQTA NDSYAKALNA IDVQSALNIL KEEQPKDYVL QNHNIRSNLE RIFAKAPEPW VPPFPLSSFT AVPEEMQEWA DDYFGSGAAA RPHRPLSLIV EGDSRTGKTM WARALGPHNY LSGHLDFNGR VYSNEVLYNV IDDVAPQYLK LKHWKELLGS QKDWQSNCKY GKPVQIKGGI PAIVLCNPGE GSSYKEYLDK EENTGLKNWT RKNAIFITLT SPLYQESTQA GQEEGNQTAE D //