ID Q96612_9GEMI Unreviewed; 361 AA. AC Q96612; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 03-AUG-2022, entry version 69. 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:AAB18173.1}; OS Abutilon mosaic virus-HW. OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes; OC Geplafuvirales; 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. 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, 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; U51137; AAB18173.1; -; 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: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 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}; 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 126..231 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 BINDING 49 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT BINDING 57 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT BINDING 59 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" FT BINDING 107 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2" 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 //