ID   Q96612_9GEMI            Unreviewed;       361 AA.
AC   Q96612;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   25-OCT-2017, entry version 55.
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; ssDNA 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}.
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DR   EMBL; U51137; AAB18173.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q96612; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
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
//