ID   Q96612_9GEMI            Unreviewed;       361 AA.
AC   Q96612;
DT   01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT   01-FEB-1997, sequence version 1.
DT   24-JUL-2024, entry version 76.
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; Abutilon mosaic virus.
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|RuleBase:RU361249};
CC   -!- SUBUNIT: Homooligomer. {ECO:0000256|RuleBase:RU361249}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC       ECO:0000256|PROSITE-ProRule:PRU01364, ECO:0000256|RuleBase:RU361249}.
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}.
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DR   EMBL; U51137; AAB18173.1; -; 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-UniRule.
DR   GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1310.20; -; 1.
DR   InterPro; IPR049912; CRESS_DNA_REP.
DR   InterPro; IPR001301; Gemini_AL1_CLV.
DR   InterPro; IPR001191; Gemini_AL1_REP.
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.
DR   SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR   PROSITE; PS52020; CRESS_DNA_REP; 1.
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|PROSITE-ProRule:PRU01364};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU361249};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|PROSITE-
KW   ProRule:PRU01364}; Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
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|PROSITE-
KW   ProRule:PRU01364};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|PROSITE-
KW   ProRule:PRU01364};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01364}.
FT   DOMAIN          8..116
FT                   /note="CRESS-DNA virus Rep endonuclease"
FT                   /evidence="ECO:0000259|PROSITE:PS52020"
FT   MOTIF           15..18
FT                   /note="RCR-1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01364"
FT   MOTIF           57..59
FT                   /note="RCR-2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01364"
FT   MOTIF           103..106
FT                   /note="RCR-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01364"
FT   ACT_SITE        103
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01364"
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
//