ID Q4GZI5_9GEMI Unreviewed; 361 AA.
AC Q4GZI5;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:CAI84286.1};
OS Alternanthera yellow vein virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=337826 {ECO:0000313|EMBL:CAI84286.1, ECO:0000313|Proteomes:UP000202624};
RN [1] {ECO:0000313|EMBL:CAI84286.1, ECO:0000313|Proteomes:UP000202624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G38 {ECO:0000313|EMBL:CAI84286.1};
RA Huang J., Jiang T., Zhou X.;
RT "Molecular characterization of two distinct begomoviruses infecting
RT Ludwigia hyssopifolia.";
RL J. Plant Pathol. 88:83-88(2006).
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|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; AJ965540; CAI84286.1; -; Genomic_DNA.
DR RefSeq; YP_271828.1; NC_007211.1.
DR KEGG; vg:3562306; -.
DR OrthoDB; 9195at10239; -.
DR Proteomes; UP000202624; Genome.
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 Gene3D; 3.40.1310.20; -; 1.
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.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000202624};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361249}.
FT DOMAIN 7..119
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT DOMAIN 126..230
FT /note="Geminivirus AL1 replication-associated protein
FT central"
FT /evidence="ECO:0000259|Pfam:PF08283"
FT REGION 342..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 41151 MW; C7464508FA67E2CC CRC64;
MRQPGRFRLN RKNFFLTYSQ CPISKEEALE QLLNIQTPVN KKFIRVCREL HEDGNPHLHA
LVQFEGKFDL TNPRFFDLQS PNSSSQYHCF ITDAKSSSDV KAYIEKDGDI LDWGTFQIDG
RSARGGQQTA NDAYARAINT GNKDQALDVI KELAPKDYVL QFHNLNANLE RIFMPPIEEY
ISPFNCSSFD QVPEEIEEWA ADNVMSAAAR PWRPISIVIE GDSRTGKTMW ARSLGPHNYL
CGHIDLSPRV YSNEAWYNII DDVDPHYVKH FKEFMGAQRD WQSNTKYGKP VQIKGGIPTI
FLCNPGPTSS YKEFLDEEKN IGLKNWAIKN ATFVTINQPL YSGSHQSPTQ ASQEETSQTE
G
//