ID H9BAB8_9GEMI Unreviewed; 347 AA.
AC H9BAB8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 08-NOV-2023, entry version 37.
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};
OS Chickpea chlorosis Australia virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=1302848 {ECO:0000313|EMBL:AFD62998.1, ECO:0000313|Proteomes:UP000202422};
RN [1] {ECO:0000313|EMBL:AFD62998.1, ECO:0000313|Proteomes:UP000202422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CpCV-D_AU_3494I_2002 {ECO:0000313|EMBL:AFD62998.1};
RX PubMed=22406325; DOI=10.1016/j.virusres.2012.02.024;
RA Hadfield J., Thomas J.E., Schwinghamer M.W., Kraberger S., Stainton D.,
RA Dayaram A., Parry J.N., Pande D., Martin D.P., Varsani A.;
RT "Molecular characterisation of dicot-infecting mastreviruses from
RT Australia.";
RL Virus Res. 166:13-22(2012).
RN [2] {ECO:0000313|EMBL:AGT45436.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:AGT45436.1};
RX PubMed=23886492; DOI=10.1016/j.virol.2013.06.024;
RA Kraberger S., Harkins G.W., Kumari S.G., Thomas J.E., Schwinghamer M.W.,
RA Sharman M., Collings D.A., Briddon R.W., Martin D.P., Varsani A.;
RT "Evidence that dicot-infecting mastreviruses are particularly prone to
RT inter-species recombination and have likely been circulating in Australia
RT for longer than in Africa and the Middle East.";
RL Virology 444:282-291(2013).
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 -!- SUBUNIT: Homooligomer. Rep binds to repeated DNA motifs (iterons).
CC Forms the O-complex, which is a Rep-DNA complex involved in the
CC initiation of RCR. Part of the C- and V-complexes which are RepA-Rep-
CC DNA complexes involved in the c-sense and v-sense transcription.
CC {ECO:0000256|ARBA:ARBA00011488}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC ECO:0000256|RuleBase:RU361249}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC {ECO:0000256|ARBA:ARBA00006240, ECO:0000256|RuleBase:RU361249}.
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DR EMBL; JN989422; AFD62998.1; -; Genomic_DNA.
DR EMBL; KC172691; AGT45436.1; -; Genomic_DNA.
DR RefSeq; YP_008472704.1; NC_022131.1.
DR GeneID; 16691596; -.
DR KEGG; vg:16691596; -.
DR OrthoDB; 9195at10239; -.
DR Proteomes; UP000202422; Genome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR027417; P-loop_NTPase.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Covalent protein-DNA linkage {ECO:0000256|ARBA:ARBA00023124};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562,
KW ECO:0000256|RuleBase:RU361249};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361249};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601191-2}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..116
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT DOMAIN 122..225
FT /note="Geminivirus AL1 replication-associated protein
FT central"
FT /evidence="ECO:0000259|Pfam:PF08283"
FT ACT_SITE 101
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT BINDING 53
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ SEQUENCE 347 AA; 40551 MW; 9B8209103BF2CA5B CRC64;
MPQTKKPSSS FRLQTKYVFL TYPRCSSDAE SLRDFLWEKL SRFAIFFIAV ATELHQDGTP
HLHCLLQLDK RSNIRDPSFF DFQGNHPNIQ PAKNSEQVLD YISKDGSVIT RGDFRKHKVS
PTKSDDRWRT IIQTATTKED YLEMIKTEFP HEWATKLQWL EYSANKLFPD IEPPYSSPFP
NEFLQCDEEI TEWLNRDLYV EPEQLQHRRR SLYICGPTRT GKTSWARSLG RHNYFNGGID
FTTYDPNATF NIIDDIPFKF CPNWKQLVGS QKDFTVNPKY GKKKRVKGGI PTIILVNNDD
DWIKDMSSSQ NEYFESNCLI HYMTEGETFI AARRQVTQRA SPPSENI
//
