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Database: UniProt
Entry: B2CPX8_9GEMI
LinkDB: B2CPX8_9GEMI
Original site: B2CPX8_9GEMI 
ID   B2CPX8_9GEMI            Unreviewed;       264 AA.
AC   B2CPX8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   08-NOV-2023, entry version 25.
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=repA {ECO:0000313|EMBL:ACB21033.1};
OS   Wheat dwarf virus - [Yunnan Kunming].
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Mastrevirus; Wheat dwarf virus.
OX   NCBI_TaxID=452669 {ECO:0000313|EMBL:ACB21033.1};
RN   [1] {ECO:0000313|EMBL:ACB21033.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YNKM07-29 {ECO:0000313|EMBL:ACB21033.1};
RA   Wang J., Wu B., Wang X.;
RT   "The sequence of wheat dwarf virus hosted on barley in China.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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. {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   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000256|ARBA:ARBA00006240, ECO:0000256|RuleBase:RU361249}.
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DR   EMBL; EU541489; ACB21033.1; -; Genomic_DNA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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   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   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          9..124
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00799"
FT   DOMAIN          133..233
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   central"
FT                   /evidence="ECO:0000259|Pfam:PF08283"
FT   REGION          242..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        106
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT   BINDING         51
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         61
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT   BINDING         110
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ   SEQUENCE   264 AA;  30228 MW;  CB1EA28BE9E4FED4 CRC64;
     MASSSTPRFR VYSKYLFLTY PQCTLEPQYA LDSLRTLLNK YEPLYIAAVR ELHEDGSPHL
     HVLVQNKLRA SITNPNALNL RMDTSPFSIF HPNIQAAKDC NQVRDYITKE VDSDVNTAEW
     GTFVAVSTPG RKDRDADMKQ IIESSSSREE FLSMVCNRFP FEWSIRLKDF EYTARHLFPD
     PVATYTPEFP TESLICHETI ESWKNEHLYS VSLESYILCT STPADQAQSD LEWMDNYSRS
     HRGGISPSTS ADQPELERLP GQGL
//
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