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Database: UniProt
Entry: B2G3M1_9GEMI
LinkDB: B2G3M1_9GEMI
Original site: B2G3M1_9GEMI 
ID   B2G3M1_9GEMI            Unreviewed;       347 AA.
AC   B2G3M1;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=C1-2 {ECO:0000313|EMBL:CAQ42961.1};
OS   Wheat dwarf virus - barley/SxA43-16.
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Mastrevirus; Wheat dwarf virus.
OX   NCBI_TaxID=520123 {ECO:0000313|EMBL:CAQ42961.1};
RN   [1] {ECO:0000313|EMBL:CAQ42961.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schubert J., Habekuss A., Qui Y., Zhou X.;
RT   "Appearance of defective forms of Wheat dwarf virus.";
RL   Submitted (APR-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. 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; AM980883; CAQ42961.1; -; Genomic_DNA.
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   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          9..124
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00799"
FT   DOMAIN          133..232
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   central"
FT                   /evidence="ECO:0000259|Pfam:PF08283"
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   347 AA;  40145 MW;  C4402B367ADFB054 CRC64;
     MASPSAPRFR VYSKYLFLTY PQCILEPQYA LDSLRTLLAK YEPLYIAAVR ELHEDGSPHL
     HVLVQNKLRA SITNPNALNI GMNTSPFSFF HPNIQAAKDC NQVRDYIMKE VDSDVNTAEW
     GTFVAVTTPG RKDRDADMKQ IIESSTSREE FLSMVCHRFP FEWSIRLKDF EYTARHLFPD
     PVSTYTPEFP IESLMCHETI ESWKNEHLYS ESPGRHKSIY ICGPTRTGKT SWARSLGIHN
     YYNSLVDFTT YDVNAKYNII DDIPFKFTPN WKCFVGAQRD FTVNPKYGKR KMIRGGIPCI
     ILVNPDEDWL KDMTPEQSDY MYSNAVIHYM YEGESFFAFG ENVTASQ
//
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