ID C3UK92_9GEMI Unreviewed; 351 AA.
AC C3UK92;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Rep {ECO:0000313|EMBL:ACP28913.1};
GN Synonyms=rep {ECO:0000313|EMBL:QCZ25039.1};
OS Wheat dwarf virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=10834 {ECO:0000313|EMBL:ACP28913.1};
RN [1] {ECO:0000313|EMBL:ACP28913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CZ1841 {ECO:0000313|EMBL:ACP28925.1}, CZ6239
RC {ECO:0000313|EMBL:ACP28921.1}, CZ7040 {ECO:0000313|EMBL:ACP28929.1},
RC and CZWDV-W {ECO:0000313|EMBL:ACP28913.1};
RX PubMed=19326201; DOI=10.1007/s11262-009-0352-3;
RA Kundu J.K., Gadiou S., Cervena G.;
RT "Discrimination and genetic diversity of Wheat dwarf virus in the Czech
RT Republic.";
RL Virus Genes 38:468-474(2009).
RN [2] {ECO:0000313|EMBL:CCW72612.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UK193WDV {ECO:0000313|EMBL:CCW72612.1}, and Wheat strain
RC {ECO:0000313|EMBL:CDG49300.1};
RX PubMed=24122067; DOI=10.1007/s11262-013-0989-9;
RA Schubert J., Habekuss A., Wu B., Thieme T., Wang X.;
RT "Analysis of complete genomes of isolates of the Wheat dwarf virus from new
RT geographical locations and descriptions of their defective forms.";
RL Virus Genes 48:133-139(2014).
RN [3] {ECO:0000313|EMBL:AHZ65061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Triticale_117 {ECO:0000313|EMBL:AHZ65080.1}, Winter_rye_49
RC {ECO:0000313|EMBL:AHZ65061.1}, Winter_wheat_110
RC {ECO:0000313|EMBL:AHZ65073.1}, and Winter_wheat_111
RC {ECO:0000313|EMBL:AHZ65077.1};
RA Schubert J., Habekuss A.;
RT "The population diversity of Wheat dwarf virus in Germany.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AIT14664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pol-WDV-W {ECO:0000313|EMBL:AIT14664.1};
RA Trzmiel K., Jezewska M.;
RT "Detection and discrimination of wheat and barley isolates of Wheat dwarf
RT virus (WDV-B and WDV-W).";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QCZ25039.1}
RP NUCLEOTIDE SEQUENCE.
RA Somera M., Truve E., Soovali P.;
RT "First report of Wheat dwarf virus in winter wheat in Estonia.";
RL Submitted (NOV-2018) 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; FJ546188; ACP28913.1; -; Genomic_DNA.
DR EMBL; FJ546190; ACP28921.1; -; Genomic_DNA.
DR EMBL; FJ546191; ACP28925.1; -; Genomic_DNA.
DR EMBL; FJ546192; ACP28929.1; -; Genomic_DNA.
DR EMBL; KJ473697; AHZ65061.1; -; Genomic_DNA.
DR EMBL; KJ473700; AHZ65073.1; -; Genomic_DNA.
DR EMBL; KJ473701; AHZ65077.1; -; Genomic_DNA.
DR EMBL; KJ473702; AHZ65080.1; -; Genomic_DNA.
DR EMBL; KM079154; AIT14664.1; -; Genomic_DNA.
DR EMBL; HF968636; CCW72612.1; -; Genomic_DNA.
DR EMBL; HG422310; CDG49300.1; -; Genomic_DNA.
DR EMBL; HG422311; CDG49304.1; -; Genomic_DNA.
DR EMBL; MK193742; QCZ25039.1; -; Genomic_DNA.
DR RefSeq; NP_542349.1; NC_003326.1.
DR SMR; C3UK92; -.
DR GeneID; 929289; -.
DR KEGG; vg:929289; -.
DR OrthoDB; 9195at10239; -.
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 351 AA; 40437 MW; B540DAA37E0AB6CC CRC64;
MASSSAPRFR VYSKYLFLTY PQCTLEPQYA LDSLRTLLNK YEPLYIAAVR ELHEDGSPHL
HVLVQNKLRA SITNPNALNL RMDTSPFSIF HPNIQAAKDC NQVRDYITKE VDSDANTAEW
GTFVAVSTPG RKDRDADMKQ IIESSSSREE FLSMVCNRFP FEWSIRLKDF EYTARHLFPD
PVATYTPEFP TESLICHETI ESWKNEHLYS ESPGRHKSIY ICGPTRTGKT SWARSLGTHN
YYNSLVDFTT YDVNAKYNII DDIPFKFTPN WKCFVGAQRD FTVNPKYGKR KVIRGGIPCI
ILVNPDEDWL KDMTPEQSDY MYSNAVVHYM YEGESFINYS FASGEDVTAS Q
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