ID A6GVG5_9GEMI Unreviewed; 347 AA.
AC A6GVG5; B3KYE9;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 61.
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:CAL30109.1};
GN Synonyms=Rep {ECO:0000313|EMBL:ACP28885.1};
OS Wheat dwarf virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=10834 {ECO:0000313|EMBL:CAL30109.1};
RN [1] {ECO:0000313|EMBL:CAL30109.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SxA18 {ECO:0000313|EMBL:CAL30109.1};
RX PubMed=17449126; DOI=10.1016/j.virusres.2007.03.018;
RA Schubert J., Habekuss A., Kazmaier K., Jeske H.;
RT "Surveying cereal-infecting geminiviruses in Germany--diagnostics and
RT direct sequencing using rolling circle amplification.";
RL Virus Res. 127:61-70(2007).
RN [2] {ECO:0000313|EMBL:CAP57976.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SA12PstFL1 {ECO:0000313|EMBL:CAP57984.1}, SA1EcoFL2
RC {ECO:0000313|EMBL:CAP57980.1}, and SA41WhEcoFL6
RC {ECO:0000313|EMBL:CAP57976.1};
RA Schubert J., Habekuss A., Qui Y., Zhou X.;
RT "Appearance of defective forms of Barley dwarf virus.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAO77846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Barley {ECO:0000313|EMBL:CAO77846.1};
RA Ramsell J.N.E., Boulton M.I., Martin D.P., Valkonen J.P.T., Kvarnheden A.;
RT "Studies on the host range of the barley strain of Wheat dwarf virus using
RT an agroinfectious viral clone.";
RL Plant Pathol. 58:1161-1169(2009).
RN [4] {ECO:0000313|EMBL:ACP28885.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CZ6482 {ECO:0000313|EMBL:ACP28885.1}, and CZWDV-B
RC {ECO:0000313|EMBL:ACP28933.1};
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 [5] {ECO:0000313|EMBL:AIT14667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WDV-B {ECO:0000313|EMBL:AIT14667.1};
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.
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}.
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; FJ546178; ACP28885.1; -; Genomic_DNA.
DR EMBL; FJ546193; ACP28933.1; -; Genomic_DNA.
DR EMBL; KM079155; AIT14667.1; -; Genomic_DNA.
DR EMBL; AM296018; CAL30109.1; -; Genomic_DNA.
DR EMBL; AM747816; CAO77846.1; -; Genomic_DNA.
DR EMBL; AM921991; CAP57976.1; -; Genomic_DNA.
DR EMBL; AM921992; CAP57980.1; -; Genomic_DNA.
DR EMBL; AM921993; CAP57984.1; -; Genomic_DNA.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; 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: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 Capsid protein {ECO:0000313|EMBL:CAL30109.1};
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};
KW Virion {ECO:0000313|EMBL:CAL30109.1}.
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; 40135 MW; A97007CB89CD4248 CRC64;
MASSSAPRFR 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
//
