ID B6CZ77_9GEMI Unreviewed; 272 AA.
AC B6CZ77;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 30.
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};
OS Maize streak virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=10821 {ECO:0000313|EMBL:ACF40345.1};
RN [1] {ECO:0000313|EMBL:ACF40345.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSV-A1_Za-ThoE-g132-2006 {ECO:0000313|EMBL:ACF40345.1};
RX PubMed=18753214; DOI=10.1099/vir.0.2008/003590-0;
RA Varsani A., Shepherd D.N., Monjane A.L., Owor B.E., Erdmann J.B.,
RA Rybicki E.P., Peterschmitt M., Briddon R.W., Markham P.G., Oluwafemi S.,
RA Windram O.P., Lefeuvre P., Lett J.M., Martin D.P.;
RT "Recombination, decreased host specificity and increased mobility may have
RT driven the emergence of maize streak virus as an agricultural pathogen.";
RL J. Gen. Virol. 89:2063-2074(2008).
RN [2] {ECO:0000313|EMBL:ACZ04171.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSV-A_MZ_Xai1_xaimoz-2007 {ECO:0000313|EMBL:ACZ04171.1};
RX PubMed=19692547; DOI=10.1099/vir.0.015537-0;
RA Harkins G.W., Martin D.P., Duffy S., Monjane A.L., Shepherd D.N.,
RA Windram O.P., Owor B.E., Donaldson L., van Antwerpen T., Sayed R.A.,
RA Flett B., Ramusi M., Rybicki E.P., Peterschmitt M., Varsani A.;
RT "Dating the origins of the maize-adapted strain of maize streak virus, MSV-
RT A.";
RL J. Gen. Virol. 90:3066-3074(2009).
RN [3] {ECO:0000313|EMBL:AEL32046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSV-A_MZ_Map8_Moz3-2007 {ECO:0000313|EMBL:AEL32046.1}, and
RC MSV-A_MZ_Map9_Moz4-2007 {ECO:0000313|EMBL:AEL32049.1};
RX PubMed=21715477; DOI=10.1128/JVI.00640-11;
RA Monjane A.L., Harkins G.W., Martin D.P., Lemey P., Lefeuvre P.,
RA Shepherd D.N., Oluwafemi S., Simuyandi M., Zinga I., Komba E.K.,
RA Lakoutene D.P., Mandakombo N., Mboukoulida J., Semballa S., Tagne A.,
RA Tiendrebeogo F., Erdmann J.B., van Antwerpen T., Owor B.E., Flett B.,
RA Ramusi M., Windram O.P., Syed R., Lett J.M., Briddon R.W., Markham P.G.,
RA Rybicki E.P., Varsani A.;
RT "Reconstructing the history of maize streak virus strain a dispersal to
RT reveal diversification hot spots and its origin in southern Africa.";
RL J. Virol. 85:9623-9636(2011).
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; EU628568; ACF40345.1; -; Genomic_DNA.
DR EMBL; FJ882101; ACZ04171.1; -; Genomic_DNA.
DR EMBL; HQ693358; AEL32046.1; -; Genomic_DNA.
DR EMBL; HQ693359; AEL32049.1; -; 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; IPR001146; Gemini_AL1_MSV.
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; PR00229; GEMCOATMSVL1.
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 10..116
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT DOMAIN 131..239
FT /note="Geminivirus AL1 replication-associated protein
FT central"
FT /evidence="ECO:0000259|Pfam:PF08283"
FT REGION 245..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ SEQUENCE 272 AA; 31589 MW; EA37F4D704D61A2C CRC64;
MASSSSNRQF SHRNVNTFLT YPKCPENPEI ACQMIWELVV RWIPKYIVCA REAHKDGSLH
LHALLQTEKP VRISDSRFFD INGFHPNIQS AKSVNRVRDY ILKEPLAMFE RGTFIPRKSP
FLGKSDSEVK EKKPSKDEIM RDIISHSTSK EEYLSMIQKE FPYDWSTKLQ YFEYSANKLF
PEIQEEFTNP HPQSTPDLLC NESINDWLQP NIFQVSPEAY MLLQPTCYTL EDAISDLQWM
DNVSSHQMKD QESRASTSSG QQEQENLLGP EA
//
