ID O73466_9GEMI Unreviewed; 258 AA.
AC O73466;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 60.
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};
DE Flags: Fragment;
GN Name=repA {ECO:0000313|EMBL:CAA12298.1};
OS Maize streak virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Mastrevirus.
OX NCBI_TaxID=10821 {ECO:0000313|EMBL:CAA12298.1};
RN [1] {ECO:0000313|EMBL:CAA12298.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:CAA12298.1};
RX PubMed=8893787; DOI=10.1007/BF01718288;
RA Peterschmitt M., Granier M., Frutos R., Reynaud B.;
RT "Infectivity and complete nucleotide sequence of the genome of a
RT genetically distinct strain of maize streak virus from Reunion Island.";
RL Arch. Virol. 141:1637-1650(1996).
RN [2] {ECO:0000313|EMBL:CAA12298.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:CAA12298.1};
RA Isnard M., Granier M., Frutos R., Reynaud B., Peterschmitt M.;
RT "Quasispecies nature of three related maize streak virus isolates obtained
RT through different modes of selection from a population used to asses
RT response to infection of maize cultivars.";
RL J. Gen. Virol. 79:3091-3099(1998).
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; AJ225005; CAA12298.1; -; 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 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"
FT NON_TER 258
FT /evidence="ECO:0000313|EMBL:CAA12298.1"
SQ SEQUENCE 258 AA; 30163 MW; ECC3388CB5CE6C02 CRC64;
MASSSSNRQF SHRNANTFLT YPKCPENPEI ACQMIWELVV RWIPKYIICA REAHKDGSWH
LHALLQTEKP VRISDSRFFD INGFHPNIQS AKSVNRVRDY ILKEPLAMFE RGTFIPRKSP
FLGKSDSEVK EKKPSKDEIM RDIISHSTSK EEYLSMIQKE FPYDWSTKLQ YFEYSANKLF
PEIQEEFTNP HPPSSPDLLC NESINDWLQP NIFQVSPEAY MLLQPTCYTL EDAISDLQWM
DSVSRHQMKD QESRASTS
//
