ID I3QQ81_9GEMI Unreviewed; 302 AA.
AC I3QQ81;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 08-NOV-2023, entry version 28.
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};
GN Name=C1 {ECO:0000313|EMBL:AFK14046.1};
OS Beet curly top Iran virus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Becurtovirus.
OX NCBI_TaxID=391228 {ECO:0000313|EMBL:AFK14046.1};
RN [1] {ECO:0000313|EMBL:AFK14046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IR:Kav:B22K:Sug:08 {ECO:0000313|EMBL:AFK14046.1};
RX PubMed=23081676; DOI=10.1007/s00705-012-1485-6;
RA Heydarnejad J., Keyvani N., Razavinejad S., Massumi H., Varsani A.;
RT "Fulfilling Koch's postulates for beet curly top Iran virus and proposal
RT for consideration of new genus in the family Geminiviridae.";
RL Arch. Virol. 158:435-443(2013).
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; JQ707941; AFK14046.1; -; Genomic_DNA.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..125
FT /note="Geminivirus AL1 replication-associated protein
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00799"
FT DOMAIN 151..225
FT /note="Geminivirus AL1 replication-associated protein
FT central"
FT /evidence="ECO:0000259|Pfam:PF08283"
FT REGION 273..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-1"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 75
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 77
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
FT BINDING 124
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR601191-2"
SQ SEQUENCE 302 AA; 35183 MW; 30D207EE789FC08E CRC64;
MPRAPNRNRP TPNQPGYLRF QKKNAFLTYS QIGGDFKDYI FEKLKTLLES YVILFLAVSL
EHHQPTEEQS EGGFHTHCSI QRDKKLDVNG NLFFSIILPD GRTIHPRIDG LNAPKRAFEY
ITKEDTSPRT FGELRLGGRS PNSIGNSNVE WRRILDSSNT KEEFFSNIRE SCPTDFVLRW
PSILSFANYH FRPVVQPYTP RWTEFSRLPD PIKEWAEQNI YFVSSDCLHY EICENCRGAI
LQDREMTLEE YFHLDRLSRD LACSEDTNIL NFSRSQTTDQ SDQEVSTYAD HPEQERPSGQ
DL
//
