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Database: UniProt
Entry: T1YSH3_9VIRU
LinkDB: T1YSH3_9VIRU
Original site: T1YSH3_9VIRU 
ID   T1YSH3_9VIRU            Unreviewed;       339 AA.
AC   T1YSH3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531};
OS   Blackbird associated gemycircularvirus 1.
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Genomoviridae; Gemycircularvirus; Gemycircularvirus blabi1.
OX   NCBI_TaxID=1985371 {ECO:0000313|EMBL:AGU67673.1, ECO:0000313|Proteomes:UP000122601};
RN   [1] {ECO:0000313|EMBL:AGU67673.1, ECO:0000313|Proteomes:UP000122601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=As41 {ECO:0000313|EMBL:AGU67673.1};
RX   PubMed=23994297; DOI=10.1016/j.virusres.2013.08.008;
RA   Sikorski A., Massaro M., Kraberger S., Young L.M., Smalley D., Martin D.P.,
RA   Varsani A.;
RT   "Novel myco-like DNA viruses discovered in the faecal matter of various
RT   animals.";
RL   Virus Res. 177:209-216(2013).
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the geminiviridae Rep protein family.
CC       {ECO:0000256|ARBA:ARBA00006240}.
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DR   EMBL; KF371643; AGU67673.1; -; Genomic_DNA.
DR   OrthoDB; 9195at10239; -.
DR   Proteomes; UP000122601; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001301; Gemini_AL1_CLV.
DR   InterPro; IPR022690; Gemini_AL1_REP_cat-dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00799; Gemini_AL1; 1.
DR   PRINTS; PR00228; GEMCOATCLVL1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   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          16..106
FT                   /note="Geminivirus AL1 replication-associated protein
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00799"
SQ   SEQUENCE   339 AA;  38224 MW;  4806BBBFE288345B CRC64;
     MPPKQKPPYA NFRYALLTYA QCGDLDAWAV NDHMAFLGAE CIIGRELHAD GGTHLHAFVD
     FSRRFRSRRS DVFDVGGRHP NLVPSYGSPE GGFDYAIKDG DVVAGGLSRP SGRGVYEDVS
     SWSIVVGQKS EGDFWECVAR LDPRSLCTNY NSLRAYANWK YKPVPVRYEH PAGVEFELGM
     VPELAVWREI ALGANRERGI LVIYGDTRLG KTLWSRSLGN HIYTIGQMSG EVILRDQADA
     EYAVFDDMRG GLEFFHGWKE WFGCQNVVTV KKLYKDPVQM PWGRPVIWLA NRDPREELRD
     GVTQHTSMGK QAAIEGDIKW LDGNCIFVEL DHAIFRAST
//
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