ID L7P648_9CIRC Unreviewed; 351 AA.
AC L7P648;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Replication-associated protein {ECO:0000256|ARBA:ARBA00014531};
DE AltName: Full=ATP-dependent helicase Rep {ECO:0000256|ARBA:ARBA00030754};
DE AltName: Full=RepP {ECO:0000256|ARBA:ARBA00032243};
GN ORFNames=AtCopCV_gp1 {ECO:0000313|EMBL:AFN42891.1};
OS Acartia tonsa copepod circovirus.
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Circovirus.
OX NCBI_TaxID=1168547 {ECO:0000313|EMBL:AFN42891.1, ECO:0000313|Proteomes:UP000165262};
RN [1] {ECO:0000313|EMBL:AFN42891.1, ECO:0000313|Proteomes:UP000165262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154_D11 {ECO:0000313|EMBL:AFN42891.1};
RX PubMed=23297243; DOI=10.1073/pnas.1216595110;
RA Dunlap D.S., Ng T.F., Rosario K., Barbosa J.G., Greco A.M., Breitbart M.,
RA Hewson I.;
RT "Molecular and microscopic evidence of viruses in marine copepods.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1375-1380(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Interacts with the capsid protein; this interaction relocates
CC Rep into the nucleus. {ECO:0000256|ARBA:ARBA00011448}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the nanoviruses/circoviruses replication-
CC associated protein family. {ECO:0000256|ARBA:ARBA00008545}.
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DR EMBL; JQ837277; AFN42891.1; -; Genomic_DNA.
DR RefSeq; YP_007353980.1; NC_020099.1.
DR GeneID; 14445251; -.
DR KEGG; vg:14445251; -.
DR OrthoDB; 9195at10239; -.
DR Proteomes; UP000165262; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.40.1310.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003365; Viral_rep_N.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF02407; Viral_Rep; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Reference proteome {ECO:0000313|Proteomes:UP000165262}.
FT DOMAIN 44..146
FT /note="Viral replication-associated protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02407"
FT DOMAIN 216..302
FT /note="Helicase superfamily 3 single-stranded DNA/RNA
FT virus"
FT /evidence="ECO:0000259|Pfam:PF00910"
FT REGION 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 40411 MW; 1FB4CCC32D9A510C CRC64;
MKSLHISKIE FSQWPQSIKP RAKRAVGIFS LTKMPSNATT NRARGWCFTL NNPPPEMISE
RRVVVPGHVS GLDAAIPTEP NLPEHRHCDY RVGQLERGDN GTLHIQGYYH HRVMKSFNQM
KKLIPNAHWE IAKGSPKQNR DYCTKEDTRV PDTRPFEEGE CPHQGTRFDL RQCADVLANG
GSLLDLPGEM VIRYHRGFSA YRSLFHKRRQ EAPTVLWIYG PTGSGKSRFA STLRDECYWK
PPGKWFDGYD QEPLVILDDY RSEWAEWGVF GQLLRLLDRY PLMVEYKGGS VQFCSELIVI
TCDRPPSELW FSQGDIGQLT RRISHVIHAV GMWLPVEPAV HESIKRRDNI E
//
