ID   REP52_AAV2S             Reviewed;         397 AA.
AC   Q89270; Q77XX9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein Rep52;
GN   Name=Rep52;
OS   Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Parvovirinae; Dependoparvovirus.
OX   NCBI_TaxID=648242;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6300419; DOI=10.1128/jvi.45.2.555-564.1983;
RA   Srivastava A., Lusby E.W., Berns K.I.;
RT   "Nucleotide sequence and organization of the adeno-associated virus 2
RT   genome.";
RL   J. Virol. 45:555-564(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7996133; DOI=10.1099/0022-1317-75-12-3385;
RA   Ruffing M., Heid H., Kleinschmidt J.A.;
RT   "Mutations in the carboxy terminus of adeno-associated virus 2 capsid
RT   proteins affect viral infectivity: lack of an RGD integrin-binding motif.";
RL   J. Gen. Virol. 75:3385-3392(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Berns K.I., Bohenzky R.A., Cassinotti P., Colvin D., Donahue B.A., Dull T.,
RA   Horer M., Kleinschmidt J.A., Ruffing M., Snyder R.O., Tratschin J.-D.,
RA   Weitz M.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1370086; DOI=10.1128/jvi.66.1.317-324.1992;
RA   Hunter L.A., Samulski R.J.;
RT   "Colocalization of adeno-associated virus Rep and capsid proteins in the
RT   nuclei of infected cells.";
RL   J. Virol. 66:317-324(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=9573254; DOI=10.1128/jvi.72.6.4874-4881.1998;
RA   Smith R.H., Kotin R.M.;
RT   "The Rep52 gene product of adeno-associated virus is a DNA helicase with
RT   3'-to-5' polarity.";
RL   J. Virol. 72:4874-4881(1998).
RN   [6]
RP   INTERACTION WITH HOST PRKX.
RX   PubMed=9742109; DOI=10.1128/mcb.18.10.5921;
RA   Chiorini J.A., Zimmermann B., Yang L., Smith R.H., Ahearn A., Herberg F.,
RA   Kotin R.M.;
RT   "Inhibition of PrKX, a novel protein kinase, and the cyclic AMP-dependent
RT   protein kinase PKA by the regulatory proteins of adeno-associated virus
RT   type 2.";
RL   Mol. Cell. Biol. 18:5921-5929(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=11406604; DOI=10.1093/emboj/20.12.3282;
RA   King J.A., Dubielzig R., Grimm D., Kleinschmidt J.A.;
RT   "DNA helicase-mediated packaging of adeno-associated virus type 2 genomes
RT   into preformed capsids.";
RL   EMBO J. 20:3282-3291(2001).
CC   -!- FUNCTION: Plays a critical role during packaging of viral DNA into
CC       empty capsids, where they are thought to be part of the packaging motor
CC       complex. The single stranded genomic DNA is packaged in a 3' to 5'
CC       direction and requires the association between viral DNA and Rep40.
CC       Regulates host PKA activity by interacting with host PRKX as a
CC       mechanism to interfere with helper virus propagation and to promote its
CC       own replication. {ECO:0000269|PubMed:11406604,
CC       ECO:0000269|PubMed:9573254}.
CC   -!- SUBUNIT: Homooligomer. Interacts with host PRKX.
CC       {ECO:0000269|PubMed:9742109}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:1370086}.
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DR   EMBL; J01901; AAA42375.1; -; Genomic_DNA.
DR   EMBL; AF043303; AAC03777.1; -; Genomic_DNA.
DR   RefSeq; YP_680425.1; NC_001401.2.
DR   SMR; Q89270; -.
DR   DNASU; 1489607; -.
DR   GeneID; 1489607; -.
DR   KEGG; vg:1489607; -.
DR   Proteomes; UP000008469; Genome.
DR   Proteomes; UP000180764; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001257; Parvovirus_NS1_helicase.
DR   Pfam; PF01057; Parvo_NS1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51206; SF3_HELICASE_1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA replication; Host nucleus; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..397
FT                   /note="Protein Rep52"
FT                   /id="PRO_0000428952"
FT   DOMAIN          84..239
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   REGION          265..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ   SEQUENCE   397 AA;  44774 MW;  95763A5A51E408F7 CRC64;
     MELVGWLVDK GITSEKQWIQ EDQASYISFN AASNSRSQIK AALDNAGKIM SLTKTAPDYL
     VGQQPVEDIS SNRIYKILEL NGYDPQYAAS VFLGWATKKF GKRNTIWLFG PATTGKTNIA
     EAIAHTVPFY GCVNWTNENF PFNDCVDKMV IWWEEGKMTA KVVESAKAIL GGSKVRVDQK
     CKSSAQIDPT PVIVTSNTNM CAVIDGNSTT FEHQQPLQDR MFKFELTRRL DHDFGKVTKQ
     EVKDFFRWAK DHVVEVEHEF YVKKGGAKKR PAPSDADISE PKRVRESVAQ PSTSDAEASI
     NYADRYQNKC SRHVGMNLML FPCRQCERMN QNSNICFTHG QKDCLECFPV SESQPVSVVK
     KAYQKLCYIH HIMGKVPDAC TACDLVNVDL DDCIFEQ