ID   REP40_AAV2S             Reviewed;         312 AA.
AC   Q89269; Q77XY0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein Rep40;
DE            EC=3.6.4.12;
GN   Name=Rep40;
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=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).
RN   [6]
RP   FUNCTION.
RX   PubMed=12824181; DOI=10.1074/jbc.m301537200;
RA   Collaco R.F., Kalman-Maltese V., Smith A.D., Dignam J.D., Trempe J.P.;
RT   "A biochemical characterization of the adeno-associated virus Rep40
RT   helicase.";
RL   J. Biol. Chem. 278:34011-34017(2003).
RN   [7]
RP   SUBUNIT.
RX   PubMed=17209567; DOI=10.1021/bi061762v;
RA   Dignam S.S., Collaco R.F., Bieszczad J., Needham P., Trempe J.P.,
RA   Dignam J.D.;
RT   "Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase.";
RL   Biochemistry 46:568-576(2007).
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 of viral DNA with Rep40.
CC       {ECO:0000269|PubMed:11406604, ECO:0000269|PubMed:12824181}.
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; EC=3.6.4.12;
CC   -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:17209567}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:1370086}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF043303; AAC03776.1; -; Genomic_DNA.
DR   EMBL; J01901; AAA42373.1; -; Genomic_DNA.
DR   RefSeq; YP_680424.1; NC_001401.2.
DR   SMR; Q89269; -.
DR   IntAct; Q89269; 1.
DR   GeneID; 4192014; -.
DR   KEGG; vg:4192014; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="Protein Rep40"
FT                   /id="PRO_0000428951"
FT   DOMAIN          84..239
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   REGION          264..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..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   312 AA;  34965 MW;  9465A291F2B044F0 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
     NYADRLARGH SL