Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein Rep68

Gene

Rep68

Organism
Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Plays also a role as transcriptional regulator, DNA helicase and as key factor in site-specific integration of the viral genome. Inhibits the host cell cycle G1/S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi334 – 3418ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA replication, G1/S host cell cycle checkpoint dysregulation by virus, Host G2/M cell cycle arrest by virus, Host-virus interaction, Modulation of host cell cycle by virus, Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membrane, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Rep68 (EC:3.6.4.12)
Gene namesi
Name:Rep68
OrganismiAdeno-associated virus 2 (isolate Srivastava/1982) (AAV-2)
Taxonomic identifieri648242 [NCBI]
Taxonomic lineageiVirusesssDNA virusesParvoviridaeParvovirinaeDependoparvovirus
Virus hostiMammalia [TaxID: 40674]
Proteomesi
  • UP000008469 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Protein Rep68PRO_0000222474Add
BLAST

Interactioni

Subunit structurei

Interacts with host TOPORS. Interacts with host KCTD5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E2P031202EBI-7387242,EBI-1779322From a different organism.
KCTD5Q9NXV23EBI-7387242,EBI-1056857From a different organism.
SUB1P539993EBI-7387242,EBI-998260From a different organism.
TOPORSQ9NS563EBI-7387242,EBI-1996473From a different organism.

Protein-protein interaction databases

IntActiP03132. 4 interactions.
MINTiMINT-6732280.

Structurei

Secondary structure

1
536
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Helixi15 – 184Combined sources
Helixi24 – 329Combined sources
Helixi45 – 473Combined sources
Helixi50 – 7122Combined sources
Beta strandi78 – 847Combined sources
Beta strandi89 – 968Combined sources
Helixi102 – 1043Combined sources
Helixi105 – 11915Combined sources
Turni120 – 1234Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi136 – 1405Combined sources
Helixi152 – 1565Combined sources
Turni157 – 1593Combined sources
Turni162 – 1643Combined sources
Beta strandi165 – 1706Combined sources
Helixi173 – 1753Combined sources
Turni176 – 1805Combined sources
Helixi182 – 20423Combined sources
Helixi225 – 23410Combined sources
Helixi239 – 25416Combined sources
Helixi260 – 27718Combined sources
Helixi280 – 2845Combined sources
Helixi293 – 2953Combined sources
Helixi297 – 3048Combined sources
Helixi309 – 32012Combined sources
Turni322 – 3265Combined sources
Beta strandi329 – 3335Combined sources
Helixi340 – 35011Combined sources
Beta strandi354 – 3563Combined sources
Turni360 – 3634Combined sources
Helixi367 – 3693Combined sources
Beta strandi373 – 3775Combined sources
Turni384 – 3863Combined sources
Helixi387 – 3948Combined sources
Beta strandi399 – 4013Combined sources
Turni404 – 4063Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi416 – 4227Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi432 – 4343Combined sources
Helixi438 – 4425Combined sources
Beta strandi445 – 4495Combined sources
Helixi463 – 47513Combined sources
Beta strandi483 – 4853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9HX-ray2.40A/B/C225-490[»]
1U0JX-ray2.10A225-490[»]
4ZO0X-ray2.30A/B/C1-206[»]
4ZQ9X-ray2.60A/B/C1-208[»]
5DCXX-ray2.60A/B/C/D/E/F/G/H/I/J/K1-224[»]
ProteinModelPortaliP03132.
SMRiP03132. Positions 1-198, 225-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 463156SF3 helicasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR001257. Parvovirus_NS1_helicase.
IPR014835. Rep_N.
[Graphical view]
PfamiPF01057. Parvo_NS1. 1 hit.
PF08724. Rep_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGFYEIVIK VPSDLDGHLP GISDSFVNWV AEKEWELPPD SDMDLNLIEQ
60 70 80 90 100
APLTVAEKLQ RDFLTEWRRV SKAPEALFFV QFEKGESYFH MHVLVETTGV
110 120 130 140 150
KSMVLGRFLS QIREKLIQRI YRGIEPTLPN WFAVTKTRNG AGGGNKVVDE
160 170 180 190 200
CYIPNYLLPK TQPELQWAWT NMEQYLSACL NLTERKRLVA QHLTHVSQTQ
210 220 230 240 250
EQNKENQNPN SDAPVIRSKT SARYMELVGW LVDKGITSEK QWIQEDQASY
260 270 280 290 300
ISFNAASNSR SQIKAALDNA GKIMSLTKTA PDYLVGQQPV EDISSNRIYK
310 320 330 340 350
ILELNGYDPQ YAASVFLGWA TKKFGKRNTI WLFGPATTGK TNIAEAIAHT
360 370 380 390 400
VPFYGCVNWT NENFPFNDCV DKMVIWWEEG KMTAKVVESA KAILGGSKVR
410 420 430 440 450
VDQKCKSSAQ IDPTPVIVTS NTNMCAVIDG NSTTFEHQQP LQDRMFKFEL
460 470 480 490 500
TRRLDHDFGK VTKQEVKDFF RWAKDHVVEV EHEFYVKKGG AKKRPAPSDA
510 520 530
DISEPKRVRE SVAQPSTSDA EASINYADRL ARGHSL
Length:536
Mass (Da):60,754
Last modified:July 21, 1986 - v1
Checksum:i7C1ECDD4E07703C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171G → E in AAC03774 (PubMed:7996133).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01901 Genomic DNA. Translation: AAA42372.1.
AF043303 Genomic DNA. Translation: AAC03774.1.
PIRiA03694. UYAD1A.
RefSeqiYP_680422.1. NC_001401.2.

Genome annotation databases

GeneIDi4192013.
KEGGivg:4192013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01901 Genomic DNA. Translation: AAA42372.1.
AF043303 Genomic DNA. Translation: AAC03774.1.
PIRiA03694. UYAD1A.
RefSeqiYP_680422.1. NC_001401.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9HX-ray2.40A/B/C225-490[»]
1U0JX-ray2.10A225-490[»]
4ZO0X-ray2.30A/B/C1-206[»]
4ZQ9X-ray2.60A/B/C1-208[»]
5DCXX-ray2.60A/B/C/D/E/F/G/H/I/J/K1-224[»]
ProteinModelPortaliP03132.
SMRiP03132. Positions 1-198, 225-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03132. 4 interactions.
MINTiMINT-6732280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4192013.
KEGGivg:4192013.

Miscellaneous databases

EvolutionaryTraceiP03132.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR001257. Parvovirus_NS1_helicase.
IPR014835. Rep_N.
[Graphical view]
PfamiPF01057. Parvo_NS1. 1 hit.
PF08724. Rep_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence and organization of the adeno-associated virus 2 genome."
    Srivastava A., Lusby E.W., Berns K.I.
    J. Virol. 45:555-564(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutations in the carboxy terminus of adeno-associated virus 2 capsid proteins affect viral infectivity: lack of an RGD integrin-binding motif."
    Ruffing M., Heid H., Kleinschmidt J.A.
    J. Gen. Virol. 75:3385-3392(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Colocalization of adeno-associated virus Rep and capsid proteins in the nuclei of infected cells."
    Hunter L.A., Samulski R.J.
    J. Virol. 66:317-324(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Biochemical characterization of adeno-associated virus rep68 DNA helicase and ATPase activities."
    Zhou X., Zolotukhin I., Im D.S., Muzyczka N.
    J. Virol. 73:1580-1590(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The adeno-associated virus type 2 regulatory proteins rep78 and rep68 interact with the transcriptional coactivator PC4."
    Weger S., Wendland M., Kleinschmidt J.A., Heilbronn R.
    J. Virol. 73:260-269(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST SUB1/PC4.
  7. "Topors, a p53 and topoisomerase I binding protein, interacts with the adeno-associated virus (AAV-2) Rep78/68 proteins and enhances AAV-2 gene expression."
    Weger S., Hammer E., Heilbronn R.
    J. Gen. Virol. 83:511-516(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST TOPORS.
  8. "Identification of a cytoplasmic interaction partner of the large regulatory proteins Rep78/Rep68 of adeno-associated virus type 2 (AAV-2)."
    Weger S., Hammer E., Goetz A., Heilbronn R.
    Virology 362:192-206(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCTD5.
  9. "Crystal structure of the SF3 helicase from adeno-associated virus type 2."
    James J.A., Escalante C.R., Yoon-Robarts M., Edwards T.A., Linden R.M., Aggarwal A.K.
    Structure 11:1025-1035(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 225-490.
  10. "Structure of adeno-associated virus type 2 Rep40-ADP complex: insight into nucleotide recognition and catalysis by superfamily 3 helicases."
    James J.A., Aggarwal A.K., Linden R.M., Escalante C.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:12455-12460(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-490.

Entry informationi

Entry nameiREP68_AAV2S
AccessioniPrimary (citable) accession number: P03132
Secondary accession number(s): O56650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.