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Q9YUD3

- REP_BFDV

UniProt

Q9YUD3 - REP_BFDV

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Protein

Replication-associated protein

Gene

Rep

Organism
Beak and feather disease virus (BFDV)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities. ATPase activity is probably carried by the isoform Rep (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Divalent metal cations, possibly magnesium or manganese.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Divalent metal cationSequence Analysis
Metal bindingi51 – 511Divalent metal cationSequence Analysis
Active sitei89 – 891For DNA cleavage activityBy similarity
Metal bindingi93 – 931Divalent metal cationSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1728ATPBy similarity

GO - Molecular functioni

  1. ATPase activity, uncoupled Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: UniProtKB-KW
  4. endodeoxyribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. nucleotidyltransferase activity Source: UniProtKB-KW
  7. RNA binding Source: InterPro
  8. RNA helicase activity Source: InterPro

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. protein-DNA covalent cross-linking Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Replication-associated protein (EC:2.7.7.-, EC:3.1.21.-, EC:3.6.1.3)
Alternative name(s):
ATP-dependent helicase Rep
RepP
Gene namesi
Name:Rep
ORF Names:ORF1
OrganismiBeak and feather disease virus (BFDV)
Taxonomic identifieri77856 [NCBI]
Taxonomic lineageiVirusesssDNA virusesCircoviridaeCircovirus
Virus hostiGracula [TaxID: 116991]
Psittaciformes [TaxID: 9223]
ProteomesiUP000007454: Genome

Subcellular locationi

Host nucleus Curated

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Replication-associated proteinPRO_0000319862Add
BLAST

Keywords - PTMi

Covalent protein-DNA linkage

Interactioni

Subunit structurei

Interacts with the capsid protein; this interaction relocates Rep into the nucleus.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9YUD3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 1310Nuclear localization signalSequence Analysis
Motifi14 – 174RCR-1By similarity
Motifi51 – 566RCR-2By similarity
Motifi60 – 8021Nuclear localization signalSequence AnalysisAdd
BLAST
Motifi89 – 924RCR-3By similarity

Domaini

There are 3 rolling circle replication (RCR) motifs. RCR-2 is probably involved in metal coordination. RCR-3 is required for phosphodiester bond cleavage for initiation of RCR.

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR027417. P-loop_NTPase.
IPR003365. Viral_rep_N.
[Graphical view]
PfamiPF00910. RNA_helicase. 1 hit.
PF02407. Viral_Rep. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9YUD3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSKEGSGCR RWCFTLNNPT DGEIEFVRSL GPDEFYYAIV GREKGEQGTP
60 70 80 90 100
HLQGYFHFKN KKRLSALKKL LPRAHFERAK GSDADNEKYC SKEGDVILTL
110 120 130 140 150
GIVARDGHRA FDGAVAAVMS GRKMKEVARE FPEVYVRHGR GLHNLSLLVG
160 170 180 190 200
SSPRDFKTEV DVIYGPPGCG KSRWANEQPG TKYYKMRGEW WDGYDGEDVV
210 220 230 240 250
VLDDFYGWLP YCEMLRLCDR YPHKVPVKGA FVEFTSKRII ITSNKPPETW
260 270 280
YKEDCDPKPL FRRFTRVWWY NVDKLEQVRP DFLAHPINY
Length:289
Mass (Da):33,446
Last modified:May 1, 1999 - v1
Checksum:iA52614012B831791
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF080560 Genomic DNA. Translation: AAC69861.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF080560 Genomic DNA. Translation: AAC69861.1 .

3D structure databases

ProteinModelPortali Q9YUD3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR027417. P-loop_NTPase.
IPR003365. Viral_rep_N.
[Graphical view ]
Pfami PF00910. RNA_helicase. 1 hit.
PF02407. Viral_Rep. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Psittacine beak and feather disease virus nucleotide sequence analysis and its relationship to porcine circovirus, plant circoviruses, and chicken anaemia virus."
    Bassami M.R., Berryman D., Wilcox G.E., Raidal S.R.
    Virology 249:453-459(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The capsid protein of beak and feather disease virus binds to the viral DNA and is responsible for transporting the replication-associated protein into the nucleus."
    Heath L., Williamson A.L., Rybicki E.P.
    J. Virol. 80:7219-7225(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAPSID PROTEIN.

Entry informationi

Entry nameiREP_BFDV
AccessioniPrimary (citable) accession number: Q9YUD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 57 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

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3