NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/viro.1998.9324; PubMed=9791035 [NCBI, ExPASy, EBI, Israel, Japan]
Bassami M.R., Berryman D., Wilcox G.E., Raidal S.R.;
"Psittacine beak and feather disease virus nucleotide sequence analysis and its relationship to porcine circovirus, plant circoviruses, and chicken anaemia virus.";
Virology 249:453-459(1998).

Comments

FUNCTION: 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).
CATALYTIC ACTIVITY: ATP + H₂O = ADP + phosphate.
COFACTOR: Divalent metal cations, possibly magnesium or manganese (By similarity).
SUBCELLULAR LOCATION: Nucleus (Potential).
DOMAIN: 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.
SIMILARITY: Belongs to the nanoviruses/circoviruses replication-associated protein family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF080560; AAC69861.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9YUD3.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042624;	Molecular function: ATPase activity, uncoupled (inferred from electronic annotation from EC).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004519;	Molecular function: endonuclease activity (inferred from electronic annotation from UniProtKB-KW).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016779;	Molecular function: nucleotidyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0003724;	Molecular function: RNA helicase activity (inferred from electronic annotation from InterPro).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from UniProtKB-KW).
GO:0018142;	Biological process: DNA-protein covalent cross-linking (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR003365; Viral_rep_N.
Graphical view of domain structure.

Pfam

PF00910; RNA_helicase; 1.
PF02407; Viral_Rep; 1.
Pfam graphical view of domain structure.

ProtoNet

Q9YUD3.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Covalent protein-DNA linkage; DNA replication; DNA-binding; Endonuclease; Helicase; Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 289`	`289`	`Replication-associated protein.`	`PRO_0000319862`
`NP_BIND`	`170 172`	`3`	`ATP (By similarity).`
`MOTIF`	`14 17`	`4`	`RCR-1 (By similarity).`
`MOTIF`	`51 56`	`6`	`RCR-2 (By similarity).`
`MOTIF`	`60 80`	`21`	`Nuclear localization signal (Potential).`
`MOTIF`	`89 92`	`4`	`RCR-3 (By similarity).`
`MOTIF`	`103 109`	`7`	`Nuclear localization signal (Potential).`
`ACT_SITE`	`89 89`		`For DNA cleavage activity (By similarity).`
`METAL`	`43 43`		`Divalent metal cation (Potential).`
`METAL`	`51 51`		`Divalent metal cation (Potential).`
`METAL`	`93 93`		`Divalent metal cation (Potential).`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 33446 Da [This is the MW of the unprocessed precursor]

CRC64: A52614012B831791 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSKEGSGCR RWCFTLNNPT DGEIEFVRSL GPDEFYYAIV GREKGEQGTP HLQGYFHFKN 

        70         80         90        100        110        120 
KKRLSALKKL LPRAHFERAK GSDADNEKYC SKEGDVILTL GIVARDGHRA FDGAVAAVMS 

       130        140        150        160        170        180 
GRKMKEVARE FPEVYVRHGR GLHNLSLLVG SSPRDFKTEV DVIYGPPGCG KSRWANEQPG 

       190        200        210        220        230        240 
TKYYKMRGEW WDGYDGEDVV VLDDFYGWLP YCEMLRLCDR YPHKVPVKGA FVEFTSKRII 

       250        260        270        280 
ITSNKPPETW YKEDCDPKPL FRRFTRVWWY NVDKLEQVRP DFLAHPINY

Q9YUD3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools