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P05400

- POL_CERV

UniProt

P05400 - POL_CERV

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Protein

Enzymatic polyprotein

Gene
ORF V
Organism
Carnation etched ring virus (CERV)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated, and reverse-transcribed inside the nucleocapsid. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA) By similarity.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. endonuclease activity Source: UniProtKB-KW
  3. RNA binding Source: InterPro
  4. RNA-directed DNA polymerase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Protein family/group databases

MEROPSiA03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Enzymatic polyprotein
Including the following 3 domains:
Aspartic protease (EC:3.4.23.-)
Endonuclease
Reverse transcriptase (EC:2.7.7.49)
Gene namesi
ORF Names:ORF V
OrganismiCarnation etched ring virus (CERV)
Taxonomic identifieri10640 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesCaulimoviridaeCaulimovirus
Virus hostiDianthus caryophyllus (Carnation) (Clove pink) [TaxID: 3570]
ProteomesiUP000008446: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Enzymatic polyproteinPRO_0000222055Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP05400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini252 – 436185Reverse transcriptaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 180180Protease By similarityAdd
BLAST

Domaini

The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template By similarity.

Sequence similaritiesi

Family and domain databases

InterProiIPR000588. Pept_A3A.
IPR000477. RT_dom.
[Graphical view]
PfamiPF02160. Peptidase_A3. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]
PRINTSiPR00731. CAULIMOPTASE.
PROSITEiPS50878. RT_POL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05400-1 [UniParc]FASTAAdd to Basket

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MSLRNRTNPN SIYVKGILKF PGYQTNLDLH CYVDTGSSLC MASKYVIPEE    50
YWQTAEKPLN IKIANGKIIQ LTKVCSKLPI RLGGERFLIP TLFQQESGID 100
LLLGNNFCQL YSPFIQYTDR IYFHLNKQSV IIGKITKAYQ YGVKGFLESM 150
KKKSKVNRPE PINITSNQHL FLEEGGNHVD EMLYEIQISK FSAIEEMLER 200
VSSENPIDPE KSKQWMTATI ELIDPKTVVK VKPMSYSPSD REEFDRQIKE 250
LLELKVIKPS KSTHMSPAFL VENEAERRRG KKRMVVNYKA MNKATKGDAH 300
NLPNKDELLT LVRGKKIYSS FDCKSGLWQV LLDKESQLLT AFTCPQGHYQ 350
WNVVPFGLKQ APSIFPKTYA NSHSNQYSKY CCVYVDDILV FSNTGRKEHY 400
IHVLNILRRC EKLGIILSKK KAQLFKEKIN FLGLEIDQGT HCPQNHILEH 450
IHKFPDRIED KKQLQRFLGI LTYASDYIPK LASIRKPLQS KLKEDSTWTW 500
NDTDSQYMAK IKKNLKSFPK LYHPEPNDKL VIETDASEEF WGGILKAIHN 550
SHEYICRYAS GSFKAAERNY HSNEKELLAV IRVIKKFSIY LTPSRFLIRT 600
DNKNFTHFVN INLKGDRKQG RLVRWQMWLS QYDFDVEHIA GTKNVFADFL 650
QENTLTNYV 659
Length:659
Mass (Da):76,517
Last modified:November 1, 1988 - v1
Checksum:i25CC30475E38B3C6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04658 Genomic DNA. Translation: CAA28360.1.
PIRiS00854.
RefSeqiNP_612577.1. NC_003498.1.

Genome annotation databases

GeneIDi935429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04658 Genomic DNA. Translation: CAA28360.1 .
PIRi S00854.
RefSeqi NP_612577.1. NC_003498.1.

3D structure databases

ProteinModelPortali P05400.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi A03.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 935429.

Family and domain databases

InterProi IPR000588. Pept_A3A.
IPR000477. RT_dom.
[Graphical view ]
Pfami PF02160. Peptidase_A3. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view ]
PRINTSi PR00731. CAULIMOPTASE.
PROSITEi PS50878. RT_POL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The sequence of carnation etched ring virus DNA: comparison with cauliflower mosaic virus and retroviruses."
    Hull R., Sadler J., Longstaff M.
    EMBO J. 5:3083-3090(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPOL_CERV
AccessioniPrimary (citable) accession number: P05400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 14, 2014
This is version 75 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

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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