P05400 (POL_CERV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enzymatic polyprotein

Including the following 3 domains:

1. Aspartic protease
   EC=3.4.23.-
2. Endonuclease
3. Reverse transcriptase
   EC=2.7.7.49

Gene names

ORF Names:

ORF V

Organism

Carnation etched ring virus (CERV) [Complete proteome]

Taxonomic identifier

10640 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Caulimoviridae › Caulimovirus

Virus host

Dianthus caryophyllus (Carnation) (Clove pink) [TaxID: 3570]

Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Domain	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 similarities	Belongs to the caulimoviridae enzymatic polyprotein family. Contains 1 peptidase A3A domain. Contains 1 reverse transcriptase domain.

Ontologies

Keywords
Molecular function	Aspartyl protease Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 659	659	Enzymatic polyprotein		PRO_0000222055
Regions
	Domain	252 – 436	185	Reverse transcriptase
	Region	1 – 180	180	Protease By similarity
Sites
	Active site	34	1

Sequences

	Sequence		Length	Mass (Da)
	P05400 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 25CC30475E38B3C6	FASTA	659	76,517
	10 20 30 40 50 60 MSLRNRTNPN SIYVKGILKF PGYQTNLDLH CYVDTGSSLC MASKYVIPEE YWQTAEKPLN 70 80 90 100 110 120 IKIANGKIIQ LTKVCSKLPI RLGGERFLIP TLFQQESGID LLLGNNFCQL YSPFIQYTDR 130 140 150 160 170 180 IYFHLNKQSV IIGKITKAYQ YGVKGFLESM KKKSKVNRPE PINITSNQHL FLEEGGNHVD 190 200 210 220 230 240 EMLYEIQISK FSAIEEMLER VSSENPIDPE KSKQWMTATI ELIDPKTVVK VKPMSYSPSD 250 260 270 280 290 300 REEFDRQIKE LLELKVIKPS KSTHMSPAFL VENEAERRRG KKRMVVNYKA MNKATKGDAH 310 320 330 340 350 360 NLPNKDELLT LVRGKKIYSS FDCKSGLWQV LLDKESQLLT AFTCPQGHYQ WNVVPFGLKQ 370 380 390 400 410 420 APSIFPKTYA NSHSNQYSKY CCVYVDDILV FSNTGRKEHY IHVLNILRRC EKLGIILSKK 430 440 450 460 470 480 KAQLFKEKIN FLGLEIDQGT HCPQNHILEH IHKFPDRIED KKQLQRFLGI LTYASDYIPK 490 500 510 520 530 540 LASIRKPLQS KLKEDSTWTW NDTDSQYMAK IKKNLKSFPK LYHPEPNDKL VIETDASEEF 550 560 570 580 590 600 WGGILKAIHN SHEYICRYAS GSFKAAERNY HSNEKELLAV IRVIKKFSIY LTPSRFLIRT 610 620 630 640 650 DNKNFTHFVN INLKGDRKQG RLVRWQMWLS QYDFDVEHIA GTKNVFADFL QENTLTNYV

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04658 Genomic DNA. Translation: CAA28360.1.
PIR	S00854.
RefSeq	NP_612577.1. NC_003498.1.
3D structure databases
ProteinModelPortal	P05400.
ModBase	Search...
Protein family/group databases
MEROPS	A03.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	935429.
Family and domain databases
InterPro	IPR000588. Pept_A3A. IPR000477. RVT. [Graphical view]
Pfam	PF02160. Peptidase_A3. 1 hit. PF00078. RVT_1. 1 hit. [Graphical view]
PRINTS	PR00731. CAULIMOPTASE.
PROSITE	PS00141. ASP_PROTEASE. False negative. PS50878. RT_POL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POL_CERV

Accession

Primary (citable) accession number: P05400

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	July 11, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program