[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8383793 [NCBI, ExPASy, EBI, Israel, Japan] Burke W.D., Eickbush D.G., Xiong Y., Jakubczak J.L., Eickbush T.H.; "Sequence relationship of retrotransposable elements R1 and R2 within and between divergent insect species."; Mol. Biol. Evol. 10:163-185(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-323. PubMed=1849649 [NCBI, ExPASy, EBI, Israel, Japan] Jakubczak J.L., Burke W.D., Eickbush T.H.; "Retrotransposable elements R1 and R2 interrupt the rRNA genes of most insects."; Proc. Natl. Acad. Sci. U.S.A. 88:3295-3299(1991).

Comments

CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
SIMILARITY: Contains 1 reverse transcriptase domain.

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

L00942; AAA30339.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D44490; D44490.

3D structure databases

ModBase

Q03271.

Ontologies

GO:0004519;	Molecular function: endonuclease activity (inferred from electronic annotation from UniProtKB-KW).
GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0003964;	Molecular function: RNA-directed DNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0006278;	Biological process: RNA-dependent DNA replication (inferred from electronic annotation from InterPro).
GO:0032196;	Biological process: transposition (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000477; DNA_pol_RVTase.
IPR015706; Reverse_transcriptase-related.
Graphical view of domain structure.

PANTHER

PTHR19446; Rev_txptase; 1.

PROSITE

PS50878; RT_POL; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q03271.

Other

UniRef

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

Keywords

Endonuclease; Hydrolase; Nuclease; Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase; Transposable element.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 383`	`>383`	`Retrovirus-related Pol polyprotein from type-1 retrotransposable element R1 3.`	`PRO_0000058495`
`DOMAIN`	`<1 88`	`>88`	`Reverse transcriptase.`
`REGION`	`229 383`	`155`	`Nucleic acid-binding endonuclease.`
`NON_TER`	`1 1`

Sequence information

Length: 383 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 43411 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: DE296B380925251B [This is a checksum on the sequence]

        10         20         30         40         50         60 
VDAFADDLLL LVQGNRRNEL EQSASEALSV VYRYGTNIGV EVSDSKTVCM MLKGSLNMLN 

        70         80         90        100        110        120 
RVVHVSTNGM DDKRIRCVDR VRYLGVNVGI GMDFSVHIDG MKRRLTTAIM RLRGVLRKSW 

       130        140        150        160        170        180 
GLKRGVVSMV VKGLFLPAVM YGASVWYEQL HKRKLRGSRR LSEELVSCQR VVLYACTRVC 

       190        200        210        220        230        240 
RTVSTEAMQI LFGSLPWDIE CFRRANCTKS KGPAMNESDL VTDEDLYELS LHECRELVDQ 

       250        260        270        280        290        300 
RALAAWQDRW EATSNGRVTY EWIRDVGFSG RSMKYFGAEP EGLLRLTGHG SMNSFLFSRN 

       310        320        330        340        350        360 
LSNSPACACG TEREDWIHVL CECDMYAAFR DLDSIGVRRT EVGWDVSGVL LDRASMSVCV 

       370        380 
PLSSCAFRMR ELIVQRMREN EES

Q03271 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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