NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1099/vir.0.79778-0; PubMed=14993650 [NCBI, ExPASy, EBI, Israel, Japan]
Tomioka Y., Ochiai K., Ohashi K., Ono E., Toyoda T., Kimura T., Umemura T.;
"Genome sequence analysis of the avian retrovirus causing so-called fowl glioma and the promoter activity of the long terminal repeat.";
J. Gen. Virol. 85:647-652(2004).

Comments

FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-phosphomonoester.
COFACTOR: Binds 8 manganese or magnesium ions per integrase homotetramer (By similarity).
SUBUNIT: The integrase forms a homotetramer. The reverse transcriptase forms a heterodimer of alpha and beta subunits (By similarity).
DOMAIN: The integrase is composed of three domains. The N-terminal domain is a zinc binding domain. The central domain is the catalytic domain. The C-terminal domain is a non-specific DNA binding domain (By similarity).
PTM: Specific enzymatic cleavages in vivo yield mature proteins. The pol-derived portion of gag-pol precursor is processed to yield the reverse transcriptase beta subunit, which in turn is processed to yield the reverse transcriptase alpha subunit and the integrase (By similarity).
MISCELLANEOUS: This protein is synthesized as a Gag-Pol polyprotein.
SIMILARITY: Contains 1 integrase catalytic domain.
SIMILARITY: Contains 1 integrase-type DNA-binding domain.
SIMILARITY: Contains 1 integrase-type zinc finger.
SIMILARITY: Contains 1 reverse transcriptase domain.
SIMILARITY: Contains 1 RNase H 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

AB112960; BAC78443.1; -; Genomic_RNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q7SQ98; 621-842.

ModBase

Q7SQ98.

Ontologies

GO:0003887;	Molecular function: DNA-directed DNA polymerase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from UniProtKB-KW).
GO:0032196;	Biological process: transposition (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000477; DNA_pol_RVTase.
IPR001037; Integrase_C_retrovir.
IPR001584; Integrase_cat-core.
IPR003308; Integrase_Zn-bd_dom_N.
IPR002156; RNase_H.
IPR010661; RVT_thumb.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.30.10; Integrase_C; 1.

Pfam

PF00552; Integrase; 1.
PF02022; Integrase_Zn; 1.
PF00075; RnaseH; 1.
PF00665; rve; 1.
PF00078; RVT_1; 1.
PF06817; RVT_thumb; 1.
Pfam graphical view of domain structure.

PROSITE

PS50994; INTEGRASE; 1.
PS51027; INTEGRASE_DBD; 1.
PS50879; RNASE_H; 1.
PS50878; RT_POL; 1.
PS50876; ZF_INTEGRASE; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

DNA integration; DNA recombination; DNA-binding; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 572`	`572`	`Reverse transcriptase/ribonuclease H (Potential).`	`PRO_0000040978`
`CHAIN`	`573 895`	`323`	`Integrase (Potential).`	`PRO_0000040979`
`DOMAIN`	`42 230`	`189`	`Reverse transcriptase.`
`DOMAIN`	`441 572`	`132`	`RNase H.`
`DOMAIN`	`625 788`	`164`	`Integrase catalytic.`
`ZN_FING`	`573 613`	`41`	`Integrase-type.`
`DNA_BIND`	`794 842`	`49`	`Integrase-type.`
`METAL`	`636 636`		`Magnesium; catalytic; for integrase activity (By similarity).`
`METAL`	`693 693`		`Magnesium; catalytic; for integrase activity (By similarity).`
`METAL`	`729 729`		`Magnesium; catalytic; for integrase activity (By similarity).`

Sequence information

Length: 895 AA [This is the length of the unprocessed precursor]

Molecular weight: 98588 Da [This is the MW of the unprocessed precursor]

CRC64: 768028C3E5830073 [This is a checksum on the sequence]

        10         20         30         40         50         60 
TVALHLAIPL KWKPDHTPVW IDQWPLPEGK LVALTQLVEK ELQLGHIEPS LSCWNTPVFV 

        70         80         90        100        110        120 
IRKASGSYRL LHDLRAVNAK LVPFGAVQQG APVLSALPRG WPLMVLDLKD CFFSIPLAEQ 

       130        140        150        160        170        180 
DREAFAFTLP SVNNQAPARR FQWKVLPQGM TCSPTICQLV VGQVLEPLRL KHPSLRMLHY 

       190        200        210        220        230        240 
MDDLLLAASS HDGLEAAGEE VISTLERAGF TISPDKIQRE PGVQYLGYKL GSTYVAPVGL 

       250        260        270        280        290        300 
VAEPRIATLW DVQKLVGSLQ WLRPALGIPP RLMGPFYEQL RGSDPNEARE WNLDMKMAWR 

       310        320        330        340        350        360 
EIVQLSTTAA LERWDPALPL EGAVARCEQG AIGVLGQGLS THPRPCLWLF STQPTKAFTA 

       370        380        390        400        410        420 
WLEVLTLLIT KLRASAVRTF GKEVDILLLP ACFREDLPLP EGILLALKGF AGKIRSSDTP 

       430        440        450        460        470        480 
SIFDIARPLH VSLKVRVTDH PVPGPTVFTD ASSSTHKGVV VWREGPRWEI KEIADSGASV 

       490        500        510        520        530        540 
QQLEARAVAM ALLLWPTTPT NVVTDSAFVA KMLLKMGQEG VPSTAAAFIL EDALSQRSAM 

       550        560        570        580        590        600 
AAVLHVRSHS EVPGFFTEGN DVADSQATFQ AYPLREAKDL HTALHIGPRA LSKACNISMQ 

       610        620        630        640        650        660 
QAREVVQTCP HCNSAPALEA GVNPRGLGPL QIWQTDFTLE PRMAPRSWLA VTVDTASSAI 

       670        680        690        700        710        720 
VVTQHGRVTS VAAQHHWATA IAVLGRPKAI KTDNGSCFTS KSTREWLARW GIAHTTGIPG 

       730        740        750        760        770        780 
NSQGQAMVER ANRLLKDKIR VLAEGDGFMK RIPTSKQGEL LAKAMYALNH FERGENTKTP 

       790        800        810        820        830        840 
IQKHWRPTVL TEGPPVKIRI ETGEWEKGWN VLVWGRGYAA VKNRDTDKVI WVPSRKVKPD 

       850        860        870        880        890 
ITQKDEVTKK DEASPLFAGI SDWAPWKGEQ EGLQEEVASN KQERPGEDTL AANES

Q7SQ98 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