Protease
     (Retropepsin)
     (EC 3.4.23.-)
Reverse transcriptase/ribonuclease H
     (RT)
     (EC 2.7.7.49)
     (EC 3.1.26.4)
Integrase
     (IN)

Gene name

Name:

pol

From

Equine infectious anemia virus (isolate CL22) (EIAV)

[TaxID: 31675]

Taxonomy

Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; Lentivirus; Equine lentivirus group.

Virus hosts

Equus asinus (Donkey) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. PubMed=1318398 [NCBI, ExPASy, EBI, Israel, Japan] Perry S.T., Flaherty M.T., Kelley M.J., Clabough D.L., Tronick S.R., Coggins L., Whetter L., Lengel C.R., Fuller F.; "The surface envelope protein gene region of equine infectious anemia virus is not an important determinant of tropism in vitro."; J. Virol. 66:4085-4097(1992).
[2]	3D-STRUCTURE MODELING OF 81-184. DOI=10.1021/bi00064a019; PubMed=8384880 [NCBI, ExPASy, EBI, Israel, Japan] Weber I.T., Tozser J., Wu J., Friedman D., Oroszlan S.; "Molecular model of equine infectious anemia virus proteinase and kinetic measurements for peptide substrates with single amino acid substitutions."; Biochemistry 32:3354-3362(1993).
[3]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-184. PubMed=8844837 [NCBI, ExPASy, EBI, Israel, Japan] Gustchina A., Kervinen J., Powell D.J., Zdanov A., Kay J., Wlodawer A.; "Structure of equine infectious anemia virus proteinase complexed with an inhibitor."; Protein Sci. 5:1453-1465(1996).

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: Endonucleolytic cleavage to 5'-phosphomonoester.
CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
PTM: Specific enzymatic cleavages in vivo yield mature proteins.
SIMILARITY: Belongs to the retroviral Pol polyprotein family.
SIMILARITY: Contains 1 integrase catalytic domain.
SIMILARITY: Contains 1 integrase-type DNA-binding domain.
SIMILARITY: Contains 1 integrase-type zinc finger.
SIMILARITY: Contains 1 peptidase A2 domain [view classification].
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

M87581; AAA43004.1; -; Genomic_RNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B41991; GNLJ22.

3D structure databases

PDB

1EQI; Model; -; A/B=81-184.	[ExPASy / RCSB / EBI]
1FMB; X-ray; 1.80 A; A=81-184.	[ExPASy / RCSB / EBI]
2FMB; X-ray; 1.80 A; A=81-184.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1EQI; -.
1FMB; -.
2FMB; -.

SMR

P32542; 81-184, 742-861.

ModBase

P32542.

Protein family/group databases

MEROPS

A02.004; -.

Ontologies

GO:0004190;	Molecular function: aspartic-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0008907;	Molecular function: integrase activity (inferred from electronic annotation from InterPro).
GO:0004523;	Molecular function: ribonuclease H activity (inferred from electronic annotation from InterPro).
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:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0015074;	Biological process: DNA integration (inferred from electronic annotation from InterPro).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from UniProtKB-KW).
GO:0046080;	Biological process: dUTP metabolic process (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (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

IPR008180; DeoxyUTPase.
IPR000477; DNA_pol_RVTase.
IPR001037; Integrase_C_retrovir.
IPR001584; Integrase_cat-core.
IPR017856; Integrase_Zn-bd_dom-like_N.
IPR003308; Integrase_Zn-bd_dom_N.
IPR001969; Pept_Asp_AS.
IPR009007; Pept_Aspartc_cat.
IPR001995; Peptidase_A2_cat.
IPR002156; RNase_H.
IPR010659; RVT_connect.
IPR010661; RVT_thumb.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.30.10; Integrase_C; 1.
G3DSA:1.10.10.200; Intgrase_N_Zn_bd; 1.
G3DSA:2.40.70.10; Pept_Aspartc_cat; 1.

Pfam

PF00692; dUTPase; 1.
PF00552; Integrase; 1.
PF02022; Integrase_Zn; 1.
PF00075; RnaseH; 1.
PF00665; rve; 1.
PF00077; RVP; 1.
PF00078; RVT_1; 1.
PF06815; RVT_connect; 1.
PF06817; RVT_thumb; 1.
Pfam graphical view of domain structure.

ProDom

PD004900; dCTP_deaminase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS50175; ASP_PROT_RETROV; 1.
PS00141; ASP_PROTEASE; 1.
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

P32542; -.

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

Keywords

3D-structure; Aspartyl protease; Cleavage on pair of basic residues; DNA integration; DNA recombination; Endonuclease; Hydrolase; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protease; RNA-directed DNA polymerase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 195`	`195`	`Protease.`	`PRO_0000038832`
`CHAIN`	`196 914`	`719`	`Reverse transcriptase/ribonuclease H.`	`PRO_0000038833`
`CHAIN`	`915 1146`	`232`	`Integrase.`	`PRO_0000038834`
`DOMAIN`	`100 174`	`75`	`Peptidase A2.`
`DOMAIN`	`230 419`	`190`	`Reverse transcriptase.`
`DOMAIN`	`617 740`	`124`	`RNase H.`
`DOMAIN`	`921 1078`	`158`	`Integrase catalytic.`
`ZN_FING`	`878 919`	`42`	`Integrase-type.`
`DNA_BIND`	`1096 1144`	`49`	`Integrase-type.`
`ACT_SITE`	`105 105`		`By similarity.`
`STRAND`	`85 87`	`3`
`STRAND`	`90 95`	`6`
`STRAND`	`98 104`	`7`
`STRAND`	`112 114`	`3`
`HELIX`	`115 120`	`6`
`STRAND`	`133 135`	`3`
`STRAND`	`138 140`	`3`
`STRAND`	`143 151`	`9`
`STRAND`	`154 164`	`11`
`HELIX`	`172 177`	`6`
`STRAND`	`181 183`	`3`

Sequence information

Length: 1146 AA [This is the length of the unprocessed precursor]

Molecular weight: 129509 Da [This is the MW of the unprocessed precursor]

CRC64: C14058EAF93F3F5D [This is a checksum on the sequence]

        10         20         30         40         50         60 
TAWTFLKAMQ KCSKKREARG SREAPETNFP DTTEESAQQI CCTRDSSDSK SVPRSERNKK 

        70         80         90        100        110        120 
GIQCQGEGSS RGSQPGQFVG VTYNLEKRPT TIVLINDTPL NVLLDTGADT SVLTTAHYNR 

       130        140        150        160        170        180 
LKYRGRKYQG TGIIGVGGNV ETFSTPVTIK KKGRHIKTRM LVADIPVTIL GRDILQDLGA 

       190        200        210        220        230        240 
KLVLAQLSKE IKFRKIELKE GTMGPKIPQW PLTKEKLEGA KEIVQRLLSE GKISEASDNN 

       250        260        270        280        290        300 
PYNSPIFVIK KRSGKWRLLQ DLRELNKTVQ VGTEISRGLP HPGGLIKCKH MTVLDIGDAY 

       310        320        330        340        350        360 
FTIPLDPEFR PYTAFTIPSI NHQEPDKRYV WNCLPQGFVL SPYIYQKTLQ EILQPFRERY 

       370        380        390        400        410        420 
PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILLEKGFE TPDDKLQEVP PYSWLGYQLC 

       430        440        450        460        470        480 
PENWKVQKMQ LDMVKNPTLN DVQKLMGNIT WMSSGVPGLT VKHIAATTKG CLELNQKVIW 

       490        500        510        520        530        540 
TEEAQKELEE NNEKIKNAQG LQYYNPEEEM LCEVEITKNY EATYVIKQSQ GILWAGKKIM 

       550        560        570        580        590        600 
KANKGWSTVK NLMLLLQHVA TESITRVGKC PTFKVPFTKE QVMWEMQKGW YYSWLPEIVY 

       610        620        630        640        650        660 
THQVVHDDWR MKLVEEPTSG ITIYTDGGKQ NGEGIAAYVT SNGRTKQKRL GPVTHQVAER 

       670        680        690        700        710        720 
MAIQMALEDT RDKQVNIVTD SYYCWKNITE GLGLEGPQSP WWPIIQNIRE KEIVYFAWVP 

       730        740        750        760        770        780 
GHKGICGNQL ADEAAKIKEE IMLAYQGTQI KEKRDEDAGF DLCVPYDIMI PVSDTKIIPT 

       790        800        810        820        830        840 
DVKIQVPPNS FGWVTGKSSM AKQGLLINGG IIDEGYTGEI QVICTNIGKS NIKLIEGQKF 

       850        860        870        880        890        900 
AQLIILQHHS NSRQPWDENK ISQRGDKGFG STGVFWVENI QEAQDEHENW HTSPKILARN 

       910        920        930        940        950        960 
YKIPLTVAKQ ITQECPHCTK QGSGPAGCVM RSPNHWQADC THLDNKIILT FVESNSGYIH 

       970        980        990       1000       1010       1020 
ATLLSKENAL CTSLAILEWA RLFSPKSLHT DNGTNFVAEP VVNLLKFLKI AHTTGIPYHP 

      1030       1040       1050       1060       1070       1080 
ESQGIVERAN RTLKEKIQSH RDNTQTLEAA LQLALITCNK GRESMGGQTP WEVFITNQAQ 

      1090       1100       1110       1120       1130       1140 
VIHEKLLLQQ AQSSKKFCFY KIPGEHDWKG PTRVLWKGDG AVVVNDEGKG IIAVPLTRTK 


LLIKPN

P32542 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