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 (strain Wyoming) (EIAV)

[TaxID: 11672]

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

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE. PubMed=3003905 [NCBI, ExPASy, EBI, Israel, Japan] Stephens R.M., Casey J.W., Rice N.R.; "Equine infectious anemia virus gag and pol genes: relatedness to visna and AIDS virus."; Science 231:589-594(1986).
[2]	NUCLEOTIDE SEQUENCE OF 1029-1145. DOI=10.1016/0042-6822(86)90195-9; PubMed=2431539 [NCBI, ExPASy, EBI, Israel, Japan] Rushlow K., Olsen K., Stiegler G., Payne S.L., Montelaro R.C., Issel C.J.; "Lentivirus genomic organization: the complete nucleotide sequence of the env gene region of equine infectious anemia virus."; Virology 155:309-321(1986).

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.
CAUTION: The original EMBL accession numbers (M11337 and M14855) assigned to this isolate (isolate Wyoming) have been made secondary to M16575 which is from a different isolate (clone 1365).

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A03970; GNLJEV.

3D structure databases

HSSP

P11204; 1DUN. [HSSP ENTRY / PDB]

SMR

P03371; 81-184, 741-860.

ModBase

P03371.

Ontologies

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

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

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

Keywords

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_0000038835`
`CHAIN`	`196 913`	`718`	`Reverse transcriptase/ribonuclease H.`	`PRO_0000038836`
`CHAIN`	`914 1145`	`232`	`Integrase.`	`PRO_0000038837`
`DOMAIN`	`100 174`	`75`	`Peptidase A2.`
`DOMAIN`	`230 418`	`189`	`Reverse transcriptase.`
`DOMAIN`	`616 739`	`124`	`RNase H.`
`DOMAIN`	`920 1077`	`158`	`Integrase catalytic.`
`ZN_FING`	`877 918`	`42`	`Integrase-type.`
`DNA_BIND`	`1095 1143`	`49`	`Integrase-type.`
`ACT_SITE`	`105 105`		`By similarity.`

Sequence information

Length: 1145 AA [This is the length of the unprocessed precursor]

Molecular weight: 129520 Da [This is the MW of the unprocessed precursor]

CRC64: EE723380950D5D9E [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 KETVQRLLSE GKISEASDNN 

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

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

       370        380        390        400        410        420 
PEVQLYQYMD DLFVGSNGSK KQHKELIIEL RAILQKGFET PDDKLQEVPP YSWLGYQLCP 

       430        440        450        460        470        480 
ENWKVQKMQL DMVKNPTLND VQKLMGNITW MSSGVPGLTV KHIAATTKGC LELNQKVIWT 

       490        500        510        520        530        540 
EEAQKELEEN NEKIKNAQGL QYYNPEEEML CEVEITKNYE ATYVIKQSQG ILWAGKKIMK 

       550        560        570        580        590        600 
ANKGWSTVKN LMLLLQHVAT ESITRVGKCP TFKVPFTKEQ VMWEMQKGWY YSWLPEIVYT 

       610        620        630        640        650        660 
HQVVHDDWRM KLVEEPTSGI TIYTDGGKQN GEGIAAYVTS NGRTKQKRLG PVTHQVAERM 

       670        680        690        700        710        720 
AIQMALEDTR DKQVNIVTDS YYCWKNITEG LGLEGPQNPW WPIIQNIREK EIVYFAWVPG 

       730        740        750        760        770        780 
HKGIYGNQLA DEAAKIKEEI MLAYQGTQIK EKRDEDAGFD LCVPYDIMIP VSDTKIIPTD 

       790        800        810        820        830        840 
VKIQVPPNSF GWVTGKSSMA KQGLLINGGI IDEGYTGEIQ VICTNIGKSN IKLIEGQKFA 

       850        860        870        880        890        900 
QLIILQHHSN SRQPWDENKI SQRGDKGFGS TGVFWVENIQ EAQDEHENWH TSPKILARNY 

       910        920        930        940        950        960 
KIPLTVAKQI TQECPHCTKQ GSGPAGCVMR SPNHWQADCT HLDNKIILHF VESNSGYIHA 

       970        980        990       1000       1010       1020 
TLLSKENALC TSLAILEWAR LFSPKSLHTD NGTNFVAEPV VNLLKFLKIA HTTGIPYHPE 

      1030       1040       1050       1060       1070       1080 
SQGIVERANR TLKEKIQSHR DNTQTLEAAL QLALITCNKG RESMGGQTPW EVFITNQAQV 

      1090       1100       1110       1120       1130       1140 
IHEKLLLQQA QSSKKFCFYK IPGEHDWKGP TRVLWKGDGA VVVNDEGKGI IAVPLTRTKL 


LIKPN

P03371 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