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P12451 (POL_HV2SB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol

Cleaved into the following 11 chains:

  1. Matrix protein p17
    Short name=MA
  2. Capsid protein p24
    Short name=CA
  3. Spacer peptide p2
  4. Nucleocapsid protein p7
    Short name=NC
  5. Transframe peptide
    Short name=TF
  6. p6-pol
    Short name=p6*
  7. Protease
    EC=3.4.23.47
    Alternative name(s):
    PR
    Retropepsin
  8. Reverse transcriptase/ribonuclease H
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.13
    Alternative name(s):
    Exoribonuclease H
    EC=3.1.13.2
    p66 RT
  9. p51 RT
  10. p15
  11. Integrase
    Short name=IN
Gene names
Name:gag-pol
OrganismHuman immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2) [Complete proteome]
Taxonomic identifier11718 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation By similarity.

Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu By similarity.

Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV to the human species By similarity.

Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity By similarity.

The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell By similarity.

Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. 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. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends By similarity.

Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity.

Catalytic activity

Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.

3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Endopeptidase for which the P1 residue is preferably hydrophobic.

Cofactor

Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity.

Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.

Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.

Subunit structure

Matrix protein p17 is a trimer. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. The integrase is a homodimer and possibly a homotetramer By similarity.

Subcellular location

Matrix protein p17: Virion Potential. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane; Lipid-anchor Potential. Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity.

Capsid protein p24: Virion Potential.

Nucleocapsid protein p7: Virion Potential.

Reverse transcriptase/ribonuclease H: Virion Potential.

Integrase: Virion Potential. Host nucleus Potential. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential.

Domain

The p66 RT is 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 RNase H domain stabilizes the association of RT with primer-template By similarity.

The tryptophan repeat motif is involved in RT p66/p51 dimerization By similarity.

Post-translational modification

Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit By similarity.

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

Sequence similarities

Contains 2 CCHC-type zinc fingers.

Contains 1 integrase catalytic domain.

Contains 1 integrase-type DNA-binding domain.

Contains 1 integrase-type zinc finger.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Eukaryotic host gene expression shutoff by virus
Eukaryotic host translation shutoff by virus
Host gene expression shutoff by virus
Host-virus interaction
Viral genome integration
Viral penetration into host nucleus
Virion maturation
Virus entry into host cell
Virus exit from host cell
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Host nucleus
Membrane
Virion
   Coding sequence diversityRibosomal frameshifting
   DiseaseAIDS
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
RNA-binding
Viral nucleoprotein
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMLipoprotein
Myristate
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

establishment of integrated proviral latency

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from electronic annotation. Source: GOC

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-DNA hybrid ribonuclease activity

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

exoribonuclease H activity

Inferred from electronic annotation. Source: UniProtKB-EC

structural molecule activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag-Pol polyprotein (identifier: P12451-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by -1 ribosomal frameshifting.
Isoform Gag polyprotein (identifier: P12450-1)

The sequence of this isoform can be found in the external entry P12450.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 14621461Gag-Pol polyprotein
PRO_0000261299
Chain2 – 135134Matrix protein p17 By similarity
PRO_0000042515
Chain136 – 364229Capsid protein p24 By similarity
PRO_0000042516
Peptide365 – 38117Spacer peptide p2 By similarity
PRO_0000042517
Chain382 – 43049Nucleocapsid protein p7 By similarity
PRO_0000042519
Peptide431 – 44414Transframe peptide Potential
PRO_0000246748
Chain445 – 51167p6-pol Potential
PRO_0000042521
Chain512 – 61099Protease By similarity
PRO_0000038672
Chain611 – 1169559Reverse transcriptase/ribonuclease H By similarity
PRO_0000042522
Chain611 – 1049439p51 RT By similarity
PRO_0000042523
Chain1050 – 1169120p15 By similarity
PRO_0000042524
Chain1170 – 1462293Integrase By similarity
PRO_0000042525

Regions

Domain531 – 60070Peptidase A2
Domain654 – 844191Reverse transcriptase
Domain1043 – 1166124RNase H
Domain1222 – 1373152Integrase catalytic
Zinc finger388 – 40518CCHC-type 1
Zinc finger409 – 42618CCHC-type 2
Zinc finger1172 – 121342Integrase-type
DNA binding1392 – 143948Integrase-type
Region837 – 8459RT 'primer grip' By similarity
Motif16 – 227Nuclear export signal By similarity
Motif26 – 327Nuclear localization signal By similarity
Motif1007 – 102317Tryptophan repeat motif By similarity

Sites

Active site5361For protease activity; shared with dimeric partner By similarity
Metal binding7201Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7951Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding7961Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding10521Magnesium; catalytic; for RNase H activity By similarity
Metal binding10871Magnesium; catalytic; for RNase H activity By similarity
Metal binding11071Magnesium; catalytic; for RNase H activity By similarity
Metal binding11581Magnesium; catalytic; for RNase H activity By similarity
Metal binding12331Magnesium; catalytic; for integrase activity By similarity
Metal binding12851Magnesium; catalytic; for integrase activity By similarity
Site135 – 1362Cleavage; by viral protease By similarity
Site222 – 2232Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA By similarity
Site364 – 3652Cleavage; by viral protease By similarity
Site381 – 3822Cleavage; by viral protease By similarity
Site430 – 4312Cleavage; by viral protease Potential
Site444 – 4452Cleavage; by viral protease By similarity
Site511 – 5122Cleavage; by viral protease By similarity
Site610 – 6112Cleavage; by viral protease By similarity
Site10101Essential for RT p66/p51 heterodimerization By similarity
Site10231Essential for RT p66/p51 heterodimerization By similarity
Site1049 – 10502Cleavage; by viral protease; partial By similarity
Site1169 – 11702Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform Gag-Pol polyprotein [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DBA366324EA0167E

FASTA1,462165,014
        10         20         30         40         50         60 
MGAKNSVLRG KKADELEKIR LRPGGKKKYR LKHIVWAANE LDRFGLTESL LESKEGCQKI 

        70         80         90        100        110        120 
ISVLEPLVPT GSENLKSLYN TTCVIWCLHA EEKVKDTEEA KRIVGRHLVA ETETAEKMPN 

       130        140        150        160        170        180 
ISRPTAPPSG KGGNFPVQQI GGNYVHLPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG 

       190        200        210        220        230        240 
CTPYDINQML NCVGDHQAAM QIIREIINEE AADWDVQHPI PGPLPAGQLR DPRGSDIAGT 

       250        260        270        280        290        300 
TSTVEEQIEW MYRQENPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKESFQSYVD 

       310        320        330        340        350        360 
RFYKSLRAEQ TDAAVKNWMT QTLLVQSNPD CKLVLKGLGM NPTLEEMLTA CQGIGGPGQK 

       370        380        390        400        410        420 
ARLMAEALKE AMRPAPIPFA AAQQKRAIKC WNCGKEGHSA RQCRAPRRQG CWKCGKSGHI 

       430        440        450        460        470        480 
MANCPDRQAG FLRAWTMGKE APQLPRGPKF AGANTNSTPN GSSSGPTGEV HAAREKTERA 

       490        500        510        520        530        540 
ETKTIQRSDR GLAASRARRD TTQRDDRGLA APQFSLWKRP VVTAYIEDQP VEVLLDTGAD 

       550        560        570        580        590        600 
DSIVAGIELG SNYSPKIVGG IGGFINTKEY KDVEIRVLNK KVRATIMTGD TPINIFGRNI 

       610        620        630        640        650        660 
LTALGMSLNL PVAKIEPVKV TLKPGKDGPK QRQWPLTREK IEALREICEK MEREGQLEEA 

       670        680        690        700        710        720 
PPTNPYNTPT FAIKKKDKNK WRMLIDFREL NKVTQDFTEV QLGIPHPAGL AKKRRITVLD 

       730        740        750        760        770        780 
VGDAYFSIPL YEDFRQYTAF TLPSVNNAEP GKRYIYKVLP QGWKGSPAIF QYTMRQVLEP 

       790        800        810        820        830        840 
FRKANPDVII VQYMDDILIA SDRTDLEHDK VVLQLKELLN GLGFSTPDEK FQKDPPYQWM 

       850        860        870        880        890        900 
GYELWPTKWK LQKIQLPQKE VWTVNDIQKL VGVLNWAAQI YPGIKTKHLC KLIRGKMTPT 

       910        920        930        940        950        960 
EEVQWTELAE AELEENKIIL SQEQEGHYYQ EEKELEATVQ KDQDNQWTYK VHQGEKILKV 

       970        980        990       1000       1010       1020 
GKYAKIKNTH TNGVRLLAQV VQKIGKEALV IWGRIPKFHL PVERETWEQW WDNYWQVTWI 

      1030       1040       1050       1060       1070       1080 
PDWDFVSTPP LVRLAFNLVK DPIPGAETFY TDGSCNRQSK EGKAGYITDR GKDKVRILEQ 

      1090       1100       1110       1120       1130       1140 
TTNQQAELEA FAMAVTDSGP KVNIVVDSQY VMGIVTGQPA ESESRIVNKI IEEMIKKEAI 

      1150       1160       1170       1180       1190       1200 
YVAWVPAHKG IGGNQEIDHL VSQGIRQVLF LERIEPAQEE HGKYHSNVKE LAHKFGLPNL 

      1210       1220       1230       1240       1250       1260 
VARQIVNTCA QCQQKGEAIH GQVNAELGTW QMDCTHLEGK IIIVAVHVAS GFIEAEVIPQ 

      1270       1280       1290       1300       1310       1320 
ESGRQTALFL LKLASRWPIT HLHTDNGANF TSQEVKMVAW WVGIEQSFGV PYNPQSQGVV 

      1330       1340       1350       1360       1370       1380 
EAMNHHLKNQ IERIREQANT METIVLMAVH CMNFKRRGGI GDMTPVERLV NMITTEQEIQ 

      1390       1400       1410       1420       1430       1440 
FLQAKNSKLK NFRVYFREGR NQLWQGPGEL LWKGDGAVIV KVGTDIKVIP RRKAKIIRDY 

      1450       1460 
GPRQEMDSGS HLEGAREDGE MA 

« Hide

Isoform Gag polyprotein [UniParc].

See P12450.

References

[1]"Molecular and biological characterization of a replication competent human immunodeficiency type 2 (HIV-2) proviral clone."
Franchini G., Fargnoli K.A., Giombini F., Jagodzinski L.L., de Rossi A., Bosch M., Biberfeld G., Fenyo A.M., Albert J., Gallo R.C., Wong-Staal F.
Proc. Natl. Acad. Sci. U.S.A. 86:2433-2437(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Proteolytic processing and particle maturation."
Vogt V.M.
Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[3]"Structural biology of HIV."
Turner B.G., Summers M.F.
J. Mol. Biol. 285:1-32(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[4]"Mechanisms of retroviral recombination."
Negroni M., Buc H.
Annu. Rev. Genet. 35:275-302(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Retroviral proteases."
Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.
Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04498 Genomic DNA. Translation: AAB00746.1. Sequence problems.

3D structure databases

ProteinModelPortalP12451.
SMRP12451. Positions 2-135, 145-380, 384-429, 512-610, 613-1165, 1170-1215, 1224-1381, 1385-1439.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.30.30.10. 1 hit.
2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 1 hit.
InterProIPR001969. Aspartic_peptidase_AS.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR000071. Lentvrl_matrix_N.
IPR012344. Matrix_N_HIV/RSV.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
PRINTSPR00234. HIV1MATRIX.
SMARTSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 2 hits.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOL_HV2SB
AccessionPrimary (citable) accession number: P12451
Secondary accession number(s): Q85570
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries