Reviewed, UniProtKB/Swiss-Prot Q8AII1 (POL_SIVTN)

Names and origin

Protein names

Recommended name:
    Gag-Pol polyprotein
Alternative name(s):
    Pr160Gag-Pol
Cleaved into the following 9 chains:
    1- Recommended name:
            Matrix protein p17
                Short name=MA
    2- Recommended name:
            Capsid protein p24
                Short name=CA
    3- Recommended name:
            Nucleocapsid protein p7
                Short name=NC
    4- Recommended name:
            p6-pol
                Short name=p6*
    5- Recommended name:
            Protease
              EC=3.4.23.16
        Alternative name(s):
            Retropepsin
            PR
    6- Recommended name:
            Reverse transcriptase/ribonuclease H
              EC=2.7.7.49
              EC=2.7.7.7
              EC=3.1.26.4
        Alternative name(s):
            p66 RT
    7- Recommended name:
            p51 RT
    8- Recommended name:
            p15
    9- Recommended name:
            Integrase
                Short name=IN

Gene names

Name:

gag-pol

Organism

Simian immunodeficiency virus (isolate TAN1) (SIV-cpz) (Chimpanzee immunodeficiency virus)

Taxonomic identifier

388910 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group

Virus host

Pan troglodytes (Chimpanzee) [TaxID: 9598]

Protein attributes

Sequence length	1462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 myristointegration 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 dissassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian 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. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles 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 allow 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 SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity.
Catalytic activity	Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. Endonucleolytic cleavage to 5'-phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
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.
Enzyme regulation	The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies.
Subunit structure	Matrix protein p17 is a trimer. Interacts with gp120. 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 accomodating 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. Capsid protein p24 is phosphorylated.
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 process	Capsid maturation DNA integration DNA recombination
Cellular component	Capsid protein Cell membrane Cytoplasm Membrane Nucleus Virion
Coding sequence diversity	Ribosomal frameshifting
Domain	Repeat Zinc-finger
Ligand	Magnesium Metal-binding RNA-binding Viral nucleoprotein Zinc
Molecular function	Aspartyl protease DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro transposition Inferred from electronic annotation. Source: UniProtKB-KW viral procapsid maturation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW host 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 nucleus Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW integrase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC structural molecule activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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: Q8AII1-1)

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: Q8AII2-1)

The sequence of this isoform can be found in the external entry Q8AII2-1.
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host By similarity
	Chain	2 – 1462	1461	Gag-Pol polyprotein		PRO_0000261304
	Chain	2 – 155	154	Matrix protein p17 By similarity		PRO_0000249395
	Chain	156 – 389	234	Capsid protein p24 By similarity		PRO_0000249396
	Chain	390 – 463	74	Nucleocapsid protein p7 By similarity		PRO_0000249398
	Chain	464 – 515	52	p6-pol Potential		PRO_0000249400
	Chain	516 – 614	99	Protease By similarity		PRO_0000249401
	Chain	615 – 1174	560	Reverse transcriptase/ribonuclease H By similarity		PRO_0000249402
	Chain	615 – 1054	440	p51 RT By similarity		PRO_0000249403
	Chain	1055 – 1174	120	p15 By similarity		PRO_0000249404
	Chain	1175 – 1462	288	Integrase By similarity		PRO_0000249405
Regions
	Domain	535 – 604	70	Peptidase A2
	Domain	658 – 848	191	Reverse transcriptase
	Domain	1048 – 1171	124	RNase H
	Domain	1228 – 1378	151	Integrase catalytic
	Zinc finger	417 – 434	18	CCHC-type 1
	Zinc finger	438 – 455	18	CCHC-type 2
	Zinc finger	1177 – 1218	42	Integrase-type
	DNA binding	1397 – 1444	48	Integrase-type
	Region	841 – 849	9	RT 'primer grip' By similarity
	Motif	16 – 22	7	Nuclear export signal By similarity
	Motif	26 – 32	7	Nuclear localization signal By similarity
	Motif	1012 – 1028	17	Tryptophan repeat motif By similarity
Sites
	Active site	540	1	For protease activity; shared with dimeric partner By similarity
	Metal binding	724	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	799	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	800	1	Magnesium; catalytic; for reverse transcriptase activity By similarity
	Metal binding	1057	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1092	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1112	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1163	1	Magnesium; catalytic; for RNase H activity By similarity
	Metal binding	1238	1	Magnesium; catalytic; for integrase activity By similarity
	Metal binding	1290	1	Magnesium; catalytic; for integrase activity By similarity
	Site	155 – 156	2	Cleavage; by viral protease By similarity
	Site	244 – 245	2	Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA By similarity
	Site	389 – 390	2	Cleavage; by viral protease By similarity
	Site	463 – 464	2	Cleavage; by viral protease By similarity
	Site	515 – 516	2	Cleavage; by viral protease By similarity
	Site	614 – 615	2	Cleavage; by viral protease By similarity
	Site	1015	1	Essential for RT p66/p51 heterodimerization By similarity
	Site	1028	1	Essential for RT p66/p51 heterodimerization By similarity
	Site	1054 – 1055	2	Cleavage; by viral protease; partial By similarity
	Site	1174 – 1175	2	Cleavage; by viral protease By similarity
Amino acid modifications
	Modified residue	155	1	Phosphotyrosine; by host By similarity
	Lipidation	2	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gag-Pol polyprotein [UniParc]. Last modified October 2, 2007. Version 4. Checksum: 975189082B1EF05F	FASTA	1,462	164,427
	10 20 30 40 50 60 MGARASVLRG DKLDTWESIR LKSRGRKKYL IKHLVWAGSE LQRFAMNPGL MENVEGCWKI 70 80 90 100 110 120 ILQLQPSVDI GSPEIISLFN TICVLYCVHA GERVQDTEEA VKIVKMKLTV QKNNSTATSS 130 140 150 160 170 180 GQRQNAGEKE ETVPPSGNTG NTGRATETPS GSRLYPVITD AQGVARHQPI SPRTLNAWVR 190 200 210 220 230 240 VIEEKGFNPE VIPMFSALSE GATPYDLNSM LNAVGEHQAA MQMLKEVINE EAAEWDRAHP 250 260 270 280 290 300 AHAGPQQAGM LREPTGADIA GTTSTLQEQV LWMTTPQAQG GVPVGDIYKR WIILGLNKLV 310 320 330 340 350 360 RMYSPVSILD IKQGPKEPFR DYVDRFYKTI RAEQASQPVK TWMTETLLVQ NANPDCKHIL 370 380 390 400 410 420 KALGQGATLE EMLTACQGVG GPSHKAKILA EAMASATAGG VNMLQGGKRP PLKKGQLQCF 430 440 450 460 470 480 NCGKVGHTAR NCRAPRKKGC WRCGQEGHQM KDCTTRNNST GVNFFRETHP LVGVQTRELC 490 500 510 520 530 540 AEHPREREGS GAGDSTDTSG ANCPTTGDDD ERRVLPQVNL WQRPMMTVKV QGQVCQALLD 550 560 570 580 590 600 TGADDSVFCN IKLKGQWTPK TIGGIGGFVP VSEYYNIPVQ IGNKEVRATV LVGETPINII 610 620 630 640 650 660 GRNILKQLGC TLNFPISPIE VVKVQLKEGM DGPKVKQWPL SKEKIEALTE ICKTLEKEGK 670 680 690 700 710 720 ISAVGPENPY NTPIFAIKKK DTSKWRKLVD FRELNKRTQD FWELQLGIPH PAGLRKRNMV 730 740 750 760 770 780 TVLDVGDAYF SIPLDPDFRK YTAFTIPSLN NNTPGKRFQY NVLPQGWKGS PAIFQSSMTK 790 800 810 820 830 840 ILDPFRKEHP DVDIYQYMDD LYIGSDLNEE EHRKLIKKLR QHLLTWGLET PDKKYQEKPP 850 860 870 880 890 900 FMWMGYELHP NKWTVQNITL PEPEQWTVNH IQKLVGKLNW ASQIYHGIKT KELCKLIRGV 910 920 930 940 950 960 KGLTEPVEMT REAELELEEN KQILKEKVQG AYYDPKLPLQ AAIQKQGQGQ WTYQIYQEEG 970 980 990 1000 1010 1020 KNLKTGKYAK SPGTHTNEIR QLAGLIQKIG NESIIIWGIV PKFLLPVSKE TWSQWWTDYW 1030 1040 1050 1060 1070 1080 QVTWVPEWEF INTPPLIRLW YNLLSDPIPE AETFYVDGAA NRDSKKGRAG YVTNRGRYRS 1090 1100 1110 1120 1130 1140 KDLENTTNQQ AELWAVDLAL KDSGAQVNIV TDSQYVMGVL QGLPDQSDSP IVEQIIQKLT 1150 1160 1170 1180 1190 1200 QKTAIYLAWV PAHKGIGGNE EVDKLVSKNI RKILFLDGIN EAQEDHDKYH SNWKALADEY 1210 1220 1230 1240 1250 1260 NLPPVVAKEI IAQCPKCHIK GEAIHGQVDY SPEIWQIDCT HLEGKVIIVA VHVASGFIEA 1270 1280 1290 1300 1310 1320 EVIPEETGRE TAYFILKLAG RWPVKKIHTD NGPNFTSTAV KAACWWAQIQ HEFGIPYNPQ 1330 1340 1350 1360 1370 1380 SQGVVESMNK QLKQIIEQVR DQAEQLRTAV IMAVYIHNFK RKGGIGEYTA GERLLDILTT 1390 1400 1410 1420 1430 1440 NIQTKQLQKQ ILKVQNFRVY YRDARDPIWK GPARLLWKGE GAVVIKEGED IKVVPRRKAK 1450 1460 IIKEYGKQMA GAGGMDDRQN ET
	Isoform Gag polyprotein. See Q8AII2.	FASTA	–	–

References

[1]

"Amplification of a complete simian immunodeficiency virus genome from fecal RNA of a wild chimpanzee." Santiago M.L., Bibollet-Ruche F., Bailes E., Kamenya S., Muller M.N., Lukasik M., Pusey A.E., Collins D.A., Wrangham R.W., Goodall J., Shaw G.M., Sharp P.M., Hahn B.H. J. Virol. 77:2233-2242(2003) [PubMed: 12525658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF447763 Genomic RNA. Translation: AAO13960.1. Sequence problems.
3D structure databases
HSSP	HSSP built from PDB template 1BIS based on UniProtKB P12497.
SMR	Q8AII1. Positions 167-377, 612-1154, 1172-1383, 1228-1441.
ModBase	Search...
Protein family/group databases
MEROPS	A02.001.
Family and domain databases
InterPro	IPR000477. DNA_pol_RVTase. 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_HIV/RSV_N. IPR018061. Pept_A2A_retrovirus_sg. IPR001995. Peptidase_A2_cat. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR008916. Retrov_capsid_C. IPR008919. Retrov_capsid_N. IPR002156. RNase_H. IPR010659. RVT_connect. IPR010661. RVT_thumb. IPR013084. Znf_CCH_retrovir. IPR001878. Znf_CCHC. [Graphical view]
Gene3D	G3DSA:2.30.30.10. Integrase_C. 1 hit. G3DSA:1.10.10.200. Intgrase_N_Zn_bd. 1 hit. G3DSA:1.10.150.90. Matrix_HIV/RSV_N. 1 hit. G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit. G3DSA:1.10.1200.30. Retrov_capsid_C. 1 hit. G3DSA:1.10.375.10. Retrov_capsid_N. 1 hit. G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.
Pfam	PF00540. Gag_p17. 1 hit. PF00607. Gag_p24. 1 hit. PF00552. Integrase. 1 hit. PF02022. Integrase_Zn. 1 hit. PF00075. RnaseH. 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]
PRINTS	PR00234. HIV1MATRIX.
SMART	SM00343. ZnF_C2HC. 2 hits. [Graphical view]
PROSITE	PS50175. 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]
ProtoNet	Search...

Entry information

Entry name

POL_SIVTN

Accession

Primary (citable) accession number: Q8AII1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	October 2, 2007
Last modified:	June 16, 2009
This is version 59 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)