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Protein

Pro-Pol polyprotein

Gene

pol

Organism
Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of 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-Lys1,2 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 a polypurine tract (PPT) 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 probably can 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 PPT that has not been removed by RNase H as primer. PPT 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).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 at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. 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. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA (By similarity).By similarity

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei24For protease activity1 Publication1
Metal bindingi252Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi314Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi315Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi599Magnesium; catalytic; for RNase H activityCurated1
Metal bindingi646Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi669Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi740Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi874Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi936Magnesium; catalytic; for integrase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

DNA integration, DNA recombination, Viral genome integration, Viral penetration into host nucleus, Virus entry into host cell

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Protein family/group databases

MEROPSiA09.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-Pol polyprotein
Alternative name(s):
Pr125Pol
Cleaved into the following 4 chains:
Alternative name(s):
p87Pro-RT-RNaseH
Alternative name(s):
p65Pro-RT
Ribonuclease H (EC:3.1.26.4)
Short name:
RNase H
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
Alternative name(s):
p42In
Gene namesi
Name:pol
OrganismiHuman spumaretrovirus (SFVcpz(hu)) (Human foamy virus)
Taxonomic identifieri11963 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeSpumaretrovirinaeSpumavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008228 Componenti: Genome

Subcellular locationi

Integrase :
Protease/Reverse transcriptase/ribonuclease H :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24D → A: Complete loss of Gag processing and of Pol processing. Particles are non-infectious. 1 Publication1
Mutagenesisi25S → T: No effect on polyprotein processing and viral replication. 1 Publication1
Mutagenesisi152P → G: No effect on RT or RNase H activities. 1 Publication1
Mutagenesisi169P → G: 30% loss of RT activity. 1 Publication1
Mutagenesisi193P → G: 40% loss of RT activity. 1 Publication1
Mutagenesisi599D → A: 95% loss of RNase H activity. 1 Publication1
Mutagenesisi672Y → F: 50% loss of RNase H activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001254831 – 1143Pro-Pol polyproteinAdd BLAST1143
ChainiPRO_00002454431 – 751Protease/Reverse transcriptase/ribonuclease HAdd BLAST751
ChainiPRO_00002454441 – 596Protease/Reverse transcriptaseAdd BLAST596
ChainiPRO_0000245445597 – 751Ribonuclease HAdd BLAST155
ChainiPRO_0000245446752 – 1143IntegraseAdd BLAST392

Post-translational modificationi

Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, long and active p65Pro-RT, p87Pro-RT-RNaseH and even some Pr125Pol are detected in infected cells.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei596 – 597Cleavage; by viral protease; partial2
Sitei751 – 752Cleavage; by viral protease2

Miscellaneous databases

PMAP-CutDBO12817.

Interactioni

Subunit structurei

The protease is a homodimer, whose active site consists of two apposed aspartic acid residues.PROSITE-ProRule annotation

Protein-protein interaction databases

DIPiDIP-58582N.

Structurei

Secondary structure

11143
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi593 – 603Combined sources11
Beta strandi613 – 621Combined sources9
Beta strandi624 – 626Combined sources3
Beta strandi629 – 639Combined sources11
Helixi642 – 659Combined sources18
Beta strandi660 – 662Combined sources3
Beta strandi664 – 669Combined sources6
Helixi671 – 678Combined sources8
Helixi680 – 686Combined sources7
Beta strandi693 – 695Combined sources3
Helixi700 – 712Combined sources13
Beta strandi717 – 720Combined sources4
Beta strandi723 – 725Combined sources3
Beta strandi727 – 729Combined sources3
Helixi731 – 749Combined sources19
Helixi760 – 767Combined sources8
Beta strandi773 – 775Combined sources3
Beta strandi777 – 779Combined sources3
Beta strandi781 – 784Combined sources4
Beta strandi787 – 792Combined sources6
Beta strandi795 – 798Combined sources4
Helixi802 – 804Combined sources3
Helixi805 – 814Combined sources10
Turni815 – 817Combined sources3
Helixi820 – 828Combined sources9
Helixi836 – 844Combined sources9
Helixi848 – 853Combined sources6
Beta strandi858 – 860Combined sources3
Beta strandi874 – 881Combined sources8
Beta strandi892 – 898Combined sources7
Turni899 – 901Combined sources3
Beta strandi904 – 912Combined sources9
Helixi914 – 924Combined sources11
Turni925 – 927Combined sources3
Beta strandi931 – 935Combined sources5
Helixi939 – 942Combined sources4
Helixi944 – 953Combined sources10
Beta strandi956 – 959Combined sources4
Helixi965 – 968Combined sources4
Helixi970 – 987Combined sources18
Turni990 – 996Combined sources7
Helixi997 – 1005Combined sources9
Turni1010 – 1012Combined sources3
Helixi1016 – 1021Combined sources6
Beta strandi1023 – 1025Combined sources3
Beta strandi1028 – 1030Combined sources3
Turni1033 – 1036Combined sources4
Helixi1040 – 1054Combined sources15
Beta strandi1073 – 1077Combined sources5
Beta strandi1092 – 1099Combined sources8
Beta strandi1102 – 1106Combined sources5
Beta strandi1108 – 1110Combined sources3
Beta strandi1112 – 1116Combined sources5
Helixi1117 – 1119Combined sources3
Beta strandi1120 – 1122Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSNNMR-A591-751[»]
2X6NX-ray2.06A/B/C/D/E/F861-1060[»]
2X6SX-ray2.29A/B/C/D/E/F861-1060[»]
2X74X-ray2.34A/B/C/D/E/F861-1060[»]
2X78X-ray2.00A/B/C861-1060[»]
3DLRX-ray2.20A859-1058[»]
3L2QX-ray3.25A/B752-1143[»]
3L2RX-ray2.88A/B752-1143[»]
3L2UX-ray3.15A/B752-1143[»]
3L2VX-ray3.20A/B752-1143[»]
3L2WX-ray3.20A/B752-1143[»]
3OS0X-ray2.81A/B752-1143[»]
3OS1X-ray2.97A/B752-1143[»]
3OS2X-ray3.32A/B752-1143[»]
3OY9X-ray2.95A/B752-1143[»]
3OYAX-ray2.85A/B752-1143[»]
3OYBX-ray2.54A/B752-1143[»]
3OYCX-ray2.66A/B752-1143[»]
3OYDX-ray2.54A/B752-1143[»]
3OYEX-ray2.74A/B752-1143[»]
3OYFX-ray2.51A/B752-1143[»]
3OYGX-ray2.56A/B752-1143[»]
3OYHX-ray2.74A/B752-1143[»]
3OYIX-ray2.72A/B752-1143[»]
3OYJX-ray2.68A/B752-1143[»]
3OYKX-ray2.72A/B752-1143[»]
3OYLX-ray2.54A/B752-1143[»]
3OYMX-ray2.02A/B752-1143[»]
3OYNX-ray2.68A/B752-1143[»]
3S3MX-ray2.49A/B752-1143[»]
3S3NX-ray2.49A/B752-1143[»]
3S3OX-ray2.55A/B752-1143[»]
4BACX-ray3.26A/B752-1143[»]
4BDYX-ray2.52A/B752-1143[»]
4BDZX-ray2.85A/B752-1143[»]
4BE0X-ray2.68A/B752-1143[»]
4BE1X-ray2.71A/B752-1143[»]
4BE2X-ray2.38A/B752-1143[»]
4E7HX-ray2.57A/B752-1143[»]
4E7IX-ray2.53A/B752-1143[»]
4E7JX-ray3.15A/B752-1143[»]
4E7KX-ray3.02A/B752-1143[»]
4E7LX-ray3.00A/B752-1143[»]
4IKFX-ray3.40A/B752-1143[»]
4ZTFX-ray2.70A/B752-1143[»]
4ZTJX-ray2.67A/B752-1143[»]
5FRMX-ray2.58A/B752-1143[»]
5FRNX-ray2.85A/B752-1143[»]
5FROX-ray2.67A/B752-1143[»]
ProteinModelPortaliP14350.
SMRiP14350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 143Peptidase A9PROSITE-ProRule annotationAdd BLAST143
Domaini198 – 363Reverse transcriptasePROSITE-ProRule annotationAdd BLAST166
Domaini590 – 748RNase HPROSITE-ProRule annotationAdd BLAST159
Domaini868 – 1024Integrase catalyticPROSITE-ProRule annotationAdd BLAST157

Domaini

The reverse transcriptase/ribonuclease H (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).By similarity
Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).By similarity

Sequence similaritiesi

Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 peptidase A9 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
Contains 1 RNase H domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.30.420.10. 2 hits.
InterProiIPR001584. Integrase_cat-core.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001641. Spumavirus_A9.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00078. RVT_1. 1 hit.
PF03539. Spuma_A9PTase. 1 hit.
[Graphical view]
PRINTSiPR00920. SPUMVIRPTASE.
ProDomiPD013079. Peptidase_A9_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53098. SSF53098. 2 hits.
PROSITEiPS51531. FV_PR. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLQLLQPL PAEIKGTKLL AHWDSGATIT CIPESFLEDE QPIKKTLIKT
60 70 80 90 100
IHGEKQQNVY YVTFKVKGRK VEAEVIASPY EYILLSPTDV PWLTQQPLQL
110 120 130 140 150
TILVPLQEYQ EKILSKTALP EDQKQQLKTL FVKYDNLWQH WENQVGHRKI
160 170 180 190 200
RPHNIATGDY PPRPQKQYPI NPKAKPSIQI VIDDLLKQGV LTPQNSTMNT
210 220 230 240 250
PVYPVPKPDG RWRMVLDYRE VNKTIPLTAA QNQHSAGILA TIVRQKYKTT
260 270 280 290 300
LDLANGFWAH PITPESYWLT AFTWQGKQYC WTRLPQGFLN SPALFTADVV
310 320 330 340 350
DLLKEIPNVQ VYVDDIYLSH DDPKEHVQQL EKVFQILLQA GYVVSLKKSE
360 370 380 390 400
IGQKTVEFLG FNITKEGRGL TDTFKTKLLN ITPPKDLKQL QSILGLLNFA
410 420 430 440 450
RNFIPNFAEL VQPLYNLIAS AKGKYIEWSE ENTKQLNMVI EALNTASNLE
460 470 480 490 500
ERLPEQRLVI KVNTSPSAGY VRYYNETGKK PIMYLNYVFS KAELKFSMLE
510 520 530 540 550
KLLTTMHKAL IKAMDLAMGQ EILVYSPIVS MTKIQKTPLP ERKALPIRWI
560 570 580 590 600
TWMTYLEDPR IQFHYDKTLP ELKHIPDVYT SSQSPVKHPS QYEGVFYTDG
610 620 630 640 650
SAIKSPDPTK SNNAGMGIVH ATYKPEYQVL NQWSIPLGNH TAQMAEIAAV
660 670 680 690 700
EFACKKALKI PGPVLVITDS FYVAESANKE LPYWKSNGFV NNKKKPLKHI
710 720 730 740 750
SKWKSIAECL SMKPDITIQH EKGISLQIPV FILKGNALAD KLATQGSYVV
760 770 780 790 800
NCNTKKPNLD AELDQLLQGH YIKGYPKQYT YFLEDGKVKV SRPEGVKIIP
810 820 830 840 850
PQSDRQKIVL QAHNLAHTGR EATLLKIANL YWWPNMRKDV VKQLGRCQQC
860 870 880 890 900
LITNASNKAS GPILRPDRPQ KPFDKFFIDY IGPLPPSQGY LYVLVVVDGM
910 920 930 940 950
TGFTWLYPTK APSTSATVKS LNVLTSIAIP KVIHSDQGAA FTSSTFAEWA
960 970 980 990 1000
KERGIHLEFS TPYHPQSGSK VERKNSDIKR LLTKLLVGRP TKWYDLLPVV
1010 1020 1030 1040 1050
QLALNNTYSP VLKYTPHQLL FGIDSNTPFA NQDTLDLTRE EELSLLQEIR
1060 1070 1080 1090 1100
TSLYHPSTPP ASSRSWSPVV GQLVQERVAR PASLRPRWHK PSTVLKVLNP
1110 1120 1130 1140
RTVVILDHLG NNRTVSIDNL KPTSHQNGTT NDTATMDHLE KNE
Length:1,143
Mass (Da):129,742
Last modified:July 11, 2006 - v2
Checksum:i786E3203B06FFB3C
GO

Sequence cautioni

The sequence AAA46122 differs from that shown. Reason: Frameshift at position 1075.Curated
The sequence AAA66556 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21247 Genomic RNA. Translation: AAB48112.1.
Y07723 Genomic DNA. Translation: CAA68997.1.
Y07724 Genomic DNA. Translation: CAA68999.1.
Y07725 Genomic DNA. Translation: CAA69003.1.
M19427 Genomic RNA. Translation: AAA66556.1. Different initiation.
M54978 Genomic RNA. Translation: AAA46122.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21247 Genomic RNA. Translation: AAB48112.1.
Y07723 Genomic DNA. Translation: CAA68997.1.
Y07724 Genomic DNA. Translation: CAA68999.1.
Y07725 Genomic DNA. Translation: CAA69003.1.
M19427 Genomic RNA. Translation: AAA66556.1. Different initiation.
M54978 Genomic RNA. Translation: AAA46122.1. Frameshift.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSNNMR-A591-751[»]
2X6NX-ray2.06A/B/C/D/E/F861-1060[»]
2X6SX-ray2.29A/B/C/D/E/F861-1060[»]
2X74X-ray2.34A/B/C/D/E/F861-1060[»]
2X78X-ray2.00A/B/C861-1060[»]
3DLRX-ray2.20A859-1058[»]
3L2QX-ray3.25A/B752-1143[»]
3L2RX-ray2.88A/B752-1143[»]
3L2UX-ray3.15A/B752-1143[»]
3L2VX-ray3.20A/B752-1143[»]
3L2WX-ray3.20A/B752-1143[»]
3OS0X-ray2.81A/B752-1143[»]
3OS1X-ray2.97A/B752-1143[»]
3OS2X-ray3.32A/B752-1143[»]
3OY9X-ray2.95A/B752-1143[»]
3OYAX-ray2.85A/B752-1143[»]
3OYBX-ray2.54A/B752-1143[»]
3OYCX-ray2.66A/B752-1143[»]
3OYDX-ray2.54A/B752-1143[»]
3OYEX-ray2.74A/B752-1143[»]
3OYFX-ray2.51A/B752-1143[»]
3OYGX-ray2.56A/B752-1143[»]
3OYHX-ray2.74A/B752-1143[»]
3OYIX-ray2.72A/B752-1143[»]
3OYJX-ray2.68A/B752-1143[»]
3OYKX-ray2.72A/B752-1143[»]
3OYLX-ray2.54A/B752-1143[»]
3OYMX-ray2.02A/B752-1143[»]
3OYNX-ray2.68A/B752-1143[»]
3S3MX-ray2.49A/B752-1143[»]
3S3NX-ray2.49A/B752-1143[»]
3S3OX-ray2.55A/B752-1143[»]
4BACX-ray3.26A/B752-1143[»]
4BDYX-ray2.52A/B752-1143[»]
4BDZX-ray2.85A/B752-1143[»]
4BE0X-ray2.68A/B752-1143[»]
4BE1X-ray2.71A/B752-1143[»]
4BE2X-ray2.38A/B752-1143[»]
4E7HX-ray2.57A/B752-1143[»]
4E7IX-ray2.53A/B752-1143[»]
4E7JX-ray3.15A/B752-1143[»]
4E7KX-ray3.02A/B752-1143[»]
4E7LX-ray3.00A/B752-1143[»]
4IKFX-ray3.40A/B752-1143[»]
4ZTFX-ray2.70A/B752-1143[»]
4ZTJX-ray2.67A/B752-1143[»]
5FRMX-ray2.58A/B752-1143[»]
5FRNX-ray2.85A/B752-1143[»]
5FROX-ray2.67A/B752-1143[»]
ProteinModelPortaliP14350.
SMRiP14350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58582N.

Protein family/group databases

MEROPSiA09.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14350.
PMAP-CutDBO12817.

Family and domain databases

Gene3Di3.30.420.10. 2 hits.
InterProiIPR001584. Integrase_cat-core.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001641. Spumavirus_A9.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00078. RVT_1. 1 hit.
PF03539. Spuma_A9PTase. 1 hit.
[Graphical view]
PRINTSiPR00920. SPUMVIRPTASE.
ProDomiPD013079. Peptidase_A9_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53098. SSF53098. 2 hits.
PROSITEiPS51531. FV_PR. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOL_FOAMV
AccessioniPrimary (citable) accession number: P14350
Secondary accession number(s): O12528
, O12817, Q76U32, Q98835
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 11, 2006
Last modified: November 30, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.
Foamy viruses are distinct from other retroviruses in many respects. Their protease is active as an uncleaved Pro-Pol protein. Mature particles do not include the usual processed retroviral structural protein (MA, CA and NC), but instead contain two large Gag proteins. Their functional nucleic acid appears to be either RNA or dsDNA (up to 20% of extracellular particles), because they probably proceed either to an early (before integration) or late reverse transcription (after assembly). Foamy viruses have the ability to retrotranspose intracellularly with high efficiency. They bud predominantly into the endoplasmic reticulum (ER) and occasionally at the plasma membrane. Budding requires the presence of Env proteins. Most viral particles probably remain within the infected cell.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.