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P14350

- POL_FOAMV

UniProt

P14350 - POL_FOAMV

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Protein

Pro-Pol polyprotein

Gene

pol

Organism
Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei24 – 241For protease activity1 Publication
Metal bindingi252 – 2521Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi314 – 3141Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi315 – 3151Magnesium; catalytic; for reverse transcriptase activityBy similarity
Sitei596 – 5972Cleavage; by viral protease; partial
Metal bindingi599 – 5991Magnesium; catalytic; for RNase H activityCurated
Metal bindingi646 – 6461Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi669 – 6691Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi740 – 7401Magnesium; catalytic; for RNase H activityBy similarity
Sitei751 – 7522Cleavage; by viral protease
Metal bindingi874 – 8741Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi936 – 9361Magnesium; catalytic; for integrase activityBy similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed DNA polymerase activity Source: UniProtKB-KW
  6. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA integration Source: UniProtKB-KW
  2. DNA recombination Source: UniProtKB-KW
  3. establishment of integrated proviral latency Source: UniProtKB-KW
  4. viral entry into host cell Source: UniProtKB-KW
  5. viral penetration into host nucleus Source: UniProtKB-KW
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
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]
ProteomesiUP000008228: Genome

Subcellular locationi

Chain Integrase : Virion Curated. Host nucleus. Host cytoplasm Curated
Note: Nuclear at initial phase, cytoplasmic at assembly.Curated
Chain Protease/Reverse transcriptase/ribonuclease H : Host nucleus By similarity. Host cytoplasm Curated
Note: Nuclear at initial phase, cytoplasmic at assembly.Curated

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
  3. intracellular Source: GOC
  4. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241D → A: Complete loss of Gag processing and of Pol processing. Particles are non-infectious. 1 Publication
Mutagenesisi25 – 251S → T: No effect on polyprotein processing and viral replication. 1 Publication
Mutagenesisi152 – 1521P → G: No effect on RT or RNase H activities. 1 Publication
Mutagenesisi169 – 1691P → G: 30% loss of RT activity. 1 Publication
Mutagenesisi193 – 1931P → G: 40% loss of RT activity. 1 Publication
Mutagenesisi599 – 5991D → A: 95% loss of RNase H activity. 1 Publication
Mutagenesisi672 – 6721Y → F: 50% loss of RNase H activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11431143Pro-Pol polyproteinPRO_0000125483Add
BLAST
Chaini1 – 751751Protease/Reverse transcriptase/ribonuclease HPRO_0000245443Add
BLAST
Chaini1 – 596596Protease/Reverse transcriptasePRO_0000245444Add
BLAST
Chaini597 – 751155Ribonuclease HPRO_0000245445Add
BLAST
Chaini752 – 1143392IntegrasePRO_0000245446Add
BLAST

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

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

1
1143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi593 – 60311Combined sources
Beta strandi613 – 6219Combined sources
Beta strandi624 – 6263Combined sources
Beta strandi629 – 63911Combined sources
Helixi642 – 65918Combined sources
Beta strandi660 – 6623Combined sources
Beta strandi664 – 6696Combined sources
Helixi671 – 6788Combined sources
Helixi680 – 6867Combined sources
Beta strandi693 – 6953Combined sources
Helixi700 – 71213Combined sources
Beta strandi717 – 7204Combined sources
Beta strandi723 – 7253Combined sources
Beta strandi727 – 7293Combined sources
Helixi731 – 74919Combined sources
Helixi760 – 7678Combined sources
Beta strandi773 – 7753Combined sources
Beta strandi777 – 7793Combined sources
Beta strandi781 – 7844Combined sources
Beta strandi787 – 7926Combined sources
Beta strandi795 – 7984Combined sources
Helixi802 – 8043Combined sources
Helixi805 – 81410Combined sources
Turni815 – 8173Combined sources
Helixi820 – 8289Combined sources
Helixi836 – 8449Combined sources
Helixi848 – 8536Combined sources
Beta strandi858 – 8603Combined sources
Beta strandi874 – 8818Combined sources
Beta strandi892 – 8987Combined sources
Turni899 – 9013Combined sources
Beta strandi904 – 9129Combined sources
Helixi914 – 92411Combined sources
Turni925 – 9273Combined sources
Beta strandi931 – 9355Combined sources
Helixi939 – 9424Combined sources
Helixi944 – 95310Combined sources
Beta strandi956 – 9594Combined sources
Helixi965 – 9684Combined sources
Helixi970 – 98718Combined sources
Turni990 – 9967Combined sources
Helixi997 – 10059Combined sources
Turni1010 – 10123Combined sources
Helixi1016 – 10216Combined sources
Beta strandi1023 – 10253Combined sources
Beta strandi1028 – 10303Combined sources
Turni1033 – 10364Combined sources
Helixi1040 – 105415Combined sources
Beta strandi1073 – 10775Combined sources
Beta strandi1092 – 10998Combined sources
Beta strandi1102 – 11065Combined sources
Beta strandi1108 – 11103Combined sources
Beta strandi1112 – 11165Combined sources
Helixi1117 – 11193Combined sources
Beta strandi1120 – 11223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14350.
SMRiP14350. Positions 8-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 143143Peptidase A9PROSITE-ProRule annotationAdd
BLAST
Domaini198 – 363166Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini590 – 748159RNase HPROSITE-ProRule annotationAdd
BLAST
Domaini868 – 1024157Integrase catalyticPROSITE-ProRule annotationAdd
BLAST

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 AAA46122.1 differs from that shown. Reason: Frameshift at position 1075. Curated
The sequence AAA66556.1 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
Entry Method Resolution (Å) Chain Positions PDBsum
2LSN NMR - A 591-751 [» ]
2X6N X-ray 2.06 A/B/C/D/E/F 861-1060 [» ]
2X6S X-ray 2.29 A/B/C/D/E/F 861-1060 [» ]
2X74 X-ray 2.34 A/B/C/D/E/F 861-1060 [» ]
2X78 X-ray 2.00 A/B/C 861-1060 [» ]
3DLR X-ray 2.20 A 859-1058 [» ]
3L2Q X-ray 3.25 A/B 752-1143 [» ]
3L2R X-ray 2.88 A/B 752-1143 [» ]
3L2U X-ray 3.15 A/B 752-1143 [» ]
3L2V X-ray 3.20 A/B 752-1143 [» ]
3L2W X-ray 3.20 A/B 752-1143 [» ]
3OS0 X-ray 2.81 A/B 752-1143 [» ]
3OS1 X-ray 2.97 A/B 752-1143 [» ]
3OS2 X-ray 3.32 A/B 752-1143 [» ]
3OY9 X-ray 2.95 A/B 752-1143 [» ]
3OYA X-ray 2.85 A/B 752-1143 [» ]
3OYB X-ray 2.54 A/B 752-1143 [» ]
3OYC X-ray 2.66 A/B 752-1143 [» ]
3OYD X-ray 2.54 A/B 752-1143 [» ]
3OYE X-ray 2.74 A/B 752-1143 [» ]
3OYF X-ray 2.51 A/B 752-1143 [» ]
3OYG X-ray 2.56 A/B 752-1143 [» ]
3OYH X-ray 2.74 A/B 752-1143 [» ]
3OYI X-ray 2.72 A/B 752-1143 [» ]
3OYJ X-ray 2.68 A/B 752-1143 [» ]
3OYK X-ray 2.72 A/B 752-1143 [» ]
3OYL X-ray 2.54 A/B 752-1143 [» ]
3OYM X-ray 2.02 A/B 752-1143 [» ]
3OYN X-ray 2.68 A/B 752-1143 [» ]
3S3M X-ray 2.49 A/B 752-1143 [» ]
3S3N X-ray 2.49 A/B 752-1143 [» ]
3S3O X-ray 2.55 A/B 752-1143 [» ]
4BAC X-ray 3.26 A/B 752-1143 [» ]
4BDY X-ray 2.52 A/B 752-1143 [» ]
4BDZ X-ray 2.85 A/B 752-1143 [» ]
4BE0 X-ray 2.68 A/B 752-1143 [» ]
4BE1 X-ray 2.71 A/B 752-1143 [» ]
4BE2 X-ray 2.38 A/B 752-1143 [» ]
4E7H X-ray 2.57 A/B 752-1143 [» ]
4E7I X-ray 2.53 A/B 752-1143 [» ]
4E7J X-ray 3.15 A/B 752-1143 [» ]
4E7K X-ray 3.02 A/B 752-1143 [» ]
4E7L X-ray 3.00 A/B 752-1143 [» ]
4IKF X-ray 3.40 A/B 752-1143 [» ]
ProteinModelPortali P14350.
SMRi P14350. Positions 8-98.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-58582N.

Protein family/group databases

MEROPSi A09.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14350.
PMAP-CutDB O12817.

Family and domain databases

Gene3Di 3.30.420.10. 2 hits.
InterProi IPR001584. Integrase_cat-core.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001641. Spumavirus_A9.
[Graphical view ]
Pfami PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00078. RVT_1. 1 hit.
PF03539. Spuma_A9PTase. 1 hit.
[Graphical view ]
PRINTSi PR00920. SPUMVIRPTASE.
ProDomi PD013079. Peptidase_A9_cat. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53098. SSF53098. 2 hits.
PROSITEi PS51531. FV_PR. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Fluegel R.M.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION.
  2. "Long terminal repeat U3-length polymorphism of human foamy virus."
    Schmidt M., Herchenrder O., Heeney J.L., Rethwilm A.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus."
    Maurer B., Bannert H., Darai G., Fluegel R.M.
    J. Virol. 62:1590-1597(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-742.
  4. "Nucleotide sequence analysis of the env gene and its flanking regions of the human spumaretrovirus reveals two novel genes."
    Fluegel R.M., Rethwilm A., Maurer B., Darai G.
    EMBO J. 6:2077-2084(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 741-886.
  5. "Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein."
    Konvalinka J., Loechelt M., Zentgraf H., Fluegel R.M., Kraeusslich H.-G.
    J. Virol. 69:7264-7268(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE OF PROTEASE, MUTAGENESIS OF ASP-24 AND SER-25.
  6. "Mutational analysis of the reverse transcriptase and ribonuclease H domains of the human foamy virus."
    Kogel D., Aboud M., Fluegel R.M.
    Nucleic Acids Res. 23:2621-2625(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-152; PRO-169; PRO-193; ASP-599 AND TYR-672.
  7. "The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein."
    Loechelt M., Fluegel R.M.
    J. Virol. 70:1033-1040(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF POLYPROTEIN.
  8. "Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease."
    Pfrepper K.-I., Rackwitz H.R., Schnoelzer M., Heid H., Loechelt M., Fluegel R.M.
    J. Virol. 72:7648-7652(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  9. "Primate foamy virus Pol proteins are imported into the nucleus."
    Imrich H., Heinkelein M., Herchenroder O., Rethwilm A.
    J. Gen. Virol. 81:2941-2947(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: Isolate HSRV2.
  10. "Biphasic DNA synthesis in spumaviruses."
    Delelis O., Saib A., Sonigo P.
    J. Virol. 77:8141-8146(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF REVERSE TRANSCRIPTASE.
  11. Cited for: CHARACTERIZATION OF INTEGRASE.
  12. "Proteolytic processing of foamy virus Gag and Pol proteins."
    Fluegel R.M., Pfrepper K.-I.
    Curr. Top. Microbiol. Immunol. 277:63-88(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. Cited for: REVIEW.

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 26, 2014
This is version 123 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

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

External Data

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