Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P14350

- POL_FOAMV

UniProt

P14350 - POL_FOAMV

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (11 Jul 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

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

    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-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. intracellular Source: GOC
    4. virion Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MNPLQLLQPL PAEIKGTKLL AHWDSGATIT CIPESFLEDE QPIKKTLIKT     50
    IHGEKQQNVY YVTFKVKGRK VEAEVIASPY EYILLSPTDV PWLTQQPLQL 100
    TILVPLQEYQ EKILSKTALP EDQKQQLKTL FVKYDNLWQH WENQVGHRKI 150
    RPHNIATGDY PPRPQKQYPI NPKAKPSIQI VIDDLLKQGV LTPQNSTMNT 200
    PVYPVPKPDG RWRMVLDYRE VNKTIPLTAA QNQHSAGILA TIVRQKYKTT 250
    LDLANGFWAH PITPESYWLT AFTWQGKQYC WTRLPQGFLN SPALFTADVV 300
    DLLKEIPNVQ VYVDDIYLSH DDPKEHVQQL EKVFQILLQA GYVVSLKKSE 350
    IGQKTVEFLG FNITKEGRGL TDTFKTKLLN ITPPKDLKQL QSILGLLNFA 400
    RNFIPNFAEL VQPLYNLIAS AKGKYIEWSE ENTKQLNMVI EALNTASNLE 450
    ERLPEQRLVI KVNTSPSAGY VRYYNETGKK PIMYLNYVFS KAELKFSMLE 500
    KLLTTMHKAL IKAMDLAMGQ EILVYSPIVS MTKIQKTPLP ERKALPIRWI 550
    TWMTYLEDPR IQFHYDKTLP ELKHIPDVYT SSQSPVKHPS QYEGVFYTDG 600
    SAIKSPDPTK SNNAGMGIVH ATYKPEYQVL NQWSIPLGNH TAQMAEIAAV 650
    EFACKKALKI PGPVLVITDS FYVAESANKE LPYWKSNGFV NNKKKPLKHI 700
    SKWKSIAECL SMKPDITIQH EKGISLQIPV FILKGNALAD KLATQGSYVV 750
    NCNTKKPNLD AELDQLLQGH YIKGYPKQYT YFLEDGKVKV SRPEGVKIIP 800
    PQSDRQKIVL QAHNLAHTGR EATLLKIANL YWWPNMRKDV VKQLGRCQQC 850
    LITNASNKAS GPILRPDRPQ KPFDKFFIDY IGPLPPSQGY LYVLVVVDGM 900
    TGFTWLYPTK APSTSATVKS LNVLTSIAIP KVIHSDQGAA FTSSTFAEWA 950
    KERGIHLEFS TPYHPQSGSK VERKNSDIKR LLTKLLVGRP TKWYDLLPVV 1000
    QLALNNTYSP VLKYTPHQLL FGIDSNTPFA NQDTLDLTRE EELSLLQEIR 1050
    TSLYHPSTPP ASSRSWSPVV GQLVQERVAR PASLRPRWHK PSTVLKVLNP 1100
    RTVVILDHLG NNRTVSIDNL KPTSHQNGTT NDTATMDHLE KNE 1143
    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.
    The sequence AAA66556.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 121 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

    Dasty 3