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)

P11283

- POL_MMTVC

UniProt

P11283 - POL_MMTVC

Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Mouse mammary tumor virus (strain C3H) (MMTV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Matrix protein p10: Matrix protein.By similarity
    Nucleocapsid protein p14: Nucleocapsid protein. Binds to single-stranded DNA By similarity.By similarity
    Capsid protein p27: capsid protein.By similarity
    NC-dUTPase has dUTPase activity, thereby preventing incorporation of uracil into DNA.
    The aspartyl protease mediates proteolytic cleavages of Gag, Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell By similarity.By similarity
    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 a polypurine tract (PPT) situated at the 5' end 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 primers. 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

    Catalytic activityi

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

    Cofactori

    RT polymerase domain: Binds 2 magnesium ions.By similarity
    Magnesium ions for NC-dUTPase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei99 – 1002Cleavage; by viral proteaseBy similarity
    Sitei195 – 1962Cleavage; by viral proteaseBy similarity
    Sitei228 – 2292Cleavage; by viral proteaseBy similarity
    Sitei252 – 2532Cleavage; by viral proteaseBy similarity
    Sitei269 – 2702Cleavage; by viral proteaseBy similarity
    Sitei496 – 4972Cleavage; by viral proteaseBy similarity
    Sitei745 – 7462Cleavage; by viral proteaseBy similarity
    Active sitei771 – 7711Protease; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei833 – 8342Cleavage; by viral proteaseBy similarity
    Metal bindingi970 – 9701Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi1045 – 10451Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi1046 – 10461Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi1316 – 13161Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1346 – 13461Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1366 – 13661Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1429 – 14291Magnesium; catalytic; for RNase H activityBy similarity
    Sitei1437 – 14382Cleavage; by viral proteaseBy similarity
    Metal bindingi1501 – 15011Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1558 – 15581Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri525 – 54218CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri552 – 56918CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1436 – 147742Integrase-typePROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi1653 – 170250Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    4. nucleotide binding Source: UniProtKB-KW
    5. RNA binding Source: InterPro
    6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    7. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
    8. structural constituent of virion Source: UniProtKB-KW
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA integration Source: UniProtKB-KW
    2. DNA recombination Source: UniProtKB-KW
    3. dUTP metabolic process Source: InterPro
    4. establishment of integrated proviral latency Source: UniProtKB-KW
    5. viral entry into host cell 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, Virus entry into host cell

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Nucleotide-binding, Viral nucleoprotein, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag-Pro-Pol polyprotein
    Cleaved into the following 10 chains:
    Gene namesi
    Name:gag-pro-pol
    OrganismiMouse mammary tumor virus (strain C3H) (MMTV)
    Taxonomic identifieri11759 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeBetaretrovirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000006540: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Viral matrix protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 17551754Gag-Pro-Pol polyproteinPRO_0000125493Add
    BLAST
    Chaini2 – 9998Matrix protein p10PRO_0000403612Add
    BLAST
    Chaini100 – 19596Phosphorylated protein pp21PRO_0000403613Add
    BLAST
    Chaini196 – 22833Protein p3PRO_0000403614Add
    BLAST
    Chaini229 – 25224Protein p8Sequence AnalysisPRO_0000403615Add
    BLAST
    Chaini253 – 26917Protein nPRO_0000403616Add
    BLAST
    Chaini270 – 496227Capsid protein p27PRO_0000403617Add
    BLAST
    Chaini497 – 745249Nucleocapsid protein-dUTPaseSequence AnalysisPRO_0000403618Add
    BLAST
    Chaini746 – 83388ProteaseSequence AnalysisPRO_0000403619Add
    BLAST
    Chaini834 – 1437604Reverse transcriptase/ribonuclease HSequence AnalysisPRO_0000403620Add
    BLAST
    Chaini1438 – 1755318IntegraseSequence AnalysisPRO_0000403621Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins.2 Publications
    p10 is myristoylated.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    NC-dUTPase is a homotrimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP11283.
    SMRiP11283. Positions 550-580, 619-724.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini766 – 84176Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini905 – 1093189Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1307 – 1435129RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini1490 – 1647158Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi278 – 2814Poly-Asp
    Compositional biasi716 – 7194Poly-Leu

    Sequence similaritiesi

    Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
    Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
    Contains 1 RNase H domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri525 – 54218CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri552 – 56918CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1436 – 147742Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Family and domain databases

    Gene3Di1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    2.70.40.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR003322. B_retro_matrix_N.
    IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    PF02337. Gag_p10. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    ProDomiPD004265. B_retro_matrix_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00343. ZnF_C2HC. 2 hits.
    [Graphical view]
    SUPFAMiSSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF51283. SSF51283. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 2 hits.
    PROSITEiPS50175. 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. 1 hit.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by ribosomal frameshifting. Align

    Note: Translation results in the formation of the Gag-Pro. Ribosomal frameshifting at the gag-pro/pol genes boundary produces the Gag-Pro-Pol polyprotein.2 Publications

    Isoform Gag-Pro-Pol polyprotein (identifier: P11283-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG     50
    GLNLQDWKRV GREMKKYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL 100
    SAEAKSVTEE ELEEGLTGLL SASSQEKTYG TRGTAYAEID TEVDKLSEHI 150
    YDEPYEEKEK ADKNEEKDHV RKVKKIVQRK ENSEHKRKEK DQKAFLATDW 200
    NNDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVDKKKPL ALRRKPLPPV 250
    GFAGAMAEAR EKGDLTFTFP VVFMGESDDD DTPVWEPLPL KTLKELQSAV 300
    RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK 350
    SKETVQKTAG KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL 400
    AWRAIPPPGV KKTVLAGLKQ GNEESYETFI SRLEEAVYRM MPRGEGSDIL 450
    IKQLAWENAN SLCQDLIRPM RKTGTMQDYI RACLDASPAV VQGMAYAAAM 500
    RGQKYSTFVK QTYGGGKGGQ GSEGPVCFSC GKTGHIKRDC KEEKGSKRAP 550
    PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPT 600
    QKGDKGKDSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS 650
    LVPTLVKGTL PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA 700
    AKNAVIIHKG ERIAQLLLLP YLKLPNPIIK EERGSEGFGS TSHVHWVQEI 750
    SDSRPMLHIS LNGRRFLGLL DTGADKTCIA GRDWPANWPI HQTESSLQGL 800
    GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD IMKEIKVRLM 850
    TDSPDDSQDL MIGAIESNLF ADQISWKSDQ PVWLNQWPLK QEKLQALQQL 900
    VTEQLQLGHL EESNSPWNTP VFVIKKKSGK WRLLQDLRAV NATMHDMGAL 950
    QPGLPSPVAV PKGWEIIIID LQDCFFNIKL HPEDCKRFAF SVPSPNFKRP 1000
    YQRFQWKVLP QGMKNSPTLC QKFVDKAILT VRDKYQDSYI VHYMDDILLA 1050
    HPSRSIVDEI LTSMIQALNK HGLVVSTEKI QKYDNLKYLG THIQGDAVSY 1100
    QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL FEILNGDSNP 1150
    ISIRKLTPEA CKALQLVNER LSIARVKRLD LSRPWSLCIL KTEYTPTACL 1200
    WQNGVLEWIH LPHISPKVIT PYDIFCTQLI IKGRHRSKEL FSKDPDYIVV 1250
    PYTKVQFDLL LQEKEDWPIS LLGFLGEVHF HLPKDPLLTF TLQTAIIFPH 1300
    MTSTTPLEKG IVIFTDGSAN GRSVTYIQGR EPIIKENTQN TAQQAEIVAV 1350
    ITAFEEVSQS FNLYTDSKYV TGLFPEIETA TLSPRTKIYT ELRHLQRLIH 1400
    KRQEKFYIGH IRGHTGLPGP LAQGNAYADS LTRILTALES AQESHALHHQ 1450
    NAAALRFQFH ITREQAREIV KLCPNCPDWG HAPQLGVNPR GLKPRVLWQM 1500
    DVTHVSEFGK LKYVHVTVDT YSHFTFATAR TGEATKDVLQ HLAQSFAYMG 1550
    FPQKIKTDNA PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI 1600
    KAQLNKLQKA GKYYTPHHLL AHALFVLNHV NMDNQGHTAA ERHWGPISAD 1650
    PKPMVMWKDL LAGSWKGPDV LITAGRGYAC VFPQDAETPI WVPDRFIRPF 1700
    TERKEATPTP GTAEKTPPRD EKDQQKSPED ESSPHQREDG LATSAGVNLR 1750
    SGGGS 1755

    Note: Produced by -1 ribosomal frameshifting between gag-pro and pro-pol.

    Length:1,755
    Mass (Da):197,329
    Last modified:January 11, 2011 - v2
    Checksum:i0E99A2ADD96823A4
    GO
    Isoform Gag-Pro polyprotein (identifier: Q9IZT2-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q9IZT2.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by -1 ribosomal frameshifting between gag-pro.

    Length:860
    Mass (Da):95,593
    GO
    Isoform Gag polyprotein (identifier: P11284-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P11284.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:591
    Mass (Da):66,351
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti857 – 8604SQDL → FTGF in AAA66625. (PubMed:3035577)Curated
    Sequence conflicti867 – 8671S → T in AAA66625. (PubMed:3035577)Curated
    Sequence conflicti952 – 9521P → L in AAA66625. (PubMed:3035577)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti523 – 5231E → K.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF228552 Genomic DNA. Translation: AAF31474.1.
    M16766 Genomic RNA. Translation: AAA66623.1.
    M16766 Genomic RNA. Translation: AAA66625.1.
    PIRiB29029.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF228552 Genomic DNA. Translation: AAF31474.1 .
    M16766 Genomic RNA. Translation: AAA66623.1 .
    M16766 Genomic RNA. Translation: AAA66625.1 .
    PIRi B29029.

    3D structure databases

    ProteinModelPortali P11283.
    SMRi P11283. Positions 550-580, 619-724.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    2.70.40.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR003322. B_retro_matrix_N.
    IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    PF02337. Gag_p10. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    ProDomi PD004265. B_retro_matrix_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00343. ZnF_C2HC. 2 hits.
    [Graphical view ]
    SUPFAMi SSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF51283. SSF51283. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 2 hits.
    PROSITEi 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. 1 hit.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genetics of mouse mammary tumor virus-induced mammary tumors: linkage of tumor induction to the gag gene."
      Hook L.M., Agafonova Y., Ross S.R., Turner S.J., Golovkina T.V.
      J. Virol. 74:8876-8883(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Two efficient ribosomal frameshifting events are required for synthesis of mouse mammary tumor virus gag-related polyproteins."
      Jacks T., Townsley K., Varmus H.E., Majors J.
      Proc. Natl. Acad. Sci. U.S.A. 84:4298-4302(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-591 AND 857-970, RIBOSOMAL FRAMESHIFT.
    3. "Analysis of gag proteins from mouse mammary tumor virus."
      Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Krutzsch H.C., Oroszlan S.
      J. Virol. 63:2543-2549(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-58; 65-116; 194-218; 227-241; 251-252; 270-276 AND 362-591, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MYRISTOYLATION AT GLY-2.
    4. "Purification and characterization of the mouse mammary tumor virus protease expressed in Escherichia coli."
      Menendez-Arias L., Young M., Oroszlan S.
      J. Biol. Chem. 267:24134-24139(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    5. "The protein p30, encoded at the gag-pro junction of mouse mammary tumor virus, is a dUTPase fused with a nucleocapsid protein."
      Bergman A.C., Bjornberg O., Nord J., Nyman P.O., Rosengren A.M.
      Virology 204:420-424(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: RIBOSOMAL FRAMESHIFT, SUBUNIT, CHARACTERIZATION OF NC-DUTPASE.

    Entry informationi

    Entry nameiPOL_MMTVC
    AccessioniPrimary (citable) accession number: P11283
    Secondary accession number(s): Q9IZT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 76 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 swiching 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.PROSITE-ProRule annotation

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3