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P03355

- POL_MLVMS

UniProt

P03355 - POL_MLVMS

Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Gag-Pol polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release.
    Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex By similarity.By similarity
    Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
    Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.
    The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.PROSITE-ProRule annotation
    Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for 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
    Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome 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

    Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
    Binds 2 magnesium ions for ribonuclease H (RNase H) activity.By similarity
    Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.By similarity

    Enzyme regulationi

    The viral protease p14 is most effciently inhibited by amprenavir, which is able to block Gag processing in MoLV-infected cells.

    pH dependencei

    Optimum pH is 5.0 for protease activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei131 – 1322Cleavage; by viral protease p14
    Sitei215 – 2162Cleavage; by viral protease p14
    Sitei478 – 4792Cleavage; by viral protease p14
    Sitei534 – 5352Cleavage; by viral protease p14
    Active sitei566 – 5661Protease; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei659 – 6602Cleavage; by viral protease p14
    Metal bindingi809 – 8091Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi883 – 8831Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi884 – 8841Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi1183 – 11831Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1221 – 12211Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1242 – 12421Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1312 – 13121Magnesium; for RNase H activityPROSITE-ProRule annotation
    Sitei1330 – 13312Cleavage; by viral protease p14
    Metal bindingi1455 – 14551Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1514 – 15141Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri502 – 51918CCHC-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. RNA binding Source: UniProtKB-KW
    5. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    6. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
    7. structural constituent of virion Source: UniProtKB-KW
    8. zinc ion binding Source: InterPro

    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. virion assembly Source: InterPro

    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, Host-virus interaction, Viral genome integration, Virus entry into host cell

    Keywords - Ligandi

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

    Protein family/group databases

    MEROPSiA02.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag-Pol polyprotein
    Short name:
    Pr180gag-pol
    Cleaved into the following 7 chains:
    Matrix protein p15
    Short name:
    MA
    Alternative name(s):
    pp12
    Capsid protein p30
    Short name:
    CA
    Nucleocapsid protein p10
    Short name:
    NC-pol
    Protease p14 (EC:3.4.23.-)
    Short name:
    PR
    Integrase p46
    Short name:
    IN
    Gene namesi
    Name:gag-pol
    OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
    Taxonomic identifieri928306 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000006625: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-KW
    3. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host membrane, Membrane, Viral matrix protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141P → A: Slight reduction in the number of virus-like particles produced.
    Mutagenesisi137 – 1371S → A: No effect on reverse transcription activity. 1 Publication
    Mutagenesisi148 – 1481S → A: No effect on reverse transcription activity; when associated with A-150. 1 Publication
    Mutagenesisi150 – 1501S → A: No effect on reverse transcription activity; when associated with A-148. 1 Publication
    Mutagenesisi165 – 1651Y → A: Drastic reduction in the number of virus-like particles produced. 1 Publication
    Mutagenesisi192 – 1921S → A: Complete loss of reverse transcription activity. 1 Publication
    Mutagenesisi192 – 1921S → D: Complete loss of reverse transcription activity. 1 Publication
    Mutagenesisi196 – 1961S → A: No effect on reverse transcription activity. 1 Publication
    Mutagenesisi209 – 2091S → A: Strongly reduced reverse transcription activity. 1 Publication
    Mutagenesisi209 – 2091S → D: Strongly reduced reverse transcription activity. 1 Publication
    Mutagenesisi212 – 2121S → A: No effect on reverse transcription activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host1 Publication
    Chaini2 – 17381737Gag-Pol polyproteinPRO_0000390795Add
    BLAST
    Chaini2 – 131130Matrix protein p15PRO_5000053618Add
    BLAST
    Chaini132 – 21584RNA-binding phosphoprotein p12PRO_5000053619Add
    BLAST
    Chaini216 – 478263Capsid protein p30PRO_5000053620Add
    BLAST
    Chaini479 – 53456Nucleocapsid protein p10PRO_5000053621Add
    BLAST
    Chaini535 – 659125Protease p14PRO_5000053622Add
    BLAST
    Chaini660 – 1330671Reverse transcriptase/ribonuclease H p80PRO_5000053623Add
    BLAST
    Chaini1331 – 1738408Integrase p46PRO_5000053624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
    Modified residuei192 – 1921Phosphoserine; by host1 Publication

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation By similarity.By similarity
    Capsid protein p30 is sumoylated; which is required for virus replication.1 Publication
    RNA-binding phosphoprotein p12 is phosphorylated on serine residues.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    PTM databases

    PhosphoSiteiP03355.

    Miscellaneous databases

    PMAP-CutDBO92808.

    Interactioni

    Subunit structurei

    Capsid protein p30 is a homohexamer, that further associates as homomultimer. The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a monomer By similarity. Capsid protein p30 interacts with mouse UBE2I and mouse PIAS4. Reverse transcriptase/ribonuclease H p80 interacts (via RT and RNase domains) with host release factor ETF1; this interaction is essential for translational readthrough of amber codon between viral gag and pol genes. Gag-Pol polyprotein also interacts with host release factor ETF1.By similarity3 Publications

    Structurei

    Secondary structure

    1
    1738
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi684 – 6874
    Turni689 – 6913
    Helixi693 – 6964
    Beta strandi702 – 7043
    Helixi727 – 74216
    Beta strandi745 – 7495
    Beta strandi757 – 7604
    Beta strandi763 – 7664
    Beta strandi769 – 7724
    Helixi775 – 7784
    Helixi791 – 7955
    Beta strandi804 – 8107
    Turni811 – 8133
    Helixi814 – 8163
    Beta strandi817 – 8193
    Turni821 – 8233
    Helixi824 – 8274
    Beta strandi829 – 8335
    Helixi834 – 8363
    Beta strandi838 – 8469
    Helixi854 – 87219
    Beta strandi876 – 8816
    Beta strandi884 – 8918
    Helixi892 – 90918
    Turni915 – 9173
    Beta strandi919 – 9279
    Beta strandi930 – 9334
    Helixi941 – 9488
    Helixi956 – 96611
    Helixi967 – 9693
    Helixi976 – 9794
    Turni980 – 9856
    Helixi997 – 101115
    Beta strandi1025 – 104420
    Beta strandi1047 – 105711
    Helixi1060 – 10634
    Helixi1067 – 108620
    Beta strandi1091 – 10944
    Turni1100 – 11045
    Helixi1116 – 11238
    Turni1126 – 11283
    Beta strandi1129 – 11313
    Turni1139 – 11413
    Beta strandi1169 – 11713
    Beta strandi1177 – 118913
    Beta strandi1192 – 12009
    Beta strandi1205 – 12117
    Helixi1217 – 123115
    Turni1232 – 12343
    Beta strandi1235 – 12417
    Helixi1244 – 12496
    Helixi1273 – 128210
    Beta strandi1285 – 12939
    Helixi1303 – 132119
    Helixi1346 – 135510
    Beta strandi1358 – 13603
    Turni1361 – 13644
    Beta strandi1365 – 13684
    Beta strandi1371 – 13744
    Helixi1376 – 139015
    Helixi1394 – 14029
    Turni1403 – 14053
    Beta strandi1407 – 14104
    Helixi1413 – 142210
    Helixi1425 – 14317
    Beta strandi1661 – 16677
    Beta strandi1670 – 16734
    Beta strandi1676 – 168712
    Beta strandi1690 – 16934
    Beta strandi1696 – 16983
    Helixi1702 – 17043
    Beta strandi1705 – 17073
    Turni1714 – 17163
    Beta strandi1717 – 17193
    Turni1726 – 17283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D0EX-ray3.00A/B683-937[»]
    1D1UX-ray2.30A683-937[»]
    1I6JX-ray2.00A683-937[»]
    1MMLX-ray1.80A669-933[»]
    1N4LX-ray2.00A683-937[»]
    1NNDX-ray2.30A683-937[»]
    1QAIX-ray2.30A/B669-933[»]
    1QAJX-ray2.30A/B683-937[»]
    1ZTTX-ray1.85A683-937[»]
    1ZTWX-ray1.80A683-937[»]
    2FJVX-ray2.05A683-937[»]
    2FJWX-ray1.95A683-937[»]
    2FJXX-ray1.80A683-937[»]
    2FVPX-ray2.25A683-937[»]
    2FVQX-ray2.30A683-937[»]
    2FVRX-ray2.20A683-937[»]
    2FVSX-ray2.35A683-937[»]
    2HB5X-ray1.59A1157-1330[»]
    2M9UNMR-A1659-1738[»]
    2R2RX-ray2.10A683-937[»]
    2R2SX-ray2.80A683-937[»]
    2R2TX-ray2.00A683-937[»]
    2R2UX-ray2.30A683-937[»]
    3FSIX-ray1.75A683-937[»]
    3NNQX-ray2.69A/B1331-1435[»]
    4M94X-ray2.14A683-937[»]
    4M95X-ray1.72A683-937[»]
    4MH8X-ray3.00A683-1330[»]
    4NZGX-ray2.15A/B/C/D1338-1435[»]
    DisProtiDP00651.
    ProteinModelPortaliP03355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03355.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini560 – 63172Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini741 – 932192Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1174 – 1320147RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini1444 – 1602159Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili438 – 47841Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi111 – 1144PTAP/PSAP motif
    Motifi130 – 1345LYPX(n)L motif
    Motifi162 – 1654PPXY motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 193123Pro-richAdd
    BLAST

    Domaini

    Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. contains By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.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 fingeri502 – 51918CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Family and domain databases

    Gene3Di1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR001584. Integrase_cat-core.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P03355-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW     50
    PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF 100
    VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS 150
    GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG 200
    RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG 250
    KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 300
    PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN 350
    LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ 400
    SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE 450
    KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD 500
    RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDGG GQGQEPPPEP 550
    RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT 600
    TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG 650
    PMGQPLQVLT LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL 700
    AVRQAPLIIP LKATSTPVSI KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ 750
    SPWNTPLLPV KKPGTNDYRP VQDLREVNKR VEDIHPTVPN PYNLLSGLPP 800
    SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG QLTWTRLPQG 850
    FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR 900
    ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ 950
    PTPKTPRQLR EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ 1000
    KAYQEIKQAL LTAPALGLPD LTKPFELFVD EKQGYAKGVL TQKLGPWRRP 1050
    VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK DAGKLTMGQP LVILAPHAVE 1100
    ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA TLLPLPEEGL 1150
    QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT 1200
    TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA 1250
    HIHGEIYRRR GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG 1300
    HSAEARGNRM ADQAARKAAI TETPDTSTLL IENSSPYTSE HFHYTVTDIK 1350
    DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF ELLDFLHQLT HLSFSKMKAL 1400
    LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG TRVRGHRPGT 1450
    HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE 1500
    IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE 1550
    RMNRTIKETL TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG 1600
    APPPLVNFPD PDMTRVTNSP SLQAHLQALY LVQHEVWRPL AAAYQEQLDR 1650
    PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP YTVLLTTPTA LKVDGIAAWI 1700
    HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP 1738
    Length:1,738
    Mass (Da):194,841
    Last modified:July 13, 2010 - v4
    Checksum:iEDE353E6B09F91C6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033811 Genomic RNA. Translation: AAC82568.1. Sequence problems.
    J02255 Genomic RNA. No translation available.
    PIRiA03956. GNMV1M.
    RefSeqiNP_057933.2. NC_001501.1.

    Genome annotation databases

    GeneIDi2193424.

    Keywords - Coding sequence diversityi

    RNA suppression of termination

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF033811 Genomic RNA. Translation: AAC82568.1 . Sequence problems.
    J02255 Genomic RNA. No translation available.
    PIRi A03956. GNMV1M.
    RefSeqi NP_057933.2. NC_001501.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D0E X-ray 3.00 A/B 683-937 [» ]
    1D1U X-ray 2.30 A 683-937 [» ]
    1I6J X-ray 2.00 A 683-937 [» ]
    1MML X-ray 1.80 A 669-933 [» ]
    1N4L X-ray 2.00 A 683-937 [» ]
    1NND X-ray 2.30 A 683-937 [» ]
    1QAI X-ray 2.30 A/B 669-933 [» ]
    1QAJ X-ray 2.30 A/B 683-937 [» ]
    1ZTT X-ray 1.85 A 683-937 [» ]
    1ZTW X-ray 1.80 A 683-937 [» ]
    2FJV X-ray 2.05 A 683-937 [» ]
    2FJW X-ray 1.95 A 683-937 [» ]
    2FJX X-ray 1.80 A 683-937 [» ]
    2FVP X-ray 2.25 A 683-937 [» ]
    2FVQ X-ray 2.30 A 683-937 [» ]
    2FVR X-ray 2.20 A 683-937 [» ]
    2FVS X-ray 2.35 A 683-937 [» ]
    2HB5 X-ray 1.59 A 1157-1330 [» ]
    2M9U NMR - A 1659-1738 [» ]
    2R2R X-ray 2.10 A 683-937 [» ]
    2R2S X-ray 2.80 A 683-937 [» ]
    2R2T X-ray 2.00 A 683-937 [» ]
    2R2U X-ray 2.30 A 683-937 [» ]
    3FSI X-ray 1.75 A 683-937 [» ]
    3NNQ X-ray 2.69 A/B 1331-1435 [» ]
    4M94 X-ray 2.14 A 683-937 [» ]
    4M95 X-ray 1.72 A 683-937 [» ]
    4MH8 X-ray 3.00 A 683-1330 [» ]
    4NZG X-ray 2.15 A/B/C/D 1338-1435 [» ]
    DisProti DP00651.
    ProteinModelPortali P03355.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL3562.

    Protein family/group databases

    MEROPSi A02.008.

    PTM databases

    PhosphoSitei P03355.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2193424.

    Miscellaneous databases

    EvolutionaryTracei P03355.
    PMAP-CutDB O92808.

    Family and domain databases

    Gene3Di 1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR001584. Integrase_cat-core.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of Moloney murine leukaemia virus."
      Shinnick T.M., Lerner R.A., Sutcliffe J.G.
      Nature 293:543-548(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE PMLV-1).
    2. Chappey C.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Myristyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational proteins modification."
      Henderson L.E., Krutzsch H.C., Oroszlan S.
      Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31, MYRISTOYLATION AT GLY-2.
    4. "Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses."
      Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.
      J. Biol. Chem. 256:8400-8406(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 479-529.
    5. "Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon."
      Yoshinaka Y., Katoh I., Copeland T.D., Oroszlan S.
      Proc. Natl. Acad. Sci. U.S.A. 82:1618-1622(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: READTHROUGH OF AMBER CODON.
    6. "Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection."
      Yueh A., Goff S.P.
      J. Virol. 77:1820-1829(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-192, MUTAGENESIS OF SER-137; SER-148; SER-150; SER-192; SER-196; SER-209 AND SER-212.
    7. "Reverse transcriptase of Moloney murine leukemia virus binds to eukaryotic release factor 1 to modulate suppression of translational termination."
      Orlova M., Yueh A., Leung J., Goff S.P.
      Cell 115:319-331(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF REVERSE TRANSCRIPTASE/RIBONUCLEASE H P80 WITH MOUSE RELEASE FACTOR ETF1, INTERACTION OF GAG-POL POLYPROTEIN WITH MOUSE RELEASE FACTOR ETF1.
    8. "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding."
      Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E.
      J. Biol. Chem. 280:27004-27012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX, MUTAGENESIS OF TYR-165.
    9. "Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection."
      Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-Y., Goff S.P.
      J. Virol. 80:342-352(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I AND PIAS4, SUMOYLATION.
    10. "Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease."
      Feher A., Boross P., Sperka T., Miklossy G., Kadas J., Bagossi P., Oroszlan S., Weber I.T., Tozser J.
      J. Gen. Virol. 87:1321-1330(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF PROTEASE P14, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    11. "Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase."
      Georgiadis M.M., Jessen S.M., Ogata C.M., Telesnitsky A., Goff S.P., Hendrickson W.A.
      Structure 3:879-892(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 683-937.

    Entry informationi

    Entry nameiPOL_MLVMS
    AccessioniPrimary (citable) accession number: P03355
    Secondary accession number(s): O92808
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is translated as a gag-pol fusion protein by episodic readthrough of the gag protein termination codon. Readthrough of the terminator codon TAG occurs between the codons for 538-Asp and 540-Gly.
    The nucleocapsid protein p10 released from Pol polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid protein p10 released from Gag polyprotein (NC-gag).
    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

    3D-structure, Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3