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P03355 (POL_MLVMS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gag-Pol polyprotein

Short name=Pr180gag-pol

Cleaved into the following 7 chains:

  1. Matrix protein p15
    Short name=MA
  2. RNA-binding phosphoprotein p12
    Alternative name(s):
    pp12
  3. Capsid protein p30
    Short name=CA
  4. Nucleocapsid protein p10
    Short name=NC-pol
  5. Protease p14
    Short name=PR
    EC=3.4.23.-
  6. Reverse transcriptase/ribonuclease H p80
    Short name=RT
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.4
  7. Integrase p46
    Short name=IN
Gene names
Name:gag-pol
OrganismMoloney murine leukemia virus (isolate Shinnick) (MoMLV) [Reference proteome]
Taxonomic identifier928306 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length1738 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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 By similarity.

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.

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.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Endonucleolytic cleavage to 5'-phosphomonoester.

Cofactor

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.

Enzyme regulation

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

Subunit structure

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. Ref.7 Ref.8 Ref.9

Subcellular location

Gag-Pol polyprotein: Host cell membrane; Lipid-anchor Potential.

Matrix protein p15: Virion Potential.

Capsid protein p30: Virion Potential.

Nucleocapsid protein p10: Virion Potential.

Domain

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.

Post-translational modification

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. Ref.10

Capsid protein p30 is sumoylated; which is required for virus replication. Ref.9

RNA-binding phosphoprotein p12 is phosphorylated on serine residues. Ref.6

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 By similarity.

Sequence similarities

Contains 1 CCHC-type zinc finger.

Contains 1 integrase catalytic domain.

Contains 1 integrase-type DNA-binding domain.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0 for protease activity.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Host-virus interaction
Viral genome integration
Virus entry into host cell
   Cellular componentCapsid protein
Host cell membrane
Host membrane
Membrane
Viral matrix protein
Virion
   Coding sequence diversityRNA suppression of termination
   DomainCoiled coil
Zinc-finger
   LigandDNA-binding
Magnesium
Metal-binding
RNA-binding
Viral nucleoprotein
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

establishment of integrated proviral latency

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of virion

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host Ref.3
Chain2 – 17381737Gag-Pol polyprotein
PRO_0000390795
Chain2 – 131130Matrix protein p15
PRO_5000053618
Chain132 – 21584RNA-binding phosphoprotein p12
PRO_5000053619
Chain216 – 478263Capsid protein p30
PRO_5000053620
Chain479 – 53456Nucleocapsid protein p10
PRO_5000053621
Chain535 – 659125Protease p14
PRO_5000053622
Chain660 – 1330671Reverse transcriptase/ribonuclease H p80
PRO_5000053623
Chain1331 – 1738408Integrase p46
PRO_5000053624

Regions

Domain560 – 63172Peptidase A2
Domain741 – 932192Reverse transcriptase
Domain1174 – 1320147RNase H
Domain1444 – 1602159Integrase catalytic
Zinc finger502 – 51918CCHC-type
Coiled coil438 – 47841 Potential
Motif111 – 1144PTAP/PSAP motif
Motif130 – 1345LYPX(n)L motif
Motif162 – 1654PPXY motif
Compositional bias71 – 193123Pro-rich

Sites

Active site5661Protease; shared with dimeric partner By similarity
Metal binding8091Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding8831Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding8841Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding11831Magnesium; for RNase H activity By similarity
Metal binding12211Magnesium; for RNase H activity By similarity
Metal binding12421Magnesium; for RNase H activity By similarity
Metal binding13121Magnesium; for RNase H activity By similarity
Metal binding14551Magnesium; catalytic; for integrase activity By similarity
Metal binding15141Magnesium; catalytic; for integrase activity By similarity
Site131 – 1322Cleavage; by viral protease p14
Site215 – 2162Cleavage; by viral protease p14
Site478 – 4792Cleavage; by viral protease p14
Site534 – 5352Cleavage; by viral protease p14
Site659 – 6602Cleavage; by viral protease p14
Site1330 – 13312Cleavage; by viral protease p14

Amino acid modifications

Modified residue1921Phosphoserine; by host Probable
Lipidation21N-myristoyl glycine; by host Ref.3

Experimental info

Mutagenesis1141P → A: Slight reduction in the number of virus-like particles produced.
Mutagenesis1371S → A: No effect on reverse transcription activity. Ref.6
Mutagenesis1481S → A: No effect on reverse transcription activity; when associated with A-150. Ref.6
Mutagenesis1501S → A: No effect on reverse transcription activity; when associated with A-148. Ref.6
Mutagenesis1651Y → A: Drastic reduction in the number of virus-like particles produced. Ref.8
Mutagenesis1921S → A: Complete loss of reverse transcription activity. Ref.6
Mutagenesis1921S → D: Complete loss of reverse transcription activity. Ref.6
Mutagenesis1961S → A: No effect on reverse transcription activity. Ref.6
Mutagenesis2091S → A: Strongly reduced reverse transcription activity. Ref.6
Mutagenesis2091S → D: Strongly reduced reverse transcription activity. Ref.6
Mutagenesis2121S → A: No effect on reverse transcription activity. Ref.6

Secondary structure

....................................................................................................................................... 1738
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03355 [UniParc].

Last modified July 13, 2010. Version 4.
Checksum: EDE353E6B09F91C6

FASTA1,738194,841
        10         20         30         40         50         60 
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL 

        70         80         90        100        110        120 
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP 

       130        140        150        160        170        180 
PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG 

       190        200        210        220        230        240 
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN 

       250        260        270        280        290        300 
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 

       310        320        330        340        350        360 
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG 

       370        380        390        400        410        420 
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL 

       430        440        450        460        470        480 
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT 

       490        500        510        520        530        540 
VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDGG 

       550        560        570        580        590        600 
GQGQEPPPEP RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT 

       610        620        630        640        650        660 
TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG PMGQPLQVLT 

       670        680        690        700        710        720 
LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL AVRQAPLIIP LKATSTPVSI 

       730        740        750        760        770        780 
KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ SPWNTPLLPV KKPGTNDYRP VQDLREVNKR 

       790        800        810        820        830        840 
VEDIHPTVPN PYNLLSGLPP SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG 

       850        860        870        880        890        900 
QLTWTRLPQG FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR 

       910        920        930        940        950        960 
ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ PTPKTPRQLR 

       970        980        990       1000       1010       1020 
EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ KAYQEIKQAL LTAPALGLPD 

      1030       1040       1050       1060       1070       1080 
LTKPFELFVD EKQGYAKGVL TQKLGPWRRP VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK 

      1090       1100       1110       1120       1130       1140 
DAGKLTMGQP LVILAPHAVE ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA 

      1150       1160       1170       1180       1190       1200 
TLLPLPEEGL QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT 

      1210       1220       1230       1240       1250       1260 
TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA HIHGEIYRRR 

      1270       1280       1290       1300       1310       1320 
GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG HSAEARGNRM ADQAARKAAI 

      1330       1340       1350       1360       1370       1380 
TETPDTSTLL IENSSPYTSE HFHYTVTDIK DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF 

      1390       1400       1410       1420       1430       1440 
ELLDFLHQLT HLSFSKMKAL LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG 

      1450       1460       1470       1480       1490       1500 
TRVRGHRPGT HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE 

      1510       1520       1530       1540       1550       1560 
IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE RMNRTIKETL 

      1570       1580       1590       1600       1610       1620 
TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG APPPLVNFPD PDMTRVTNSP 

      1630       1640       1650       1660       1670       1680 
SLQAHLQALY LVQHEVWRPL AAAYQEQLDR PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP 

      1690       1700       1710       1720       1730 
YTVLLTTPTA LKVDGIAAWI HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF033811 Genomic RNA. Translation: AAC82568.1. Sequence problems.
J02255 Genomic RNA. No translation available.
PIRGNMV1M. A03956.
RefSeqNP_057933.2. NC_001501.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00651.
ProteinModelPortalP03355.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL3562.

Protein family/group databases

MEROPSA02.008.

PTM databases

PhosphoSiteP03355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2193424.

Family and domain databases

Gene3D1.10.150.180. 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.
InterProIPR001969. 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]
PfamPF01140. 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]
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEPS50175. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP03355.
PMAP-CutDBO92808.

Entry information

Entry namePOL_MLVMS
AccessionPrimary (citable) accession number: P03355
Secondary accession number(s): O92808
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references