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P03355

- POL_MLVMS

UniProt

P03355 - POL_MLVMS

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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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.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
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

DNA integration, DNA recombination, 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
RNA-binding phosphoprotein p12
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
Reverse transcriptase/ribonuclease H p80 (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.4)
Short name:
RT
Integrase p46
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
Taxonomic identifieri928306 [NCBI]
Taxonomic lineageiViruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus ›
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000006625: Genome

Subcellular locationi

Chain Gag-Pol polyprotein : Host cell membrane Curated; Lipid-anchor Curated
Chain Matrix protein p15 : Virion Curated
Chain Capsid protein p30 : Virion Curated
Chain Nucleocapsid protein p10 : Virion Curated

GO - Cellular componenti

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

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
Turni488 – 4914Combined sources
Helixi496 – 4983Combined sources
Turni505 – 5073Combined sources
Beta strandi510 – 5123Combined sources
Helixi514 – 5163Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi524 – 5263Combined sources
Helixi529 – 5324Combined sources
Helixi684 – 6874Combined sources
Turni689 – 6913Combined sources
Helixi693 – 6964Combined sources
Beta strandi702 – 7043Combined sources
Helixi727 – 74216Combined sources
Beta strandi745 – 7495Combined sources
Beta strandi757 – 7604Combined sources
Beta strandi763 – 7664Combined sources
Beta strandi769 – 7724Combined sources
Helixi775 – 7784Combined sources
Helixi791 – 7955Combined sources
Beta strandi804 – 8107Combined sources
Turni811 – 8133Combined sources
Helixi814 – 8163Combined sources
Beta strandi817 – 8193Combined sources
Turni821 – 8233Combined sources
Helixi824 – 8274Combined sources
Beta strandi829 – 8335Combined sources
Helixi834 – 8363Combined sources
Beta strandi838 – 8469Combined sources
Helixi854 – 87219Combined sources
Beta strandi876 – 8816Combined sources
Beta strandi884 – 8918Combined sources
Helixi892 – 90918Combined sources
Turni915 – 9173Combined sources
Beta strandi919 – 9279Combined sources
Beta strandi930 – 9334Combined sources
Helixi941 – 9488Combined sources
Helixi956 – 96611Combined sources
Helixi967 – 9693Combined sources
Helixi976 – 9794Combined sources
Turni980 – 9856Combined sources
Helixi997 – 101115Combined sources
Beta strandi1025 – 104420Combined sources
Beta strandi1047 – 105711Combined sources
Helixi1060 – 10634Combined sources
Helixi1067 – 108620Combined sources
Beta strandi1091 – 10944Combined sources
Turni1100 – 11045Combined sources
Helixi1116 – 11238Combined sources
Turni1126 – 11283Combined sources
Beta strandi1129 – 11313Combined sources
Turni1139 – 11413Combined sources
Beta strandi1169 – 11713Combined sources
Beta strandi1177 – 118913Combined sources
Beta strandi1192 – 12009Combined sources
Beta strandi1205 – 12117Combined sources
Helixi1217 – 123115Combined sources
Turni1232 – 12343Combined sources
Beta strandi1235 – 12417Combined sources
Helixi1244 – 12496Combined sources
Helixi1273 – 128210Combined sources
Beta strandi1285 – 12939Combined sources
Helixi1303 – 132119Combined sources
Helixi1346 – 135510Combined sources
Beta strandi1358 – 13603Combined sources
Turni1361 – 13644Combined sources
Beta strandi1365 – 13684Combined sources
Beta strandi1371 – 13744Combined sources
Helixi1376 – 139015Combined sources
Helixi1394 – 14029Combined sources
Turni1403 – 14053Combined sources
Beta strandi1407 – 14104Combined sources
Helixi1413 – 142210Combined sources
Helixi1425 – 14317Combined sources
Beta strandi1661 – 16677Combined sources
Beta strandi1670 – 16734Combined sources
Beta strandi1676 – 168712Combined sources
Beta strandi1690 – 16934Combined sources
Beta strandi1696 – 16983Combined sources
Helixi1702 – 17043Combined sources
Beta strandi1705 – 17073Combined sources
Turni1714 – 17163Combined sources
Beta strandi1717 – 17193Combined sources
Turni1726 – 17283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MQVNMR-A479-534[»]
2MS0NMR-A/C479-534[»]
2MS1NMR-A479-534[»]
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 integrase-type DNA-binding domain.Curated
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.
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.
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

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        10         20         30         40         50
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW 
        60         70         80         90        100
PRDGTFNRDL ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF 
       110        120        130        140        150
VHPKPPPPLP PSAPSLPLEP PRSTPPRSSL YPALTPSLGA KPKPQVLSDS 
       160        170        180        190        200
GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG EATPAGEAPD PSPMASRLRG 
       210        220        230        240        250
RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN NNPSFSEDPG 
       260        270        280        290        300
KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 
       310        320        330        340        350
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN 
       360        370        380        390        400
LAKVKGITQG PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ 
       410        420        430        440        450
SAPDIGRKLE RLEDLKNKTL GDLVREAEKI FNKRETPEER EERIRRETEE 
       460        470        480        490        500
KEERRRTEDE QKEKERDRRR HREMSKLLAT VVSGQKQDRQ GGERRRSQLD 
       510        520        530        540        550
RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDGG GQGQEPPPEP 
       560        570        580        590        600
RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT 
       610        620        630        640        650
TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG 
       660        670        680        690        700
PMGQPLQVLT LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL 
       710        720        730        740        750
AVRQAPLIIP LKATSTPVSI KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ 
       760        770        780        790        800
SPWNTPLLPV KKPGTNDYRP VQDLREVNKR VEDIHPTVPN PYNLLSGLPP 
       810        820        830        840        850
SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG QLTWTRLPQG 
       860        870        880        890        900
FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR 
       910        920        930        940        950
ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ 
       960        970        980        990       1000
PTPKTPRQLR EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ 
      1010       1020       1030       1040       1050
KAYQEIKQAL LTAPALGLPD LTKPFELFVD EKQGYAKGVL TQKLGPWRRP 
      1060       1070       1080       1090       1100
VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK DAGKLTMGQP LVILAPHAVE 
      1110       1120       1130       1140       1150
ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA TLLPLPEEGL 
      1160       1170       1180       1190       1200
QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT 
      1210       1220       1230       1240       1250
TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA 
      1260       1270       1280       1290       1300
HIHGEIYRRR GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG 
      1310       1320       1330       1340       1350
HSAEARGNRM ADQAARKAAI TETPDTSTLL IENSSPYTSE HFHYTVTDIK 
      1360       1370       1380       1390       1400
DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF ELLDFLHQLT HLSFSKMKAL 
      1410       1420       1430       1440       1450
LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG TRVRGHRPGT 
      1460       1470       1480       1490       1500
HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE 
      1510       1520       1530       1540       1550
IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE 
      1560       1570       1580       1590       1600
RMNRTIKETL TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG 
      1610       1620       1630       1640       1650
APPPLVNFPD PDMTRVTNSP SLQAHLQALY LVQHEVWRPL AAAYQEQLDR 
      1660       1670       1680       1690       1700
PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP YTVLLTTPTA LKVDGIAAWI 
      1710       1720       1730 
HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP
Length:1,738
Mass (Da):194,841
Last modified:July 13, 2010 - v4
Checksum:iEDE353E6B09F91C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
2MQV NMR - A 479-534 [» ]
2MS0 NMR - A/C 479-534 [» ]
2MS1 NMR - A 479-534 [» ]
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.
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.
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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 143 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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