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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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-Pol, or to Gag-Pol binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.By similarity
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 pre-integration complex.By similarity
RNA-binding phosphoprotein p12: Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes. This allows the integration of the viral genome into the host DNA.2 Publications
Capsid protein p30: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p10-Pol: Involved in the packaging and encapsidation of two copies of the genome (By similarity). Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome (By similarity). This binding is dependent on genome dimerization (By similarity). Acts as a nucleic acid chaperone which is involved in rearrangement of nucleic acid secondary structures during gRNA retrotranscription (PubMed:25209668).By similarity1 Publication
Protease: 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 (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (PubMed:14610163).PROSITE-ProRule annotation1 Publication
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.Sequence analysis
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.2 Publications

Miscellaneous

Gag-Pol polyprotein: 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.2 Publications
Nucleocapsid protein p10-Pol: Nucleocapsid protein p10-Pol released from Pol polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid protein p10 released from Gag polyprotein (NC-gag).Curated
Reverse transcriptase/ribonuclease H: 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

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:

Activity regulationi

Protease: Most efficiently inhibited by Amprenavir, which is able to block Gag-Pol processing in infected cells.1 Publication

pH dependencei

Optimum pH is 5.0 for protease activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei566Protease; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi809Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi883Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi884Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1183Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication1
Metal bindingi1221Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication1
Metal bindingi1242Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1 Publication1
Metal bindingi1312MagnesiumPROSITE-ProRule annotation1 Publication1
Metal bindingi1455Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1514Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri502 – 519CCHC-typePROSITE-ProRule annotation1 PublicationAdd BLAST18
Zinc fingeri1387 – 1427HHCC-type1 PublicationAdd BLAST41

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processDNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral genome integration, Virus entry into host cell
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.49 3393
3.1.13.2 3393
3.4.23.B5 3393

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
Protease (EC:3.4.23.-PROSITE-ProRule annotation2 Publications)
Short name:
PR
Alternative name(s):
p14
Reverse transcriptase/ribonuclease H (EC:2.7.7.49PROSITE-ProRule annotation, EC:2.7.7.7PROSITE-ProRule annotation, EC:3.1.26.4PROSITE-ProRule annotation)
Short name:
RT
Alternative name(s):
p80
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
Alternative name(s):
p46
Gene namesi
Name:gag-pol
OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
Taxonomic identifieri928306 [NCBI]
Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000006625 Componenti: Genome
  • UP000180702 Componenti: Genome

Subcellular locationi

Gag-Pol polyprotein :
Protease :
RNA-binding phosphoprotein p12 :

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi114P → A: Slight reduction in the number of virus-like particles produced. 1
Mutagenesisi137S → A: No effect on reverse transcription activity. 1 Publication1
Mutagenesisi148S → A: No effect on reverse transcription activity; when associated with A-150. 1 Publication1
Mutagenesisi150S → A: No effect on reverse transcription activity; when associated with A-148. 1 Publication1
Mutagenesisi165Y → A: Drastic reduction in the number of virus-like particles produced. 1 Publication1
Mutagenesisi192S → A: Complete loss of reverse transcription activity. 1 Publication1
Mutagenesisi192S → A: Complete loss of stable anchoring of viral PIC to mitotic chromosomes; when associated with A-196. 1 Publication1
Mutagenesisi192S → D: Complete loss of reverse transcription activity. 1 Publication1
Mutagenesisi196S → A: Complete loss of stable anchoring of viral PIC to mitotic chromosomes; when associated with A-192. 1 Publication1
Mutagenesisi196S → A: No effect on reverse transcription activity. 1 Publication1
Mutagenesisi209S → A: Strongly reduced reverse transcription activity. 1 Publication1
Mutagenesisi209S → D: Strongly reduced reverse transcription activity. 1 Publication1
Mutagenesisi212S → A: No effect on reverse transcription activity. 1 Publication1
Mutagenesisi1244R → A: No effect on readthrough between Gag and Pol. 1 Publication1
Mutagenesisi1247F → A: No effect on readthrough between Gag and Pol. 1 Publication1
Mutagenesisi1248A → K: Almost complete loss of readthrough between Gag and Pol. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3562

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostSequence analysis1 Publication
ChainiPRO_00003907952 – 1738Gag-Pol polyproteinAdd BLAST1737
ChainiPRO_50000536182 – 131Matrix protein p15Add BLAST130
ChainiPRO_5000053619132 – 215RNA-binding phosphoprotein p12Add BLAST84
ChainiPRO_5000053620216 – 478Capsid protein p30Add BLAST263
ChainiPRO_5000053621479 – 534Nucleocapsid protein p10-PolAdd BLAST56
ChainiPRO_5000053622535 – 659ProteaseAdd BLAST125
ChainiPRO_5000053623660 – 1330Reverse transcriptase/ribonuclease HAdd BLAST671
ChainiPRO_50000536241331 – 1738IntegraseAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostSequence analysis1 Publication1
Modified residuei192Phosphoserine; by host1 Publication1

Post-translational modificationi

Gag-Pol polyprotein: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination.By similarity
Gag-Pol polyprotein: 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.1 Publication
Capsid protein p30: Sumoylated; which is required for virus replication.1 Publication
RNA-binding phosphoprotein p12: Phosphorylated on serine residues.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei131 – 132Cleavage; by viral protease1 Publication2
Sitei215 – 216Cleavage; by viral protease1 Publication2
Sitei478 – 479Cleavage; by viral protease1 Publication2
Sitei534 – 535Cleavage; by viral protease1 Publication2
Sitei659 – 660Cleavage; by viral protease1 Publication2
Sitei1330 – 1331Cleavage; by viral protease1 Publication2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP03355

PTM databases

iPTMnetiP03355
PhosphoSitePlusiP03355

Interactioni

Subunit structurei

Capsid protein p30: Homohexamer; further associates as homomultimer (By similarity). Capsid protein p30: The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers (PubMed:12093170). Capsid protein p30: Interacts with mouse UBE2I and mouse PIAS4 (PubMed:16352559). Gag-Pol polyprotein: Interacts (via PPXY motif) with host NEDD4 (PubMed:15908698). Gag-Pol polyprotein: Interacts (via PSAP motif) with host TSG101 (PubMed:15908698). Gag-Pol polyprotein: Interacts (via LYPX(n)L motif) with host PDCD6IP (PubMed:15908698). Reverse transcriptase/ribonuclease H: The reverse transcriptase is a monomer (Potential). Reverse transcriptase/ribonuclease H: Interacts (via RNase domains) with host release factor ETF1; this interaction is essential for translational readthrough of amber codon between viral gag and pol genes, as well as for viral replication (PubMed:14636559, PubMed:27329342). Integrase: Homodimer (PubMed:14599799).PROSITE-ProRule annotationBy similarity6 Publications

Protein-protein interaction databases

ELMiP03355

Structurei

Secondary structure

11738
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00651
ProteinModelPortaliP03355
SMRiP03355
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03355

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini560 – 631Peptidase A2PROSITE-ProRule annotationAdd BLAST72
Domaini741 – 932Reverse transcriptasePROSITE-ProRule annotationAdd BLAST192
Domaini1174 – 1320RNase HPROSITE-ProRule annotationAdd BLAST147
Domaini1444 – 1602Integrase catalyticPROSITE-ProRule annotationAdd BLAST159

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni345 – 393Interaction with host PIAS4By similarityAdd BLAST49
Regioni430 – 435Interaction with host UBE2IBy similarity6

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili438 – 478Sequence analysisAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi111 – 114PTAP/PSAP motifBy similarity4
Motifi130 – 134LYPX(n)L motifBy similarity5
Motifi162 – 165PPXY motifBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi71 – 193Pro-richPROSITE-ProRule annotationAdd BLAST123
Compositional biasi440 – 501Arg-richPROSITE-ProRule annotationAdd BLAST62

Domaini

Gag-Pol polyprotein: 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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri502 – 519CCHC-typePROSITE-ProRule annotation1 PublicationAdd BLAST18
Zinc fingeri1387 – 1427HHCC-type1 PublicationAdd BLAST41

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

OrthoDBiVOG090000AJ

Family and domain databases

CDDicd06095 RP_RTVL_H_like, 1 hit
Gene3Di1.10.150.180, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
3.30.420.10, 2 hits
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000840 G_retro_matrix
IPR036946 G_retro_matrix_sf
IPR039464 Gag-pol_Znf-H3C2
IPR002079 Gag_p12
IPR003036 Gag_P30
IPR001584 Integrase_cat-core
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR034145 RP_RTVL-H-like
IPR000477 RT_dom
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
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
PF00098 zf-CCHC, 1 hit
PF16721 zf-H3C2, 1 hit
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 1 hit
SUPFAMiSSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

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

P03355-1 [UniParc]FASTAAdd to basket
« Hide
        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 TSLLTLDDQG 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):194,912
Last modified:January 31, 2018 - v5
Checksum:i3DF085F6E5EFCA83
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
KEGGivg:2193424

Keywords - Coding sequence diversityi

RNA suppression of termination

Similar proteinsi

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.
PIRiA03956 GNMV1M
RefSeqiNP_057933.2, NC_001501.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XO0X-ray1.70A683-937[»]
4XPCX-ray1.68A683-937[»]
4XPEX-ray1.78A683-937[»]
5DMQX-ray4.00A683-1330[»]
5DMRX-ray2.80A1159-1330[»]
5VBSX-ray1.75A683-937[»]
6B1QX-ray1.90A683-937[»]
6B1RX-ray1.69A683-937[»]
6B1SX-ray2.00A/B683-937[»]
DisProtiDP00651
ProteinModelPortaliP03355
SMRiP03355
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ELMiP03355

Chemistry databases

ChEMBLiCHEMBL3562

Protein family/group databases

MEROPSiA02.008

PTM databases

iPTMnetiP03355
PhosphoSitePlusiP03355

Proteomic databases

PRIDEiP03355

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2193424
KEGGivg:2193424

Phylogenomic databases

OrthoDBiVOG090000AJ

Enzyme and pathway databases

BRENDAi2.7.7.49 3393
3.1.13.2 3393
3.4.23.B5 3393

Miscellaneous databases

EvolutionaryTraceiP03355
PROiPR:P03355

Family and domain databases

CDDicd06095 RP_RTVL_H_like, 1 hit
Gene3Di1.10.150.180, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
3.30.420.10, 2 hits
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000840 G_retro_matrix
IPR036946 G_retro_matrix_sf
IPR039464 Gag-pol_Znf-H3C2
IPR002079 Gag_p12
IPR003036 Gag_P30
IPR001584 Integrase_cat-core
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR008919 Retrov_capsid_N
IPR010999 Retrovr_matrix
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR034145 RP_RTVL-H-like
IPR000477 RT_dom
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
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
PF00098 zf-CCHC, 1 hit
PF16721 zf-H3C2, 1 hit
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 1 hit
SUPFAMiSSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiPOL_MLVMS
AccessioniPrimary (citable) accession number: P03355
Secondary accession number(s): O92808
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 31, 2018
Last modified: November 7, 2018
This is version 170 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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