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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-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 p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome.By similarity
The aspartyl protease mediates proteolytic cleavages of Gag, Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Hydrolyzes host EIF4GI in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity
Reverse transcriptase (RT) is a multifunctional enzyme that converts the viral 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-Pro 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 primer. 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 dinucleotides OH's at the 3' ends. In the second step, the PIC access cell chromosomes during cell division. 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 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands (see above) are filled in and then ligated (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei481 – 4811For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
Metal bindingi680 – 6801Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi755 – 7551Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi756 – 7561Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi1040 – 10401Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1074 – 10741Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1096 – 10961Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1157 – 11571Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1230 – 12301Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi1287 – 12871Magnesium; catalytic; for integrase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri355 – 37218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri378 – 39518CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
DNA bindingi1393 – 144351Integrase-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

DNA 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

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi3.4.23.B8. 2706.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro-Pol polyprotein
Alternative name(s):
Pr160Gag-Pro-Pol
Cleaved into the following 7 chains:
Matrix protein p19
Short name:
MA
Capsid protein p24
Short name:
CA
Nucleocapsid protein p15-pro
Short name:
NC'
Short name:
NC-pro
Protease (EC:3.4.23.-)
Short name:
PR
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
Gene namesi
Name:gag-pro-pol
OrganismiHuman T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1)
Taxonomic identifieri11926 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeDeltaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007683 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi573 – 5753ILP → TAG: Complete loss of cleavage between protease and p1. 1 Publication
Mutagenesisi581 – 5844VLGL → GAGA: Complete loss of cleavage between p1 and RT. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by hostBy similarity
Chaini2 – 14621461Gag-Pro-Pol polyproteinPRO_0000259828Add
BLAST
Chaini2 – 130129Matrix protein p19By similarityPRO_0000259829Add
BLAST
Chaini131 – 344214Capsid protein p24By similarityPRO_0000259830Add
BLAST
Chaini345 – 449105Nucleocapsid protein p15-proBy similarityPRO_0000259831Add
BLAST
Chaini450 – 574125ProteaseBy similarityPRO_0000259832Add
BLAST
Peptidei575 – 5828p11 PublicationPRO_0000259833
Chaini583 – 1167585Reverse transcriptase/ribonuclease HBy similarityPRO_0000038873Add
BLAST
Chaini1168 – 1462295IntegraseBy similarityPRO_0000038874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei105 – 1051Phosphoserine; by host MAPK1By similarity

Post-translational modificationi

Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini.3 Publications
Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei130 – 1312Cleavage; by viral proteaseBy similarity
Sitei344 – 3452Cleavage; by viral proteaseBy similarity
Sitei449 – 4502Cleavage; by viral proteaseBy similarity
Sitei574 – 5752Cleavage; by viral proteaseBy similarity
Sitei582 – 5832Cleavage; by viral protease
Sitei1167 – 11682Cleavage; by viral protease

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Interacts with human TSG101 and NEDD4. These interactions are essential for budding and release of viral particles (By similarity).By similarity

Structurei

Secondary structure

1
1462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi451 – 4533Combined sources
Beta strandi456 – 4583Combined sources
Beta strandi461 – 4677Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi474 – 4807Combined sources
Beta strandi488 – 4903Combined sources
Helixi491 – 4933Combined sources
Beta strandi500 – 5023Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi510 – 52112Combined sources
Beta strandi523 – 5264Combined sources
Beta strandi534 – 5374Combined sources
Beta strandi540 – 5423Combined sources
Helixi552 – 5576Combined sources
Beta strandi561 – 5633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O0Jmodel-A/B450-564[»]
1TP1model-A/B450-564[»]
2B7FX-ray2.60A/B/C/D/E/F450-565[»]
4YDGX-ray3.25A/B450-565[»]
ProteinModelPortaliP03362.
SMRiP03362. Positions 1-130, 146-344, 450-565.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini476 – 55479Peptidase A2PROSITE-ProRule annotationAdd
BLAST
Domaini614 – 804191Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini1031 – 1165135RNase HPROSITE-ProRule annotationAdd
BLAST
Domaini1219 – 1388170Integrase catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi118 – 1214PPXY motif
Motifi124 – 1274PTAP/PSAP motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi95 – 14450Pro-richAdd
BLAST
Compositional biasi657 – 6604Poly-Ser

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. Matrix protein p19 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4 (By similarity).By similarity
The capsid protein N-terminus seems to be involved in Gag-Gag interactions.By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 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 fingeri355 – 37218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri378 – 39518CCHC-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.185.10. 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.
IPR003139. D_retro_matrix.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR003308. Integrase_Zn-bd_dom_N.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF02228. Gag_p19. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: This strategy of translation probably allows the virus to modulate the quantity of each viral protein.

Isoform Gag-Pro-Pol polyprotein (identifier: P03362-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL
60 70 80 90 100
KIALETPARI CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP
110 120 130 140 150
PPPSSPTHDP PDSDPQIPPP YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL
160 170 180 190 200
QAIKQEVSQA APGSPQFMQT IRLAVQQFDP TAKDLQDLLQ YLCSSLVASL
210 220 230 240 250
HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR REYQQLWLAA
260 270 280 290 300
FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
310 320 330 340 350
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQTWTPKDK TKVLVVQPKK
360 370 380 390 400
PPPNQPCFRC GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI
410 420 430 440 450
PEPEPEEDAL LLDLPADIPH PKNLHRGGGL TSPPTLQQVL PNQDPASILP
460 470 480 490 500
VIPLDPARRP VIKAQVDTQT SHPKTIEALL DTGADMTVLP IALFSSNTPL
510 520 530 540 550
KNTSVLGAGG QTQDHFKLTS LPVLIRLPFR TTPIVLTSCL VDTKNNWAII
560 570 580 590 600
GRDALQQCQG VLYLPEAKRP PVILPIQAPA VLGLEHLPRP PQISQFPLNP
610 620 630 640 650
ERLQALQHLV RKALEAGHIE PYTGPGNNPV FPVKKANGTW RFIHDLRATN
660 670 680 690 700
SLTIDLSSSS PGPPDLSSLP TTLAHLQTID LRDAFFQIPL PKQFQPYFAF
710 720 730 740 750
TVPQQCNYGP GTRYAWKVLP QGFKNSPTLF EMQLAHILQP IRQAFPQCTI
760 770 780 790 800
LQYMDDILLA SPSHEDLLLL SEATMASLIS HGLPVSENKT QQTPGTIKFL
810 820 830 840 850
GQIISPNHLT YDAVPTVPIR SRWALPELQA LLGEIQWVSK GTPTLRQPLH
860 870 880 890 900
SLYCALQRHT DPRDQIYLNP SQVQSLVQLR QALSQNCRSR LVQTLPLLGA
910 920 930 940 950
IMLTLTGTTT VVFQSKEQWP LVWLHAPLPH TSQCPWGQLL ASAVLLLDKY
960 970 980 990 1000
TLQSYGLLCQ TIHHNISTQT FNQFIQTSDH PSVPILLHHS HRFKNLGAQT
1010 1020 1030 1040 1050
GELWNTFLKT AAPLAPVKAL MPVFTLSPVI INTAPCLFSD GSTSRAAYIL
1060 1070 1080 1090 1100
WDKQILSQRS FPLPPPHKSA QRAELLGLLH GLSSARSWRC LNIFLDSKYL
1110 1120 1130 1140 1150
YHYLRTLALG TFQGRSSQAP FQALLPRLLS RKVVYLHHVR SHTNLPDPIS
1160 1170 1180 1190 1200
RLNALTDALL ITPVLQLSPA ELHSFTHCGQ TALTLQGATT TEASNILRSC
1210 1220 1230 1240 1250
HACRGGNPQH QMPRGHIRRG LLPNHIWQGD ITHFKYKNTL YRLHVWVDTF
1260 1270 1280 1290 1300
SGAISATQKR KETSSEAISS LLQAIAHLGK PSYINTDNGP AYISQDFLNM
1310 1320 1330 1340 1350
CTSLAIRHTT HVPYNPTSSG LVERSNGILK TLLYKYFTDK PDLPMDNALS
1360 1370 1380 1390 1400
IALWTINHLN VLTNCHKTRW QLHHSPRLQP IPETRSLSNK QTHWYYFKLP
1410 1420 1430 1440 1450
GLNSRQWKGP QEALQEAAGA ALIPVSASSA QWIPWRLLKR AACPRPVGGP
1460
ADPKEKDLQH HG
Note: Produced by -1 ribosomal frameshifting at the gag-pro and gag-pol genes boundaries.
Length:1,462
Mass (Da):162,512
Last modified:January 23, 2007 - v3
Checksum:iDCC70251EC729E87
GO
Isoform Gag-Pro polyprotein (identifier: P10274-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P10274.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting at the gag-pro genes boundary.
Length:651
Mass (Da):71,558
GO
Isoform Gag polyprotein (identifier: P03345-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P03345.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:429
Mass (Da):47,496
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5473NNW → GSM AA sequence (PubMed:11469799).Curated
Sequence conflicti569 – 5691R → G AA sequence (PubMed:11469799).Curated
Sequence conflicti592 – 5921Q → E AA sequence (PubMed:11469799).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti440 – 4412LP → FL.
Natural varianti569 – 5691R → G.
Natural varianti621 – 6211P → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02029 Genomic DNA. Translation: AAA96673.1. Sequence problems.
M13810 Genomic RNA. Translation: AAA46207.1. Sequence problems.
X14144 Genomic DNA. Translation: CAA32360.1.
PIRiA03961. GNLJGH.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02029 Genomic DNA. Translation: AAA96673.1. Sequence problems.
M13810 Genomic RNA. Translation: AAA46207.1. Sequence problems.
X14144 Genomic DNA. Translation: CAA32360.1.
PIRiA03961. GNLJGH.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O0Jmodel-A/B450-564[»]
1TP1model-A/B450-564[»]
2B7FX-ray2.60A/B/C/D/E/F450-565[»]
4YDGX-ray3.25A/B450-565[»]
ProteinModelPortaliP03362.
SMRiP03362. Positions 1-130, 146-344, 450-565.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.23.B8. 2706.

Miscellaneous databases

EvolutionaryTraceiP03362.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.185.10. 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.
IPR003139. D_retro_matrix.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR003308. Integrase_Zn-bd_dom_N.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF02228. Gag_p19. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Human adult T-cell leukemia virus: complete nucleotide sequence of the provirus genome integrated in leukemia cell DNA."
    Seiki M., Hattori S., Hirayama Y., Yoshida M.C.
    Proc. Natl. Acad. Sci. U.S.A. 80:3618-3622(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of a protease gene of human T-cell leukemia virus type I (HTLV-I) and its structural comparison."
    Nam S.H., Hatanaka M.
    Biochem. Biophys. Res. Commun. 139:129-135(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 395-672.
  3. "Enzymatic amplification of exogenous and endogenous retroviral sequences from DNA of patients with tropical spastic paraparesis."
    Bangham C.R.M., Daenke S., Philips R.E., Cruickshank J.K., Bell J.I.
    EMBO J. 7:4179-4184(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-751.
  4. "Primary structure analysis of the major internal protein p24 of human type C T-cell leukemia virus."
    Oroszlan S., Sarngadharan M.G., Copeland T.D., Kalyanaraman V.S., Gilden R.V., Gallo R.C.
    Proc. Natl. Acad. Sci. U.S.A. 79:1291-1294(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 131-155.
  5. "Proteolytic processing of the human T-cell lymphotropic virus 1 reverse transcriptase: identification of the N-terminal cleavage site by mass spectrometry."
    Agbuya P.G., Sherman N.E., Moen L.K.
    Arch. Biochem. Biophys. 392:93-102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 545-611, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  6. "Characterization of ribosomal frameshifting for expression of pol gene products of human T-cell leukemia virus type I."
    Nam S.H., Copeland T.D., Hatanaka M., Oroszlan S.
    J. Virol. 67:196-203(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 596-612, RIBOSOMAL FRAMESHIFT.
  7. "A novel protease processing site in the transframe protein of human T-cell leukemia virus type 1 PR76(gag-pro) defines the N terminus of RT."
    Heidecker G., Hill S., Lloyd P.A., Derse D.
    J. Virol. 76:13101-13105(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 583-590, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF 573-ILE--PRO-575 AND 581-VAL--LEU-584.
  8. "Processing of gag precursor polyprotein of human T-cell leukemia virus type I by virus-encoded protease."
    Nam S.H., Kidokoro M., Shida H., Hatanaka M.
    J. Virol. 62:3718-3728(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF PROTEASE.
  9. "Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase."
    Louis J.M., Oroszlan S., Toezser J.
    J. Biol. Chem. 274:6660-6666(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PROTEASE.
  10. "The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation."
    Rayne F., Bouamr F., Lalanne J., Mamoun R.Z.
    J. Virol. 75:5277-5287(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CAPSID PROTEIN P24.
  11. "Identification of the RT-RH/IN cleavage site of HTLV-I."
    Mariani V.L., Shuker S.B.
    Biochem. Biophys. Res. Commun. 300:268-270(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  12. "Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell Leukemia virus type 1 protease."
    Kadas J., Weber I.T., Bagossi P., Miklossy G., Boross P., Oroszlan S., Toezser J.
    J. Biol. Chem. 279:27148-27157(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PROTEASE.

Entry informationi

Entry nameiPOL_HTL1A
AccessioniPrimary (citable) accession number: P03362
Secondary accession number(s): Q85590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching 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).By similarity
HTLV-1 lineages are divided in four clades, A (Cosmopolitan), B (Central African group), C (Melanesian group) and D (New Central African group).

Keywords - Technical termi

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

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

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 one 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.