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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Human T-cell leukemia virus 2 (HTLV-2)
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.1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei478For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi678Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi753Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi754Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi1038Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1073Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1095Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1156Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1229Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1286Magnesium; catalytic; for integrase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri361 – 378CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri384 – 401CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
DNA bindingi1392 – 1441Integrase-typePROSITE-ProRule annotationAdd BLAST50

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

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.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
Gene namesi
Name:gag-pro-pol
OrganismiHuman T-cell leukemia virus 2 (HTLV-2)
Taxonomic identifieri11909 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeDeltaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009254 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00000854722 – 1461Gag-Pro-Pol polyproteinAdd BLAST1460
ChainiPRO_00002599462 – 136Matrix protein p19By similarityAdd BLAST135
ChainiPRO_0000259947137 – 350Capsid protein p24By similarityAdd BLAST214
ChainiPRO_0000259948351 – 446Nucleocapsid protein p15-proBy similarityAdd BLAST96
ChainiPRO_0000261318447 – 571ProteaseBy similarityAdd BLAST125
PeptideiPRO_0000259949572 – 579p1By similarity8
ChainiPRO_0000259950580 – 1166Reverse transcriptase/ribonuclease HBy similarityAdd BLAST587
ChainiPRO_00002599511167 – 1461IntegraseBy similarityAdd BLAST295

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1

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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei136 – 137Cleavage; by viral proteaseBy similarity2
Sitei350 – 351Cleavage; by viral proteaseBy similarity2
Sitei446 – 447Cleavage; by viral proteaseBy similarity2
Sitei571 – 572Cleavage; by viral proteaseBy similarity2
Sitei579 – 580Cleavage; by viral proteaseBy similarity2
Sitei1166 – 1167Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PRIDEiP03363.

Interactioni

Subunit structurei

Interacts with human TSG101. This interaction is essential for budding and release of viral particles (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MEIS2O147703EBI-9676133,EBI-2804934From a different organism.

Protein-protein interaction databases

IntActiP03363. 8 interactors.

Structurei

Secondary structure

11461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi21 – 33Combined sources13
Turni40 – 42Combined sources3
Helixi43 – 54Combined sources12
Turni60 – 63Combined sources4
Turni65 – 67Combined sources3
Helixi68 – 71Combined sources4
Helixi80 – 88Combined sources9
Turni89 – 91Combined sources3
Beta strandi99 – 103Combined sources5
Beta strandi117 – 119Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JVRNMR-A1-136[»]
ProteinModelPortaliP03363.
SMRiP03363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini473 – 551Peptidase A2PROSITE-ProRule annotationAdd BLAST79
Domaini612 – 802Reverse transcriptasePROSITE-ProRule annotationAdd BLAST191
Domaini1029 – 1164RNase HPROSITE-ProRule annotationAdd BLAST136
Domaini1218 – 1387Integrase catalyticPROSITE-ProRule annotationAdd BLAST170

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi94 – 97PTAP/PSAP motif4
Motifi124 – 127PPXY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi94 – 150Pro-richAdd BLAST57
Compositional biasi453 – 456Poly-Gln4
Compositional biasi585 – 588Poly-Pro4

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 (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)DescriptionActionsGraphical viewLength
Zinc fingeri361 – 378CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri384 – 401CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

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.
IPR010661. RVT_thumb.
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.
PF06817. RVT_thumb. 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-Pol polyprotein (identifier: P03363-1) [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
MGQIHGLSPT PIPKAPRGLS THHWLNFLQA AYRLQPRPSD FDFQQLRRFL
60 70 80 90 100
KLALKTPIWL NPIDYSLLAS LIPKGYPGRV VEIINILVKN QVSPSAPAAP
110 120 130 140 150
VPTPICPTTT PPPPPPPSPE AHVPPPYVEP TTTQCFPILH PPGAPSAHRP
160 170 180 190 200
WQMKDLQAIK QEVSSSALGS PQFMQTLRLA VQQFDPTAKD LQDLLQYLCS
210 220 230 240 250
SLVVSLHHQQ LNTLITEAET RGMTGYNPMA GPLRMQANNP AQQGLRREYQ
260 270 280 290 300
NLWLAAFSTL PGNTRDPSWA AILQGLEEPY CAFVERLNVA LDNGLPEGTP
310 320 330 340 350
KEPILRSLAY SNANKECQKI LQARGHTNSP LGEMLRTCQA WTPKDKTKVL
360 370 380 390 400
VVQPRRPPPT QPCFRCGKVG HWSRDCTQPR PPPGPCPLCQ DPSHWKRDCP
410 420 430 440 450
QLKPPQEEGE PLLLDLPSTS GTTEEKNLLK GGDLISPHPD QDISILPLIP
460 470 480 490 500
LRQQQQPILG VRISVMGQTP QPTQALLDTG ADLTVIPQTL VPGPVKLHDT
510 520 530 540 550
LILGASGQTN TQFKLLQTPL HIFLPFRRSP VILSSCLLDT HNKWTIIGRD
560 570 580 590 600
ALQQCQGLLY LPDDPSPHQL LPIATPNTIG LEHLPPPPQV DQFPLNLPER
610 620 630 640 650
LQALNDLVSK ALEAGHIEPY SGPGNNPVFP VKKPNGKWRF IHDLRATNAI
660 670 680 690 700
TTTLTSPSPG PPDLTSLPTA LPHLQTIDLT DAFFQIPLPK QYQPYFAFTI
710 720 730 740 750
PQPCNYGPGT RYAWTVLPQG FKNSPTLFEQ QLAAVLNPMR KMFPTSTIVQ
760 770 780 790 800
YMDDILLASP TNEELQQLSQ LTLQALTTHG LPISQEKTQQ TPGQIRFLGQ
810 820 830 840 850
VISPNHITYE STPTIPIKSQ WTLTELQVIL GEIQWVSKGT PILRKHLQSL
860 870 880 890 900
YSALHGYRDP RACITLTPQQ LHALHAIQQA LQHNCRGRLN PALPLLGLIS
910 920 930 940 950
LSTSGTTSVI FQPKQNWPLA WLHTPHPPTS LCPWGHLLAC TILTLDKYTL
960 970 980 990 1000
QHYGQLCQSF HHNMSKQALC DFLRNSPHPS VGILIHHMGR FHNLGSQPSG
1010 1020 1030 1040 1050
PWKTLLHLPT LLQEPRLLRP IFTLSPVVLD TAPCLFSDGS PQKAAYVLWD
1060 1070 1080 1090 1100
QTILQQDITP LPSHETHSAQ KGELLALICG LRAAKPWPSL NIFLDSKYLI
1110 1120 1130 1140 1150
KYLHSLAIGA FLGTSAHQTL QAALPPLLQG KTIYLHHVRS HTNLPDPIST
1160 1170 1180 1190 1200
FNEYTDSLIL APLVPLTPQG LHGLTHCNQR ALVSFGATPR EAKSLVQTCH
1210 1220 1230 1240 1250
TCQTINSQHH MPRGYIRRGL LPNHIWQGDV THYKYKKYKY CLHVWVDTFS
1260 1270 1280 1290 1300
GAVSVSCKKK ETSCETISAV LQAISLLGKP LHINTDNGPA FLSQEFQEFC
1310 1320 1330 1340 1350
TSYRIKHSTH IPYNPTSSGL VERTNGVIKN LLNKYLLDCP NLPLDNAIHK
1360 1370 1380 1390 1400
ALWTLNQLNV MNPSGKTRWQ IHHSPPLPPI PEASTPPKPP PKWFYYKLPG
1410 1420 1430 1440 1450
LTNQRWKGPL QSLQEAAGAA LLSIDGSPRW IPWRFLKKAA CPRPDASELA
1460
EHAATDHQHH G
Note: Produced by -1 ribosomal frameshifting at the gag-pol genes boundary.
Length:1,461
Mass (Da):162,402
Last modified:January 23, 2007 - v4
Checksum:i2D2911076BDD1002
GO
Isoform Gag-Pro polyprotein (identifier: P03353-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P03353.
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:602
Mass (Da):66,435
GO
Isoform Gag polyprotein (identifier: P03346-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P03346.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:433
Mass (Da):48,028
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10060 Genomic DNA. Translation: AAB59885.1. Sequence problems.
PIRiA03962. GNLJH2.
RefSeqiNP_041003.2. NC_001488.1.

Genome annotation databases

GeneIDi1491941.
KEGGivg:1491943.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10060 Genomic DNA. Translation: AAB59885.1. Sequence problems.
PIRiA03962. GNLJH2.
RefSeqiNP_041003.2. NC_001488.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JVRNMR-A1-136[»]
ProteinModelPortaliP03363.
SMRiP03363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03363. 8 interactors.

Proteomic databases

PRIDEiP03363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1491941.
KEGGivg:1491943.

Miscellaneous databases

EvolutionaryTraceiP03363.

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.
IPR010661. RVT_thumb.
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.
PF06817. RVT_thumb. 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...

Entry informationi

Entry nameiPOL_HTLV2
AccessioniPrimary (citable) accession number: P03363
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 131 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Complete proteome, 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

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.