P03362 (POL_HTL1A) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gag-Pro-Pol polyprotein

Alternative name(s):
Pr160Gag-Pro-Pol

Cleaved into the following 7 chains:

1. Matrix protein p19
   Short name=MA
2. Capsid protein p24
   Short name=CA
3. Nucleocapsid protein p15-pro
   Short name=NC'
   Short name=NC-pro
4. Protease
   Short name=PR
   EC=3.4.23.-
5. p1
6. Reverse transcriptase/ribonuclease H
   Short name=RT
   EC=2.7.7.49
   EC=2.7.7.7
   EC=3.1.26.4
7. Integrase
   Short name=IN

Gene names

Name:

gag-pro-pol

Organism

Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) [Complete proteome]

Taxonomic identifier

11926 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Deltaretrovirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	1462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex By similarity. Ref.8 Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome By similarity. Ref.8 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 By similarity. Ref.8 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. Ref.8 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. Ref.8
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity. Binds 2 magnesium ions for ribonuclease H (RNase H) activity By similarity.
Subunit structure	Interacts with human TSG101 and NEDD4. These interactions are essential for budding and release of viral particles By similarity.
Subcellular location	Matrix protein p19: Virion Potential. Capsid protein p24: Virion Potential. Nucleocapsid protein p15-pro: Virion Potential.
Domain	Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. 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. The capsid protein N-terminus seems to be involved in Gag-Gag interactions By similarity.
Post-translational modification	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. Ref.5 Ref.7 Ref.11 Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding By similarity.
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. HTLV-1 lineages are divided in four clades, A (Cosmopolitan), B (Central African group), C (Melanesian group) and D (New Central African group).
Sequence similarities	Contains 2 CCHC-type zinc fingers. Contains 1 integrase catalytic domain. Contains 1 integrase-type DNA-binding domain. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.

Ontologies

Keywords
Biological process	DNA integration DNA recombination Host-virus interaction Initiation of viral infection Viral genome integration
Cellular component	Virion
Coding sequence diversity	Ribosomal frameshifting
Domain	Repeat Zinc-finger
Ligand	DNA-binding Magnesium Metal-binding Viral nucleoprotein Zinc
Molecular function	Aspartyl protease Capsid protein Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Inferred from electronic annotation. Source: InterPro
Cellular component	viral nucleocapsid Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: EC RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by ribosomal frameshifting. [Align] [Select]

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)

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.

Note: Produced by -1 ribosomal frameshifting at the gag-pro and gag-pol genes boundaries.

Isoform Gag-Pro polyprotein (identifier: P10274-1)

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.

Isoform Gag polyprotein (identifier: P03345-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 1462

1461

Gag-Pro-Pol polyprotein

PRO_0000259828

Chain

2 – 130

129

Matrix protein p19 By similarity

PRO_0000259829

Chain

131 – 344

214

Capsid protein p24 By similarity

PRO_0000259830

Chain

345 – 449

105

Nucleocapsid protein p15-pro By similarity

PRO_0000259831

Chain

450 – 574

125

Protease By similarity

PRO_0000259832

Peptide

575 – 582

8

p1

PRO_0000259833

Chain

583 – 1167

585

Reverse transcriptase/ribonuclease H By similarity

PRO_0000038873

Chain

1168 – 1462

295

Integrase By similarity

PRO_0000038874

Regions

Domain

476 – 554

79

Peptidase A2

Domain

614 – 804

191

Reverse transcriptase

Domain

1031 – 1165

135

RNase H

Domain

1219 – 1388

170

Integrase catalytic

Zinc finger

355 – 372

18

CCHC-type 1

Zinc finger

378 – 395

18

CCHC-type 2

DNA binding

1393 – 1443

51

Integrase-type By similarity

Motif

118 – 121

4

PPXY motif

Motif

124 – 127

4

PTAP/PSAP motif

Compositional bias

95 – 144

50

Pro-rich

Compositional bias

657 – 660

4

Poly-Ser

Sites

Active site

481

1

For protease activity; shared with dimeric partner By similarity

Metal binding

680

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

755

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

756

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

1040

1

Magnesium; catalytic; for RNase H activity By similarity

Metal binding

1074

1

Magnesium; catalytic; for RNase H activity By similarity

Metal binding

1096

1

Magnesium; catalytic; for RNase H activity By similarity

Metal binding

1157

1

Magnesium; catalytic; for RNase H activity By similarity

Metal binding

1230

1

Magnesium; catalytic; for integrase activity By similarity

Metal binding

1287

1

Magnesium; catalytic; for integrase activity By similarity

Site

130 – 131

2

Cleavage; by viral protease By similarity

Site

344 – 345

2

Cleavage; by viral protease By similarity

Site

449 – 450

2

Cleavage; by viral protease By similarity

Site

574 – 575

2

Cleavage; by viral protease By similarity

Site

582 – 583

2

Cleavage; by viral protease

Site

1167 – 1168

2

Cleavage; by viral protease

Amino acid modifications

Modified residue

105

1

Phosphoserine; by host MAPK1 By similarity

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Natural variations

Natural variant

440 – 441

2

LP → FL

Natural variant

569

1

R → G

Natural variant

621

1

P → S

Experimental info

Mutagenesis

573 – 575

3

ILP → TAG: Complete loss of cleavage between protease and p1. Ref.7

Mutagenesis

581 – 584

4

VLGL → GAGA: Complete loss of cleavage between p1 and RT. Ref.7

Sequence conflict

545 – 547

3

NNW → GSM AA sequence Ref.5

Sequence conflict

569

1

R → G AA sequence Ref.5

Sequence conflict

592

1

Q → E AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1462

Helix Strand Turn

Details...

Helix

147 – 159

13

Helix

167 – 175

9

Turn

176 – 178

3

Helix

182 – 192

11

Helix

195 – 214

20

Helix

228 – 231

4

Helix

240 – 252

13

Helix

263 – 265

3

Helix

274 – 286

13

Helix

296 – 303

8

Turn

304 – 306

3

Helix

309 – 317

9

Helix

328 – 332

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gag-Pro-Pol polyprotein [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DCC70251EC729E87	FASTA	1,462	162,512
	10 20 30 40 50 60 MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL KIALETPARI 70 80 90 100 110 120 CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP PPPSSPTHDP PDSDPQIPPP 130 140 150 160 170 180 YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP 190 200 210 220 230 240 TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR 250 260 270 280 290 300 REYQQLWLAA FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR 310 320 330 340 350 360 SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQTWTPKDK TKVLVVQPKK PPPNQPCFRC 370 380 390 400 410 420 GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI PEPEPEEDAL LLDLPADIPH 430 440 450 460 470 480 PKNLHRGGGL TSPPTLQQVL PNQDPASILP VIPLDPARRP VIKAQVDTQT SHPKTIEALL 490 500 510 520 530 540 DTGADMTVLP IALFSSNTPL KNTSVLGAGG QTQDHFKLTS LPVLIRLPFR TTPIVLTSCL 550 560 570 580 590 600 VDTKNNWAII GRDALQQCQG VLYLPEAKRP PVILPIQAPA VLGLEHLPRP PQISQFPLNP 610 620 630 640 650 660 ERLQALQHLV RKALEAGHIE PYTGPGNNPV FPVKKANGTW RFIHDLRATN SLTIDLSSSS 670 680 690 700 710 720 PGPPDLSSLP TTLAHLQTID LRDAFFQIPL PKQFQPYFAF TVPQQCNYGP GTRYAWKVLP 730 740 750 760 770 780 QGFKNSPTLF EMQLAHILQP IRQAFPQCTI LQYMDDILLA SPSHEDLLLL SEATMASLIS 790 800 810 820 830 840 HGLPVSENKT QQTPGTIKFL GQIISPNHLT YDAVPTVPIR SRWALPELQA LLGEIQWVSK 850 860 870 880 890 900 GTPTLRQPLH SLYCALQRHT DPRDQIYLNP SQVQSLVQLR QALSQNCRSR LVQTLPLLGA 910 920 930 940 950 960 IMLTLTGTTT VVFQSKEQWP LVWLHAPLPH TSQCPWGQLL ASAVLLLDKY TLQSYGLLCQ 970 980 990 1000 1010 1020 TIHHNISTQT FNQFIQTSDH PSVPILLHHS HRFKNLGAQT GELWNTFLKT AAPLAPVKAL 1030 1040 1050 1060 1070 1080 MPVFTLSPVI INTAPCLFSD GSTSRAAYIL WDKQILSQRS FPLPPPHKSA QRAELLGLLH 1090 1100 1110 1120 1130 1140 GLSSARSWRC LNIFLDSKYL YHYLRTLALG TFQGRSSQAP FQALLPRLLS RKVVYLHHVR 1150 1160 1170 1180 1190 1200 SHTNLPDPIS RLNALTDALL ITPVLQLSPA ELHSFTHCGQ TALTLQGATT TEASNILRSC 1210 1220 1230 1240 1250 1260 HACRGGNPQH QMPRGHIRRG LLPNHIWQGD ITHFKYKNTL YRLHVWVDTF SGAISATQKR 1270 1280 1290 1300 1310 1320 KETSSEAISS LLQAIAHLGK PSYINTDNGP AYISQDFLNM CTSLAIRHTT HVPYNPTSSG 1330 1340 1350 1360 1370 1380 LVERSNGILK TLLYKYFTDK PDLPMDNALS IALWTINHLN VLTNCHKTRW QLHHSPRLQP 1390 1400 1410 1420 1430 1440 IPETRSLSNK QTHWYYFKLP GLNSRQWKGP QEALQEAAGA ALIPVSASSA QWIPWRLLKR 1450 1460 AACPRPVGGP ADPKEKDLQH HG
	Isoform Gag-Pro polyprotein [UniParc]. See P10274.		–	–
	Isoform Gag polyprotein [UniParc]. See P03345.		–	–

References

[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: 6304725] [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: 3021121] [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: 2468487] [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: 6280175] [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: 11469799] [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: 8416368] [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: 12438640] [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: 2843670] [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: 10037763] [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: 11333909] [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: 12504078] [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: 15102858] [Abstract] Cited for: CHARACTERIZATION OF PROTEASE.
[13]	"Sequence-specific 1H, 13C and 15N chemical shift assignment and secondary structure of the HTLV-I capsid protein." Khorasanizadeh S., Campos-Olivas R., Clark C.A., Summers M.F. J. Biomol. NMR 14:199-200(1999) [PubMed: 10427751] [Abstract] Cited for: STRUCTURE BY NMR OF 146-344.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02029 Genomic DNA. Translation: AAA96673.1. Sequence problems.
M13810 Genomic RNA. Translation: AAA46207.1. Sequence problems.
X14144 Genomic DNA. Translation: CAA32360.1.

PIR

GNLJGH. A03961.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O0J	model	-	A/B	450-564	[»]
1QRJ	NMR	-	B	146-344	[»]
1TP1	model	-	A/B	450-564	[»]
2B7F	X-ray	2.60	A/B/C/D/E/F	450-565	[»]

ProteinModelPortal

P03362.

SMR

P03362. Positions 1-130, 146-344, 450-565.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR003139. D_retro_matrix_N.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR003308. Integrase_Zn-bd_dom_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RVT.
IPR013084. Znf_CCH_retrovir.
IPR001878. Znf_CCHC.
[Graphical view]

Gene3D

G3DSA:1.10.185.10. D_retro_matrix_N. 1 hit.
G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
G3DSA:1.10.1200.30. Retrov_capsid_C. 1 hit.
G3DSA:1.10.375.10. Retrov_capsid_N. 1 hit.
G3DSA:4.10.60.10. Znf_CCH_retrovir. 1 hit.

Pfam

PF02228. 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]

SMART

SM00343. ZnF_C2HC. 2 hits.
[Graphical view]

SUPFAM

SSF50122. Integrase_C. 1 hit.
SSF50630. Pept_Aspartic. 1 hit.
SSF47353. Retrov_capsid_C. 1 hit.
SSF47943. Retrov_capsid_N. 1 hit.
SSF47836. Retrovir_matrix. 1 hit.
SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50175. 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.
PS50876. ZF_INTEGRASE. False negative.
[Graphical view]

ProtoNet

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Entry information

Entry name

POL_HTL1A

Accession

Primary (citable) accession number: P03362
Secondary accession number(s): Q85590

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program