Reviewed, UniProtKB/Swiss-Prot P03355 (POL_MLVMO)

Names and origin

Protein names

Recommended name:
    Pol polyprotein
Cleaved into the following 3 chains:
    1- Recommended name:
            Protease
              EC=3.4.23.-
    2- Recommended name:
            Reverse transcriptase/ribonuclease H
                Short name=RT
              EC=2.7.7.49
              EC=3.1.26.4
    3- Recommended name:
            Integrase
                Short name=IN

Gene names

Name:

pol

Organism

Moloney murine leukemia virus (MoMLV)

Taxonomic identifier

11801 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus

Virus host

Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	1199 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	During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.
Catalytic activity	Endonucleolytic cleavage to 5'-phosphomonoester. Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins.
Miscellaneous	This protein is synthesized as a Gag-Pol polyprotein.
Sequence similarities	Belongs to the retroviral Pol polyprotein family. Contains 1 integrase catalytic domain. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.

Ontologies

Keywords
Biological process	DNA integration DNA recombination
Molecular function	Aspartyl protease Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	DNA integration Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro transposition Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1199

1199

Pol polyprotein

PRO_0000259734

Chain

1 – 103

103

Protease

PRO_0000026133

Chain

104 – ?

Reverse transcriptase/ribonuclease H

PRO_0000259735

Chain

? – 1199

Integrase

PRO_0000259736

Regions

Domain

22 – 92

71

Peptidase A2

Domain

202 – 393

192

Reverse transcriptase

Domain

635 – 781

147

RNase H

Domain

905 – 1063

159

Integrase catalytic

Sites

Active site

27

1

By similarity

Secondary structure

1

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1199

Helix Strand Turn

Details...

Helix

145 – 148

4

Turn

150 – 152

3

Helix

154 – 157

4

Helix

188 – 203

16

Beta strand

206 – 210

5

Beta strand

218 – 220

3

Beta strand

223 – 227

5

Beta strand

231 – 233

3

Helix

236 – 239

4

Helix

252 – 256

5

Beta strand

265 – 271

7

Turn

272 – 274

3

Helix

275 – 277

3

Beta strand

278 – 280

3

Turn

282 – 284

3

Helix

285 – 288

4

Beta strand

295 – 298

4

Beta strand

301 – 307

7

Helix

315 – 333

19

Beta strand

338 – 342

5

Beta strand

345 – 353

9

Helix

354 – 370

17

Turn

376 – 378

3

Beta strand

380 – 388

9

Beta strand

391 – 394

4

Turn

413 – 415

3

Helix

416 – 422

7

Turn

423 – 427

5

Helix

438 – 440

3

Beta strand

461 – 463

3

Helix

466 – 470

5

Beta strand

480 – 482

3

Beta strand

489 – 494

6

Beta strand

496 – 501

6

Turn

506 – 509

4

Beta strand

524 – 526

3

Helix

531 – 544

14

Helix

545 – 547

3

Beta strand

552 – 555

4

Turn

560 – 563

4

Beta strand

564 – 566

3

Turn

567 – 571

5

Beta strand

589 – 592

4

Beta strand

630 – 632

3

Beta strand

638 – 650

13

Beta strand

653 – 661

9

Beta strand

666 – 672

7

Helix

678 – 692

15

Turn

693 – 695

3

Beta strand

696 – 702

7

Helix

705 – 710

6

Helix

734 – 743

10

Beta strand

746 – 754

9

Helix

764 – 782

19

Sequences

	Sequence		Length	Mass (Da)
	P03355-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: CC6139FC47C3D253	FASTA	1,199	133,943
	10 20 30 40 50 60 GGQGQEPPPE PRITLKVGGQ PVTFLVDTGA QHSVLTQNPG PLSDKSAWVQ GATGGKRYRW 70 80 90 100 110 120 TTDRKVHLAT GKVTHSFLHV PDCPYPLLGR DLLTKLKAQI HFEGSGAQVM GPMGQPLQVL 130 140 150 160 170 180 TLNIEDEHRL HETSKEPDVS LGSTWLSDFP QAWAETGGMG LAVRQAPLII PLKATSTPVS 190 200 210 220 230 240 IKQYPMSQEA RLGIKPHIQR LLDQGILVPC QSPWNTPLLP VKKPGTNDYR PVQDLREVNK 250 260 270 280 290 300 RVEDIHPTVP NPYNLLSGLP PSHQWYTVLD LKDAFFCLRL HPTSQPLFAF EWRDPEMGIS 310 320 330 340 350 360 GQLTWTRLPQ GFKNSPTLFD EALHRDLADF RIQHPDLILL QYVDDLLLAA TSELDCQQGT 370 380 390 400 410 420 RALLQTLGNL GYRASAKKAQ ICQKQVKYLG YLLKEGQRWL TEARKETVMG QPTPKTPRQL 430 440 450 460 470 480 REFLGTAGFC RLWIPGFAEM AAPLYPLTKT GTLFNWGPDQ QKAYQEIKQA LLTAPALGLP 490 500 510 520 530 540 DLTKPFELFV DEKQGYAKGV LTQKLGPWRR PVAYLSKKLD PVAAGWPPCL RMVAAIAVLT 550 560 570 580 590 600 KDAGKLTMGQ PLVILAPHAV EALVKQPPDR WLSNARMTHY QALLLDTDRV QFGPVVALNP 610 620 630 640 650 660 ATLLPLPEEG LQHNCLDILA EAHGTRPDLT DQPLPDADHT WYTDGSSLLQ EGQRKAGAAV 670 680 690 700 710 720 TTETEVIWAK ALPAGTSAQR AELIALTQAL KMAEGKKLNV YTDSRYAFAT AHIHGEIYRR 730 740 750 760 770 780 RGLLTSEGKE IKNKDEILAL LKALFLPKRL SIIHCPGHQK GHSAEARGNR MADQAARKAA 790 800 810 820 830 840 ITETPDTSTL LIENSSPYTS EHFHYTVTDI KDLTKLGAIY DKTKKYWVYQ GKPVMPDQFT 850 860 870 880 890 900 FELLDFLHQL THLSFSKMKA LLERSHSPYY MLNRDRTLKN ITETCKACAQ VNASKSAVKQ 910 920 930 940 950 960 GTRVRGHRPG THWEIDFTEI KPGLYGYKYL LVFIDTFSGW IEAFPTKKET AKVVTKKLLE 970 980 990 1000 1010 1020 EIFPRFGMPQ VLGTDNGPAF VSKVSQTVAD LLGIDWKLHC AYRPQSSGQV ERMNRTIKET 1030 1040 1050 1060 1070 1080 LTKLTLATGS RDWVLLLPLA LYRARNTPGP HGLTPYEILY GAPPPLVNFP DPDMTRVTNS 1090 1100 1110 1120 1130 1140 PSLQAHLQAL YLVQHEVWRP LAAAYQEQLD RPVVPHPYRV GDTVWVRRHQ TKNLEPRWKG 1150 1160 1170 1180 1190 PYTVLLTTPT ALKVDGIAAW IHAAHVKAAD PGGGPSSRLT WRVQRSQNPL KIRLTREAP

References

[1]	"Nucleotide sequence of Moloney murine leukaemia virus." Shinnick T.M., Lerner R.A., Sutcliffe J.G. Nature 293:543-548(1981) [PubMed: 6169994] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE PMLV-1).
[2]	"Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase." Georgiadis M.M., Jessen S.M., Ogata C.M., Telesnitsky A., Goff S.P., Hendrickson W.A. Structure 3:879-892(1995) [PubMed: 8535782] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 130-394.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02255 Genomic RNA. No translation available.

PIR

GNMV1M. A03956.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0E	X-ray	3.00	A/B	144-398	[»]
1D1U	X-ray	2.30	A	144-398	[»]
1I6J	X-ray	2.00	A	144-398	[»]
1MML	X-ray	1.80	A	130-394	[»]
1N4L	X-ray	2.00	A	144-398	[»]
1NND	X-ray	2.30	A	144-398	[»]
1QAI	X-ray	2.30	A/B	130-394	[»]
1QAJ	X-ray	2.30	A/B	144-398	[»]
1RW3	X-ray	3.00	A	144-594	[»]
1ZTT	X-ray	1.85	A	144-398	[»]
1ZTW	X-ray	1.80	A	144-398	[»]
2FJV	X-ray	2.05	A	144-398	[»]
2FJW	X-ray	1.95	A	144-398	[»]
2FJX	X-ray	1.80	A	144-398	[»]
2FVP	X-ray	2.25	A	144-398	[»]
2FVQ	X-ray	2.30	A	144-398	[»]
2FVR	X-ray	2.20	A	144-398	[»]
2FVS	X-ray	2.35	A	144-398	[»]
2HB5	X-ray	1.59	A	618-791	[»]
2R2R	X-ray	2.10	A	144-398	[»]
2R2S	X-ray	2.80	A	144-398	[»]
2R2T	X-ray	2.00	A	144-398	[»]
2R2U	X-ray	2.30	A	144-398	[»]

ModBase

Search...

Protein family/group databases

MEROPS

A02.008.

PTM databases

PhosphoSite

P03355.

Enzyme and pathway databases

BRENDA

2.7.7.49. 273894.
3.1.26.4. 273894.

Family and domain databases

InterPro

IPR000477. DNA_pol_RVTase.
IPR001584. Integrase_cat-core.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR002156. RNase_H.
[Graphical view]

Gene3D

G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.

Pfam

PF00075. RnaseH. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]

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.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

POL_MLVMO

Accession

Primary (citable) accession number: P03355

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)