SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11227

- POL_MLVRD

UniProt

P11227 - POL_MLVRD

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pol polyprotein

Gene
pol
Organism
Radiation murine leukemia virus
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei27 – 271 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. RNA binding Source: InterPro
  3. RNA-directed DNA polymerase activity Source: UniProtKB-KW
  4. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA integration Source: UniProtKB-KW
  2. DNA recombination Source: UniProtKB-KW
  3. establishment of integrated proviral latency Source: UniProtKB-KW
  4. viral entry into host cell Source: UniProtKB-KW
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, Viral genome integration, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Pol polyprotein
Cleaved into the following 3 chains:
Gene namesi
Name:pol
OrganismiRadiation murine leukemia virus
Taxonomic identifieri11787 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000007778: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 1196IntegrasePRO_0000259741
Chaini1 – 11961196Pol polyproteinPRO_0000259739Add
BLAST
Chaini1 – 103103ProteasePRO_0000026134Add
BLAST
Chaini104 – ?Reverse transcriptase/ribonuclease HPRO_0000259740

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.

Structurei

3D structure databases

ProteinModelPortaliP11227.
SMRiP11227. Positions 144-594, 623-788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 9271Peptidase A2Add
BLAST
Domaini202 – 393192Reverse transcriptaseAdd
BLAST
Domaini635 – 781147RNase HAdd
BLAST
Domaini905 – 1063159Integrase catalyticAdd
BLAST

Sequence similaritiesi

Contains 1 RNase H domain.

Family and domain databases

Gene3Di2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR001584. Integrase_cat-core.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
PROSITEiPS50175. 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]

Sequencei

Sequence statusi: Complete.

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

P11227-1 [UniParc]FASTAAdd to Basket

« Hide

GGQGQEPPPE PRITLKVGGQ PVTFLVDTGA QHSVLTQNPG PLSDRSAWVQ     50
GATGGKRYRW TTDRKVHLAT GKVTHSFLHV PDCPYPLLGR DLLTKLKAQI 100
HFKGSGAQIV GPMGQPLQVL TLNIEDEYRL HEISTEPDVS PGSTWLSDFP 150
QAWAETGGMG LAVRQAPLII PLKATSTPVS IKQYPMSQEA KLGIKPHIQR 200
LLDQGILVPC QSPWNTPLLP VKKPGTNDYR PVQGLREVNK RVEDIHPTVP 250
NPYNLLSGLP TSHRWYTVLD LKDAFFCLRL HPTSQPLFAS EWRDPGMGIS 300
GQLTWTRLPQ GFKNSPTLFD EALHRGLADF RIQHPDLILL QYVDDLLLAA 350
TSELDCQQGT RALLKTLGNL GYRASAKKAQ ICQKQVKYLG YLLREGQRWL 400
TEARKETVMG QPTPKTPRQL REFLGTAGFC RLWIPRFAEM AAPLYPLTKT 450
GTLFNWGPDQ QKAYHEIKQA LLTAPALGLP DLTKPFELFV DEKQGYAKGV 500
LTQKLGPWRR PVAYLSKKLD PVAAGWPPCL RMVAAIAVLT KDAGKLTMGQ 550
PLVILAPHAV EALVKQPPDR WLSNARMTHY QAMLLDTDRV QFGPVVALNP 600
ATLLPLPEEG APHDCLEILA ETHGTEPDLT DQPIPDADHT WYTDGSSFLQ 650
EGQRKAGAAV TTETEVIWAR ALPAGTSAQR AELIALTQAL KMAEGKRLNV 700
YTDSRYAFAT AHIHGEIYKR RGLLTSEGRE IKNKSEILAL LKALFLPKRL 750
SIIHCLGHQK GDSAEARGNR LADQAAREAA IKTPPDTSTL LIEDSTPYTP 800
AYFHYTETDL KKLRELGATY NQSKGYWVFQ GKPVMPDQFV FELLDSLHRL 850
THLGYQKMKA LLDRGESPYY MLNRDKTLQY VADSCTVCAQ VNASKAKIGA 900
GVRVRGHRPG THWEIDFTEV KPGLYGYKYL LVFVDTFSGW VEAFPTKHET 950
AKIVTKKLLE EIFPRFGMPQ VLGTDNGPAF VSQVSQSVAK LLGIDWKLHC 1000
AYRPQSSGQV ERMNRTIKET LTKLTLATGT RDWVLLLPLA LYRARNTPGP 1050
HGLTPYEILY GAPPPLVNFH DPEMSKFTNS PSLQAHLQAL QAVQREVWKP 1100
LAAAYQDQLD QPVIPHPFRV GDTVWVRRHQ TKNLEPRWKG PYTVLLTTPT 1150
ALKVDGISAW IHAAHVKAAT TPPIRPSWRV QRSQNPLKIR LTRGAP 1196
Length:1,196
Mass (Da):133,323
Last modified:July 1, 1989 - v1
Checksum:i9549253FCEEB5306
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03363 Genomic RNA. No translation available.
PIRiB26183. GNMVRV.

Keywords - Coding sequence diversityi

RNA suppression of termination

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03363 Genomic RNA. No translation available.
PIRi B26183. GNMVRV.

3D structure databases

ProteinModelPortali P11227.
SMRi P11227. Positions 144-594, 623-788.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
InterProi IPR001969. Aspartic_peptidase_AS.
IPR001584. Integrase_cat-core.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
[Graphical view ]
Pfami PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view ]
SUPFAMi SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of a radiation leukemia virus genome."
    Merregaert J., Janowski M., Reddy E.P.
    Virology 158:88-102(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOL_MLVRD
AccessioniPrimary (citable) accession number: P11227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is synthesized as a Gag-Pol polyprotein.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi