Skip Header

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

Reverse transcriptase/RNaseH

Gene

pol

Organism
Human immunodeficiency virus 1
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi443 – 4431ManganeseCombined sources
Metal bindingi478 – 4781ManganeseCombined sources
Metal bindingi498 – 4981ManganeseCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, RNA-directed DNA polymeraseSAAS annotationImported, Transferase

Keywords - Ligandi

ManganeseCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Reverse transcriptase/RNaseHImported
Gene namesi
Name:polImported
OrganismiHuman immunodeficiency virus 1Imported
Taxonomic identifieri11676 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL247.
DrugBankiDB01048. Abacavir.
DB00705. Delavirdine.
DB00900. Didanosine.
DB00625. Efavirenz.
DB00879. Emtricitabine.
DB00709. Lamivudine.
DB00238. Nevirapine.
DB08864. Rilpivirine.
DB00649. Stavudine.
DB00300. Tenofovir.
DB00943. Zalcitabine.
DB00495. Zidovudine.

Interactioni

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiQ72547. 1 interaction.
MINTiMINT-8208544.

Chemistry

BindingDBiQ72547.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JLEX-ray2.90A/B1-566[»]
3HYFX-ray1.70A427-506[»]
A517-561[»]
3QINX-ray1.70A427-506[»]
A517-561[»]
3QIOX-ray1.40A427-506[»]
A517-561[»]
ProteinModelPortaliQ72547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ72547.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 234191Reverse transcriptaseInterPro annotationAdd
BLAST
Domaini434 – 557124RNase HInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains 1 reverse transcriptase domain.UniRule annotation
Contains RNase H domain.SAAS annotation

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q72547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI
60 70 80 90 100
GPENPYNTPV FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL
110 120 130 140 150
KKRKSVTVLD VGDAYFSVPL DEDFRKYTAF TIPSINNETP GIRYQYNVLP
160 170 180 190 200
QGWKGSPAIF QSSMTKILEP FRKQNPDIVI YQYMDDLYVG SDLEIGQHRT
210 220 230 240 250
KIEELRQHLL RWGLTTPDKK HQKEPPFLWM GYELHPDKWT VQPIVLPEKD
260 270 280 290 300
SWTVNDIQKL VGKLNWASQI YPGIRVRQLC KLLRGTKALT EVIPLTEEAE
310 320 330 340 350
LELAENREIL KEPVHGVYYD PSKDLIAEIQ KQGQGQWTYQ IYQEPFKNLR
360 370 380 390 400
TGKYARMRGA HTNDVKQLTE AVQKITTESI VIWGKTPKFK LPIQKETWET
410 420 430 440 450
WWTEYWQATW IPEWEFVNTP PLVKLWYQLE KEPIVGAETF YVDGAANRET
460 470 480 490 500
KLGKAGYVTN RGRQKVVTLT DTTNQKTELQ AIYLALQDSG LEVNIVTDSQ
510 520 530 540 550
YALGIIQAQP DQSESELVNQ IIEQLIKKEK VYLAWVPAHK GIGGNEQVDK
560
LVSAGIRKVL FLDGID
Length:566
Mass (Da):65,224
Last modified:November 1, 1996 - v1
Checksum:iAA4B9287ECC4E5C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei566 – 5661Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28646 Genomic DNA. Translation: AAA93161.1.
PIRiA47330.
B47330.
C47330.
D47330.
E47330.
F47330.
S32132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28646 Genomic DNA. Translation: AAA93161.1.
PIRiA47330.
B47330.
C47330.
D47330.
E47330.
F47330.
S32132.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JLEX-ray2.90A/B1-566[»]
3HYFX-ray1.70A427-506[»]
A517-561[»]
3QINX-ray1.70A427-506[»]
A517-561[»]
3QIOX-ray1.40A427-506[»]
A517-561[»]
ProteinModelPortaliQ72547.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ72547. 1 interaction.
MINTiMINT-8208544.

Chemistry

BindingDBiQ72547.
ChEMBLiCHEMBL247.
DrugBankiDB01048. Abacavir.
DB00705. Delavirdine.
DB00900. Didanosine.
DB00625. Efavirenz.
DB00879. Emtricitabine.
DB00709. Lamivudine.
DB00238. Nevirapine.
DB08864. Rilpivirine.
DB00649. Stavudine.
DB00300. Tenofovir.
DB00943. Zalcitabine.
DB00495. Zidovudine.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ72547.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
[Graphical view]
PfamiPF00075. RNase_H. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterisation of foscarnet-resistant strains of human immunodeficiency virus type 1."
    Tachedjian G., Hooker D.J., Gurusinghe A.D., Bazmi H., Deacon N.J., Mellors J., Birch C., Mills J.
    Virology 212:58-68(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HXBCImported.
  2. "Novel indazole non-nucleoside reverse transcriptase inhibitors using molecular hybridization based on crystallographic overlays."
    Jones L.H., Allan G., Barba O., Burt C., Corbau R., Dupont T., Knochel T., Irving S., Middleton D.S., Mowbray C.E., Perros M., Ringrose H., Swain N.A., Webster R., Westby M., Phillips C.
    J. Med. Chem. 52:1219-1223(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS).
  3. "RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information."
    Kirschberg T.A., Balakrishnan M., Squires N.H., Barnes T., Brendza K.M., Chen X., Eisenberg E.J., Jin W., Kutty N., Leavitt S., Liclican A., Liu Q., Liu X., Mak J., Perry J.K., Wang M., Watkins W.J., Lansdon E.B.
    J. Med. Chem. 52:5781-5784(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 427-506 AND 517-561 IN COMPLEX WITH MANGANESE.
  4. "Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors."
    Lansdon E.B., Liu Q., Leavitt S.A., Balakrishnan M., Perry J.K., Lancaster-Moyer C., Kutty N., Liu X., Squires N.H., Watkins W.J., Kirschberg T.A.
    Antimicrob. Agents Chemother. 55:2905-2915(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 427-506 AND 517-561 IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ72547_9HIV1
AccessioniPrimary (citable) accession number: Q72547
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.