Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P16088

- POL_FIVPE

UniProt

P16088 - POL_FIVPE

Protein

Pol polyprotein

Gene

pol

Organism
Feline immunodeficiency virus (isolate Petaluma) (FIV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
    3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
    dUTP + H2O = dUMP + diphosphate.
    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei68 – 681For protease activity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri848 – 88942Integrase-typePROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi1067 – 111549Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. dUTP diphosphatase activity Source: UniProtKB-EC
    4. exoribonuclease H activity Source: UniProtKB-EC
    5. RNA binding Source: InterPro
    6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    7. RNA-DNA hybrid ribonuclease activity Source: InterPro
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA integration Source: UniProtKB-KW
    2. DNA recombination Source: UniProtKB-KW
    3. dUTP metabolic process Source: InterPro
    4. establishment of integrated proviral latency Source: UniProtKB-KW
    5. viral entry into host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

    Keywords - Biological processi

    DNA integration, DNA recombination, Nucleotide metabolism, Viral genome integration, Virus entry into host cell

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pol polyprotein
    Cleaved into the following 4 chains:
    Alternative name(s):
    Retropepsin (EC:3.4.23.-)
    Alternative name(s):
    Exoribonuclease H (EC:3.1.13.2)
    Integrase
    Short name:
    IN
    Gene namesi
    Name:pol
    OrganismiFeline immunodeficiency virus (isolate Petaluma) (FIV)
    Taxonomic identifieri11674 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusFeline lentivirus group
    Virus hostiFelidae (cat family) [TaxID: 9681]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154ProteasePRO_0000038841Add
    BLAST
    Chaini155 – 690536Reverse transcriptase/ribonuclease HPRO_0000038842Add
    BLAST
    Chaini691 – 843153Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000038843Add
    BLAST
    Chaini844 – 1124281IntegrasePRO_0000038844Add
    BLAST

    Post-translational modificationi

    Cleavage sites that yield the mature proteins remain to be determined.

    Proteomic databases

    PRIDEiP16088.

    Structurei

    Secondary structure

    1
    1124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 503
    Beta strandi53 – 586
    Beta strandi61 – 677
    Beta strandi71 – 733
    Beta strandi75 – 773
    Helixi78 – 803
    Beta strandi87 – 9610
    Beta strandi99 – 11315
    Turni115 – 1173
    Beta strandi121 – 13010
    Beta strandi136 – 1405
    Helixi142 – 1454
    Turni146 – 1494
    Beta strandi151 – 1533
    Beta strandi713 – 7186
    Beta strandi726 – 7316
    Beta strandi736 – 7383
    Beta strandi743 – 7475
    Beta strandi751 – 7533
    Beta strandi758 – 7636
    Helixi766 – 7694
    Turni770 – 7723
    Beta strandi773 – 7764
    Beta strandi778 – 7803
    Beta strandi789 – 7946
    Beta strandi796 – 7983
    Beta strandi800 – 8023
    Beta strandi807 – 8159
    Beta strandi830 – 8323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B11X-ray1.90A42-154[»]
    1DUTX-ray1.90A/B711-843[»]
    1F7DX-ray1.40A/B711-846[»]
    1F7KX-ray2.20A/B711-846[»]
    1F7NX-ray2.20A/B711-846[»]
    1F7OX-ray2.20A/B/C711-846[»]
    1F7PX-ray2.30A/B/C711-846[»]
    1F7QX-ray2.26A/B/C711-846[»]
    1F7RX-ray2.50A711-846[»]
    1FIVX-ray2.00A42-154[»]
    2FIVX-ray2.00A/B39-154[»]
    2HAHX-ray1.70A39-154[»]
    3FIVX-ray1.85A/B39-154[»]
    3OGPX-ray1.70A/B39-154[»]
    3OGQX-ray1.80A/B39-154[»]
    4FIVX-ray1.80A42-154[»]
    5FIVX-ray1.90A42-154[»]
    6FIVX-ray1.90A42-154[»]
    ProteinModelPortaliP16088.
    SMRiP16088. Positions 42-154, 711-843.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16088.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 14482Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini200 – 389190Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 712121RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini899 – 1049151Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the retroviral Pol polyprotein family.Curated
    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 integrase-type zinc finger.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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri848 – 88942Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Family and domain databases

    Gene3Di1.10.10.200. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    2.70.40.10. 1 hit.
    3.30.420.10. 2 hits.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    [Graphical view]
    PfamiPF00692. dUTPase. 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.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    [Graphical view]
    SUPFAMiSSF46919. SSF46919. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF51283. SSF51283. 1 hit.
    SSF53098. SSF53098. 2 hits.
    TIGRFAMsiTIGR00576. dut. 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.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16088-1 [UniParc]FASTAAdd to Basket

    « Hide

    KEFGKLEGGA SCSPSESNAA SSNAICTSNG GETIGFVNYN KVGTTTTLEK     50
    RPEILIFVNG YPIKFLLDTG ADITILNRRD FQVKNSIENG RQNMIGVGGG 100
    KRGTNYINVH LEIRDENYKT QCIFGNVCVL EDNSLIQPLL GRDNMIKFNI 150
    RLVMAQISDK IPVVKVKMKD PNKGPQIKQW PLTNEKIEAL TEIVERLEKE 200
    GKVKRADSNN PWNTPVFAIK KKSGKWRMLI DFRELNKLTE KGAEVQLGLP 250
    HPAGLQIKKQ VTVLDIGDAY FTIPLDPDYA PYTAFTLPRK NNAGPGRRFV 300
    WCSLPQGWIL SPLIYQSTLD NIIQPFIRQN PQLDIYQYMD DIYIGSNLSK 350
    KEHKEKVEEL RKLLLWWGFE TPEDKLQEEP PYTWMGYELH PLTWTIQQKQ 400
    LDIPEQPTLN ELQKLAGKIN WASQAIPDLS IKALTNMMRG NQNLNSTRQW 450
    TKEARLEVQK AKKAIEEQVQ LGYYDPSKEL YAKLSLVGPH QISYQVYQKD 500
    PEKILWYGKM SRQKKKAENT CDIALRACYK IREESIIRIG KEPRYEIPTS 550
    REAWESNLIN SPYLKAPPPE VEYIHAALNI KRALSMIKDA PIPGAETWYI 600
    DGGRKLGKAA KAAYWTDTGK WRVMDLEGSN QKAEIQALLL ALKAGSEEMN 650
    IITDSQYVIN IILQQPDMME GIWQEVLEEL EKKTAIFIDW VPGHKGIPGN 700
    EEVDKLCQTM MIIEGDGILD KRSEDAGYDL LAAKEIHLLP GEVKVIPTGV 750
    KLMLPKGYWG LIIGKSSIGS KGLDVLGGVI DEGYRGEIGV IMINVSRKSI 800
    TLMERQKIAQ LIILPCKHEV LEQGKVVMDS ERGDNGYGST GVFSSWVDRI 850
    EEAEINHEKF HSDPQYLRTE FNLPKMVAEE IRRKCPVCRI IGEQVGGQLK 900
    IGPGIWQMDC THFDGKIILV GIHVESGYIW AQIISQETAD CTVKAVLQLL 950
    SAHNVTELQT DNGPNFKNQK MEGVLNYMGV KHKFGIPGNP QSQALVENVN 1000
    HTLKVWIQKF LPETTSLDNA LSLAVHSLNF KRRGRIGGMA PYELLAQQES 1050
    LRIQDYFSAI PQKLQAQWIY YKDQKDKKWK GPMRVEYWGQ GSVLLKDEEK 1100
    GYFLIPRRHI RRVPEPCALP EGDE 1124
    Length:1,124
    Mass (Da):127,494
    Last modified:April 1, 1990 - v1
    Checksum:iEE8214169BE39CF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25381 Genomic RNA. Translation: AAB59937.1. Sequence problems.
    PIRiB33543. GNLJFP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25381 Genomic RNA. Translation: AAB59937.1 . Sequence problems.
    PIRi B33543. GNLJFP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B11 X-ray 1.90 A 42-154 [» ]
    1DUT X-ray 1.90 A/B 711-843 [» ]
    1F7D X-ray 1.40 A/B 711-846 [» ]
    1F7K X-ray 2.20 A/B 711-846 [» ]
    1F7N X-ray 2.20 A/B 711-846 [» ]
    1F7O X-ray 2.20 A/B/C 711-846 [» ]
    1F7P X-ray 2.30 A/B/C 711-846 [» ]
    1F7Q X-ray 2.26 A/B/C 711-846 [» ]
    1F7R X-ray 2.50 A 711-846 [» ]
    1FIV X-ray 2.00 A 42-154 [» ]
    2FIV X-ray 2.00 A/B 39-154 [» ]
    2HAH X-ray 1.70 A 39-154 [» ]
    3FIV X-ray 1.85 A/B 39-154 [» ]
    3OGP X-ray 1.70 A/B 39-154 [» ]
    3OGQ X-ray 1.80 A/B 39-154 [» ]
    4FIV X-ray 1.80 A 42-154 [» ]
    5FIV X-ray 1.90 A 42-154 [» ]
    6FIV X-ray 1.90 A 42-154 [» ]
    ProteinModelPortali P16088.
    SMRi P16088. Positions 42-154, 711-843.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P16088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P16088.

    Family and domain databases

    Gene3Di 1.10.10.200. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    2.70.40.10. 1 hit.
    3.30.420.10. 2 hits.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    [Graphical view ]
    Pfami PF00692. dUTPase. 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.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46919. SSF46919. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF51283. SSF51283. 1 hit.
    SSF53098. SSF53098. 2 hits.
    TIGRFAMsi TIGR00576. dut. 1 hit.
    PROSITEi 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.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Clone 34TF10.
    2. "Nucleotide sequence analysis of feline immunodeficiency virus: genome organization and relationship to other lentiviruses."
      Olmsted R.A., Hirsch V.M., Purcell R.H., Johnson P.R.
      Proc. Natl. Acad. Sci. U.S.A. 86:8088-8092(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Clone FIV-14.
    3. "Identification of proteolytic processing sites within the Gag and Pol polyproteins of feline immunodeficiency virus."
      Elder J.H., Schnoelzer M., Hasselkus-Light C.S., Henson M., Lerner D.A., Phillips T.R., Wagaman P.C., Kent S.B.H.
      J. Virol. 67:1869-1876(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154.
    5. "Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor."
      Laco G.S., Schalk-Hihi C., Lubkowski J., Morris G., Zdanov A., Olson A., Elder J.H., Wlodawer A., Gustchina A.
      Biochemistry 36:10696-10708(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154.
    6. "Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus."
      Prasad G.S., Stura E.A., McRee D.E., Laco G.S., Hasselkus-Light C., Elder J.H., Stout C.D.
      Protein Sci. 5:2429-2437(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 711-827.

    Entry informationi

    Entry nameiPOL_FIVPE
    AccessioniPrimary (citable) accession number: P16088
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Multifunctional enzyme

    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

    External Data

    Dasty 3