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)

A1Z651

- POL_XMRV6

UniProt

A1Z651 - POL_XMRV6

Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Xenotropic MuLV-related virus (isolate VP62) (XMRV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Matrix protein p15 targets Gag and gag-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.By similarity
    Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
    Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization By similarity.By similarity
    The aspartyl protease mediates proteolytic cleavages of Gag and Gag-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.PROSITE-ProRule annotation
    Reverse transcriptase/ribonuclease H is a multifunctional enzyme that converts the viral dimeric 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 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 primers. 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.By similarity
    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 CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In 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 last step is viral DNA integration into host chromosome By similarity.By similarity
    Gag-Pol polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
    Binds 2 magnesium ions for ribonuclease H (RNase H) activity.By similarity
    Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei129 – 1302Cleavage; by viral protease p14By similarity
    Sitei213 – 2142Cleavage; by viral protease p14By similarity
    Sitei476 – 4772Cleavage; by viral protease p14By similarity
    Sitei532 – 5332Cleavage; by viral protease p14By similarity
    Active sitei564 – 5641Protease; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei657 – 6582Cleavage; by viral protease p14By similarity
    Metal bindingi807 – 8071Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi881 – 8811Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi882 – 8821Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi1181 – 11811Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1219 – 12191Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1240 – 12401Magnesium; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1310 – 13101Magnesium; for RNase H activityPROSITE-ProRule annotation
    Sitei1328 – 13292Cleavage; by viral protease p14By similarity
    Metal bindingi1453 – 14531Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1512 – 15121Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri500 – 51718CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    4. identical protein binding Source: IntAct
    5. RNA binding Source: UniProtKB-KW
    6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    7. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
    8. structural constituent of virion Source: UniProtKB-KW
    9. zinc ion binding Source: InterPro

    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
    5. virion assembly Source: InterPro

    Keywords - Molecular functioni

    Aspartyl protease, DNA-directed DNA polymerase, 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

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

    Protein family/group databases

    MEROPSiA02.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag-Pol polyprotein
    Short name:
    Pr180gag-pol
    Cleaved into the following 7 chains:
    Matrix protein p15
    Short name:
    MA
    Alternative name(s):
    pp12
    Capsid protein p30
    Short name:
    CA
    Nucleocapsid protein p10
    Short name:
    NC-pol
    Protease p14 (EC:3.4.23.-)
    Short name:
    PR
    Integrase p46
    Short name:
    IN
    Gene namesi
    Name:gag-pol
    OrganismiXenotropic MuLV-related virus (isolate VP62) (XMRV)
    Taxonomic identifieri373193 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000002240: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-KW
    3. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host membrane, Membrane, Viral matrix protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 17331732Gag-Pol polyproteinBy similarityPRO_0000390868Add
    BLAST
    Chaini2 – 129128Matrix protein p15By similarityPRO_0000390869Add
    BLAST
    Chaini130 – 21384RNA-binding phosphoprotein p12By similarityPRO_0000390870Add
    BLAST
    Chaini214 – 476263Capsid protein p30By similarityPRO_0000390871Add
    BLAST
    Chaini477 – 53256Nucleocapsid protein p10By similarityPRO_0000390872Add
    BLAST
    Chaini533 – 657125Protease p14By similarityPRO_0000390873Add
    BLAST
    Chaini658 – 1328671Reverse transcriptase/ribonuclease H p80By similarityPRO_0000390874Add
    BLAST
    Chaini1329 – 1733405Integrase p46By similarityPRO_0000390875Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei190 – 1901Phosphoserine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation By similarity.By similarity
    Capsid protein p30 is sumoylated; which is required for virus replication.
    RNA-binding phosphoprotein p12 is phosphorylated on serine residues.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Interactioni

    Subunit structurei

    Capsid protein p30 is a homohexamer, that further associates as homomultimer. The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a monomer By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-7978477,EBI-7978477

    Protein-protein interaction databases

    IntActiA1Z651. 1 interaction.
    MINTiMINT-8386873.

    Structurei

    Secondary structure

    1
    1733
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi540 – 5423
    Beta strandi547 – 5548
    Beta strandi557 – 5637
    Beta strandi578 – 5869
    Beta strandi593 – 5986
    Beta strandi601 – 6055
    Beta strandi608 – 6125
    Beta strandi620 – 6223
    Helixi627 – 6337
    Beta strandi636 – 6394
    Beta strandi644 – 6474
    Helixi687 – 6893
    Helixi691 – 6944
    Helixi725 – 7306
    Helixi732 – 7398
    Turni740 – 7423
    Beta strandi743 – 7464
    Helixi775 – 7784
    Turni789 – 7913
    Helixi792 – 7954
    Beta strandi802 – 8087
    Helixi812 – 8143
    Beta strandi815 – 8173
    Turni819 – 8213
    Helixi822 – 8243
    Beta strandi825 – 8273
    Beta strandi840 – 8445
    Helixi852 – 87019
    Beta strandi874 – 8796
    Beta strandi882 – 8898
    Helixi890 – 90718
    Beta strandi913 – 9153
    Beta strandi917 – 9259
    Beta strandi928 – 9314
    Beta strandi934 – 9374
    Helixi939 – 9468
    Helixi954 – 96411
    Helixi965 – 9706
    Helixi974 – 9774
    Turni978 – 9814
    Helixi982 – 9843
    Helixi995 – 100915
    Beta strandi1023 – 10308
    Beta strandi1033 – 104210
    Beta strandi1045 – 105511
    Helixi1058 – 10625
    Helixi1065 – 108420
    Beta strandi1089 – 10957
    Helixi1098 – 11025
    Helixi1114 – 11218
    Turni1124 – 11263
    Beta strandi1127 – 11326
    Turni1137 – 11404
    Beta strandi1167 – 11693
    Beta strandi1175 – 118713
    Beta strandi1190 – 11989
    Beta strandi1203 – 12097
    Helixi1215 – 122915
    Turni1230 – 12323
    Beta strandi1233 – 12397
    Helixi1242 – 12498
    Helixi1252 – 12554
    Beta strandi1257 – 12615
    Helixi1271 – 128010
    Beta strandi1283 – 12919
    Helixi1293 – 12953
    Beta strandi1296 – 13005
    Helixi1301 – 132121

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NR6X-ray1.97A/B533-657[»]
    3P1GX-ray1.50A1155-1328[»]
    4E89X-ray2.60A1164-1320[»]
    4HKQX-ray3.04A658-1328[»]
    ProteinModelPortaliA1Z651.
    SMRiA1Z651. Positions 2-98, 214-345, 350-380, 477-532, 681-1131, 1160-1325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini559 – 62971Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini739 – 930192Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1172 – 1318147RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini1442 – 1600159Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili436 – 47641Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi109 – 1124PTAP/PSAP motif
    Motifi128 – 1325LYPX(n)L motif
    Motifi161 – 1644PPXY motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 191121Pro-richAdd
    BLAST
    Compositional biasi71 – 16898Pro-richAdd
    BLAST

    Domaini

    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. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. contains By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.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 fingeri500 – 51718CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Family and domain databases

    Gene3Di1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR001584. Integrase_cat-core.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    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.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    A1Z651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW     50
    PQDGTFNLGV ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF 100
    VSPKPPPLPT APVLPPGPSA QPPSRSALYP ALTPSIKSKP PKPQVLPDSG 150
    GPLIDLLTED PPPYGAQPSS SARENNEEEA ATTSEVSPPS PMVSRLRGRR 200
    DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN PSFSEDPGKL 250
    TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT 300
    QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA 350
    KVKGITQGPN ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA 400
    PDIGRKLERL EDLKSKTLGD LVREAEKIFN KRETPEEREE RIRREIEEKE 450
    ERRRAEDEQR ERERDRRRHR EMSKLLATVV IGQRQDRQGG ERRRPQLDKD 500
    QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGDXGGQ GQEPPPEPRI 550
    TLKVGGQPVT FLVDTGAQHS VLTQNPGPLS DKSAWVQGAT GGKRYRWTTD 600
    RKVHLATGKV THSFLHVPDC PYPLLGRDLL TKLKAQIHFE GSGAQVVGPM 650
    GQPLQVLTLN IEDEYRLHET SKEPDVPLGS TWLSDFPQAW AETGGMGLAV 700
    RQAPLIIPLK ATSTPVSIKQ YPMSQEARLG IKPHIQRLLD QGILVPCQSP 750
    WNTPLLPVKK PGTNDYRPVQ DLREVNKRVE DIHPTVPNPY NLLSGLPPSH 800
    QWYTVLDLKD AFFCLRLHPT SQPLFAFEWR DPEMGISGQL TWTRLPQGFK 850
    NSPTLFDEAL HRDLADFRIQ HPDLILLQYV DDLLLAATSE QDCQRGTRAL 900
    LQTLGNLGYR ASAKKAQICQ KQVKYLGYLL KEGQRWLTEA RKETVMGQPT 950
    PKTPRQLREF LGTAGFCRLW IPGFAEMAAP LYPLTKTGTL FNWGPDQQKA 1000
    YQEIKQALLT APALGLPDLT KPFELFVDEK QGYAKGVLTQ KLGPWRRPVA 1050
    YLSKKLDPVA AGWPPCLRMV AAIAVLTKDA GKLTMGQPLV ILAPHAVEAL 1100
    VKQPPDRWLS NARMTHYQAM LLDTDRVQFG PVVALNPATL LPLPEKEAPH 1150
    DCLEILAETH GTRPDLTDQP IPDADYTWYT DGSSFLQEGQ RRAGAAVTTE 1200
    TEVIWARALP AGTSAQRAEL IALTQALKMA EGKKLNVYTD SRYAFATAHV 1250
    HGEIYRRRGL LTSEGREIKN KNEILALLKA LFLPKRLSII HCPGHQKGNS 1300
    AEARGNRMAD QAAREAAMKA VLETSTLLIE DSTPYTPPHF HYTETDLKRL 1350
    RELGATYNQT KGYWVLQGKP VMPDQSVFEL LDSLHRLTHL SPQKMKALLD 1400
    REESPYYMLN RDRTIQYVTE TCTACAQVNA SKAKIGAGVR VRGHRPGTHW 1450
    EVDFTEVKPG LYGYKYLLVF VDTFSGWVEA FPTKRETAKV VSKKLLEDIF 1500
    PRFGMPQVLG SDNGPAFASQ VSQSVADLLG IDWKLHCAYR PQSSGQVERM 1550
    NRTIKETLTK LTLASGTRDW VLLLPLALYR ARNTPGPHGL TPYEILYGAP 1600
    PPLVNFHDPE MSKLTNSPSL QAHLQALQAV QQEVWKPLAA AYQDQLDQPV 1650
    IPHPFRVGDA VWVRRHQTKN LEPRWKGPYT VLLTTPTALK VDGISAWIHA 1700
    AHVKAATTPP AGTAWKVQRS QNPLKIRLTR GAP 1733
    Length:1,733
    Mass (Da):193,862
    Last modified:February 6, 2007 - v1
    Checksum:i5A4D87D1E1D7069D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti659 – 6591L → V.
    Natural varianti666 – 6661R → W.
    Natural varianti669 – 6713ETS → DTR.
    Natural varianti687 – 6871P → L.
    Natural varianti1079 – 10791D → N.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399707 Genomic RNA. Translation: ABD49687.1.
    EF185282 Genomic RNA. Translation: ABM47428.1.

    Keywords - Coding sequence diversityi

    RNA suppression of termination

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399707 Genomic RNA. Translation: ABD49687.1 .
    EF185282 Genomic RNA. Translation: ABM47428.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NR6 X-ray 1.97 A/B 533-657 [» ]
    3P1G X-ray 1.50 A 1155-1328 [» ]
    4E89 X-ray 2.60 A 1164-1320 [» ]
    4HKQ X-ray 3.04 A 658-1328 [» ]
    ProteinModelPortali A1Z651.
    SMRi A1Z651. Positions 2-98, 214-345, 350-380, 477-532, 681-1131, 1160-1325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A1Z651. 1 interaction.
    MINTi MINT-8386873.

    Protein family/group databases

    MEROPSi A02.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR001584. Integrase_cat-core.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    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.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant."
      Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H., DeRisi J.L.
      PLoS Pathog. 2:E25-E25(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "An infectious retrovirus susceptible to an IFN antiviral pathway from human prostate tumors."
      Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A., Ganem D., Derisi J.L., Chow S.A., Silverman R.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOL_XMRV6
    AccessioniPrimary (citable) accession number: A1Z651
    Secondary accession number(s): Q27IE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 19, 2010
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 71 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 translated as a gag-pol fusion protein by episodic readthrough of the gag protein termination codon. Readthrough of the terminator codon TAG occurs between the codons for 536-Asp and 538-Gly By similarity.By similarity
    The nucleocapsid protein p10 released from Pol polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid protein p10 released from Gag polyprotein (NC-gag).By similarity
    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 swiching 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.PROSITE-ProRule annotation

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    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