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A1Z651

- POL_XMRV6

UniProt

A1Z651 - POL_XMRV6

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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

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
Complete GO annotation...

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-KW
  2. membrane Source: UniProtKB-KW
  3. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

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

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

        10         20         30         40         50
MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW
60 70 80 90 100
PQDGTFNLGV ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF
110 120 130 140 150
VSPKPPPLPT APVLPPGPSA QPPSRSALYP ALTPSIKSKP PKPQVLPDSG
160 170 180 190 200
GPLIDLLTED PPPYGAQPSS SARENNEEEA ATTSEVSPPS PMVSRLRGRR
210 220 230 240 250
DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN PSFSEDPGKL
260 270 280 290 300
TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
310 320 330 340 350
QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA
360 370 380 390 400
KVKGITQGPN ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA
410 420 430 440 450
PDIGRKLERL EDLKSKTLGD LVREAEKIFN KRETPEEREE RIRREIEEKE
460 470 480 490 500
ERRRAEDEQR ERERDRRRHR EMSKLLATVV IGQRQDRQGG ERRRPQLDKD
510 520 530 540 550
QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGDXGGQ GQEPPPEPRI
560 570 580 590 600
TLKVGGQPVT FLVDTGAQHS VLTQNPGPLS DKSAWVQGAT GGKRYRWTTD
610 620 630 640 650
RKVHLATGKV THSFLHVPDC PYPLLGRDLL TKLKAQIHFE GSGAQVVGPM
660 670 680 690 700
GQPLQVLTLN IEDEYRLHET SKEPDVPLGS TWLSDFPQAW AETGGMGLAV
710 720 730 740 750
RQAPLIIPLK ATSTPVSIKQ YPMSQEARLG IKPHIQRLLD QGILVPCQSP
760 770 780 790 800
WNTPLLPVKK PGTNDYRPVQ DLREVNKRVE DIHPTVPNPY NLLSGLPPSH
810 820 830 840 850
QWYTVLDLKD AFFCLRLHPT SQPLFAFEWR DPEMGISGQL TWTRLPQGFK
860 870 880 890 900
NSPTLFDEAL HRDLADFRIQ HPDLILLQYV DDLLLAATSE QDCQRGTRAL
910 920 930 940 950
LQTLGNLGYR ASAKKAQICQ KQVKYLGYLL KEGQRWLTEA RKETVMGQPT
960 970 980 990 1000
PKTPRQLREF LGTAGFCRLW IPGFAEMAAP LYPLTKTGTL FNWGPDQQKA
1010 1020 1030 1040 1050
YQEIKQALLT APALGLPDLT KPFELFVDEK QGYAKGVLTQ KLGPWRRPVA
1060 1070 1080 1090 1100
YLSKKLDPVA AGWPPCLRMV AAIAVLTKDA GKLTMGQPLV ILAPHAVEAL
1110 1120 1130 1140 1150
VKQPPDRWLS NARMTHYQAM LLDTDRVQFG PVVALNPATL LPLPEKEAPH
1160 1170 1180 1190 1200
DCLEILAETH GTRPDLTDQP IPDADYTWYT DGSSFLQEGQ RRAGAAVTTE
1210 1220 1230 1240 1250
TEVIWARALP AGTSAQRAEL IALTQALKMA EGKKLNVYTD SRYAFATAHV
1260 1270 1280 1290 1300
HGEIYRRRGL LTSEGREIKN KNEILALLKA LFLPKRLSII HCPGHQKGNS
1310 1320 1330 1340 1350
AEARGNRMAD QAAREAAMKA VLETSTLLIE DSTPYTPPHF HYTETDLKRL
1360 1370 1380 1390 1400
RELGATYNQT KGYWVLQGKP VMPDQSVFEL LDSLHRLTHL SPQKMKALLD
1410 1420 1430 1440 1450
REESPYYMLN RDRTIQYVTE TCTACAQVNA SKAKIGAGVR VRGHRPGTHW
1460 1470 1480 1490 1500
EVDFTEVKPG LYGYKYLLVF VDTFSGWVEA FPTKRETAKV VSKKLLEDIF
1510 1520 1530 1540 1550
PRFGMPQVLG SDNGPAFASQ VSQSVADLLG IDWKLHCAYR PQSSGQVERM
1560 1570 1580 1590 1600
NRTIKETLTK LTLASGTRDW VLLLPLALYR ARNTPGPHGL TPYEILYGAP
1610 1620 1630 1640 1650
PPLVNFHDPE MSKLTNSPSL QAHLQALQAV QQEVWKPLAA AYQDQLDQPV
1660 1670 1680 1690 1700
IPHPFRVGDA VWVRRHQTKN LEPRWKGPYT VLLTTPTALK VDGISAWIHA
1710 1720 1730
AHVKAATTPP AGTAWKVQRS QNPLKIRLTR GAP
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.
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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 29, 2014
This is version 72 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