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Entry version 106 (08 May 2019)
Sequence version 2 (28 Jun 2011)
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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Walleye dermal sarcoma virus (WDSV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Matrix protein p10: 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 p25 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p14: 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
Protease p15: 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 (By similarity).By similarity
Reverse transcriptase/ribonuclease H p90: 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 p46: 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.1 Publication
Gag-Pol polyprotein: plays a role in budding and is processed by the viral protease during virion maturation outside the cell.By similarity

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 582-Ala and 584-Asp (By similarity).By similarity
The nucleocapsid protein p14 released from Pol polyprotein (NC-pol) is a few amino acids longer than the nucleocapsid protein p14 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 7.0 for protease p14.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei623Protease; shared with dimeric partnerBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi861Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi928Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi929Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi1231Magnesium; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1269Magnesium; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1290Magnesium; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1360Magnesium; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1493Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1550Magnesium; catalytic; for integrase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri501 – 518CCHC-typePROSITE-ProRule annotationAdd BLAST18

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processDNA integration, DNA recombination
LigandMagnesium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A02.063

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Gag-Pol polyprotein
Cleaved into the following 7 chains:
Matrix protein p10
Short name:
MA
Capsid protein p25
Short name:
CA
Nucleocapsid protein p14
Short name:
NC-pol
Protease p15 (EC:3.4.23.-)
Short name:
PR
Reverse transcriptase/ribonuclease H p90 (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.4)
Short name:
RT
Integrase p46 (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:gag-pol
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiWalleye dermal sarcoma virus (WDSV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri39720 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesOrterviralesRetroviridaeOrthoretrovirinaeEpsilonretrovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiSander vitreus (Walleye) (Perca vitrea) [TaxID: 283036]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008337 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000007081 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedSequence analysis
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004105922 – 1752Gag-Pol polyproteinAdd BLAST1751
ChainiPRO_00004105932 – 95Matrix protein p10Add BLAST94
ChainiPRO_000041059496 – 251p20Add BLAST156
ChainiPRO_0000410595252 – 457Capsid protein p25Add BLAST206
ChainiPRO_0000410596458 – 584Nucleocapsid protein p14Add BLAST127
ChainiPRO_0000410597585 – 722Protease p15Add BLAST138
ChainiPRO_0000410598723 – 1372Reverse transcriptase/ribonuclease H p90By similarityAdd BLAST650
ChainiPRO_00004105991373 – 1752Integrase p46By similarityAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by hostBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei95 – 96Cleavage; by viral proteaseBy similarity2
Sitei251 – 252Cleavage; by viral proteaseBy similarity2
Sitei457 – 458Cleavage; by viral proteaseBy similarity2
Sitei584 – 585Cleavage; by viral proteaseBy similarity2
Sitei722 – 723Cleavage; by viral proteaseBy similarity2
Sitei1372 – 1373Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
O92815

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O92815

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein p25 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

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini618 – 694Peptidase A2Add BLAST77
Domaini793 – 977Reverse transcriptasePROSITE-ProRule annotationAdd BLAST185
Domaini1222 – 1368RNase HPROSITE-ProRule annotationAdd BLAST147
Domaini1482 – 1638Integrase catalyticPROSITE-ProRule annotationAdd BLAST157

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili154 – 185Sequence analysisAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi147 – 170Gln-richAdd BLAST24
Compositional biasi181 – 184Poly-Lys4
Compositional biasi484 – 487Poly-Gln4

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri501 – 518CCHC-typePROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
317at10239

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.70.10, 1 hit
3.30.420.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001584 Integrase_cat-core
IPR040643 MLVIN_C
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18697 MLVIN_C, 1 hit
PF00075 RNase_H, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00077 RVP, 1 hit
PF00078 RVT_1, 1 hit
PF00098 zf-CCHC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00343 ZnF_C2HC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
SSF57756 SSF57756, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50994 INTEGRASE, 1 hit
PS50879 RNASE_H, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O92815-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGNSSSTPPP SALKNSDLFK TMLRTQYSGS VKTRRINQDI KKQYPLWPDQ
60 70 80 90 100
GTCATKHWEQ AVLIPLDSVS EETAKVLNFL RVKIQARKGE TARQMTAHTI
110 120 130 140 150
KKLIVGTIDK NKQQTEILQK TDESDEEMDT TNTMLFIARN KRERIAQQQQ
160 170 180 190 200
ADLAAQQQVL LLQREQQREQ REKDIKKRDE KKKKLLPDTT QKVEQTDIGE
210 220 230 240 250
ASSSDASAQK PISTDNNPDL KVDGVLTRSQ HTTVPSNITI KKDGTSVQYQ
260 270 280 290 300
HPIRNYPTGE GNLTAQVRNP FRPLELQQLR KDCPALPEGI PQLAEWLTQT
310 320 330 340 350
MAIYNCDEAD VEQLARVIFP TPVRQIAGVI NGHAAANTAA KIQNYVTACR
360 370 380 390 400
QHYPAVCDWG TIQAFTYKPP QTAHEYVKHA EIIFKNNSGL EWQHATVPFI
410 420 430 440 450
NMVVQGLPPK VTRSLMSGNP DWSTKTIPQI IPLMQHYLNL QSRQDAKIKQ
460 470 480 490 500
TPLVLQLAMP AQTMNGNKGY VGSYPTNEPY YSFQQQQRPA PRAPPGNVPS
510 520 530 540 550
NTCFFCKQPG HWKADCPNKT RNLRNMGNMG RGGRMGGPPY RSQPYPAFIQ
560 570 580 590 600
PPQNHQNQYN GRMDRSQLQA SAQEWLPGTY PAXDPIDCPY EKSGTKTTQD
610 620 630 640 650
VITTKNAEIM VTVNHTKIPM LVDTGACLTA IGGAATVVPD LKLTNTEIIA
660 670 680 690 700
VGISAEPVPH VLAKPTKIQI ENTNIDISPW YNPDQTFHIL GRDTLSKMRA
710 720 730 740 750
IVSFEKNGEM TVLLPPTYHK QLSCQTKNTL NIDEYLLQFP DQLWASLPTD
760 770 780 790 800
IGRMLVPPIT IKIKDNASLP SIRQYPLPKD KTEGLRPLIS SLENQGILIK
810 820 830 840 850
CHSPCNTPIF PIKKAGRDEY RMIHDLRAIN NIVAPLTAVV ASPTTVLSNL
860 870 880 890 900
APSLHWFTVI DLSNAFFSVP IHKDSQYLFA FTFEGHQYTW TVLPQGFIHS
910 920 930 940 950
PTLFSQALYQ SLHKIKFKIS SEICIYMDDV LIASKDRDTN LKDTAVMLQH
960 970 980 990 1000
LASEGHKVSK KKLQLCQQEV VYLGQLLTPE GRKILPDRKV TVSQFQQPTT
1010 1020 1030 1040 1050
IRQIRAFLGL VGYCRHWIPE FSIHSKFLEK QLKKDTAEPF QLDDQQVEAF
1060 1070 1080 1090 1100
NKLKHAITTA PVLVVPDPAK PFQLYTSHSE HASIAVLTQK HAGRTRPIAF
1110 1120 1130 1140 1150
LSSKFDAIES GLPPCLKACA SIHRSLTQAD SFILGAPLII YTTHAICTLL
1160 1170 1180 1190 1200
QRDRSQLVTA SRFSKWEADL LRPELTFVAC SAVSPAHLYM QSCENNIPPH
1210 1220 1230 1240 1250
DCVLLTHTIS RPRPDLSDLP IPDPDMTLFS DGSYTTGRGG AAVVMHRPVT
1260 1270 1280 1290 1300
DDFIIIHQQP GGASAQTAEL LALAAACHLA TDKTVNIYTD SRYAYGVVHD
1310 1320 1330 1340 1350
FGHLWMHRGF VTSAGTPIKN HKEIEYLLKQ IMKPKQVSVI KIEAHTKGVS
1360 1370 1380 1390 1400
MEVRGNAAAD EAAKNAVFLV QRVLKKGDAL ASTDLVMEYS ETDEKFTAGA
1410 1420 1430 1440 1450
ELHDGVFMRG DLIVPPLEML HAILLAIHGV SHTHKGGIMS YFSKFWTHPK
1460 1470 1480 1490 1500
ASQTIDLILG HCQICLKHNP KYKSRLQGHR PLPSRPFAHL QIDFVQMCVK
1510 1520 1530 1540 1550
KPMYALVIID VFSKWPEIIP CNKEDAKTVC DILMKDIIPR WGLPDQIDSD
1560 1570 1580 1590 1600
QGTHFTAKIS QELTHSIGVA WKLHCPGHPR SSGIVERTNR TLKSKIIKAQ
1610 1620 1630 1640 1650
EQLQLSKWTE VLPYVLLEMR ATPKKHGLSP HEIVMGRPMK TTYLSDMSPL
1660 1670 1680 1690 1700
WATDTLVTYM NKLTRQLSAY HQQVVDQWPS TSLPPGPEPG SWCMLRNPKK
1710 1720 1730 1740 1750
SSNWEGPFLI LLSTPTAVKV EGRPTWIHLD HCKLLRSSLS SSLGGPVNQL

LS
Length:1,752
Mass (Da):196,265
Last modified:June 28, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA9DEF76316FBE4E0
GO

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L41838 Genomic RNA No translation available.
AF033822 Genomic RNA Translation: AAC82611.1

Protein sequence database of the Protein Information Resource

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PIRi
T09394

NCBI Reference Sequences

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RefSeqi
NP_045937.2, NC_001867.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
1403495

Keywords - Coding sequence diversityi

RNA suppression of termination

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41838 Genomic RNA No translation available.
AF033822 Genomic RNA Translation: AAC82611.1
PIRiT09394
RefSeqiNP_045937.2, NC_001867.1

3D structure databases

Database of comparative protein structure models

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ModBasei
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Protein family/group databases

MEROPSiA02.063

Proteomic databases

PRIDEiO92815

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1403495

Phylogenomic databases

OrthoDBi317at10239

Miscellaneous databases

PMAP-CutDBiO92815

Family and domain databases

Gene3Di2.40.70.10, 1 hit
3.30.420.10, 2 hits
InterProiView protein in InterPro
IPR001584 Integrase_cat-core
IPR040643 MLVIN_C
IPR021109 Peptidase_aspartic_dom_sf
IPR018061 Retropepsins
IPR012337 RNaseH-like_sf
IPR002156 RNaseH_domain
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF18697 MLVIN_C, 1 hit
PF00075 RNase_H, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00077 RVP, 1 hit
PF00078 RVT_1, 1 hit
PF00098 zf-CCHC, 1 hit
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 1 hit
SUPFAMiSSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 2 hits
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
PS50994 INTEGRASE, 1 hit
PS50879 RNASE_H, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOL_WDSV
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O92815
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 8, 2019
This is version 106 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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