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Pol polyprotein [Cleaved into: Protease (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_MLVRD               Reviewed;        1734 AA.
P11227;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
31-JAN-2018, sequence version 2.
12-SEP-2018, entry version 119.
RecName: Full=Gag-Pol polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10-Pol;
Short=NC-pol;
Contains:
RecName: Full=Protease;
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
Name=pol;
Radiation murine leukemia virus.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; Murine leukemia virus.
NCBI_TaxID=11787;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3033897; DOI=10.1016/0042-6822(87)90241-8;
Merregaert J., Janowski M., Reddy E.P.;
"Nucleotide sequence of a radiation leukemia virus genome.";
Virology 158:88-102(1987).
-!- FUNCTION: 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-Pol, or to Gag-Pol binding host
factors. Interaction with HECT ubiquitin ligases probably links
the viral protein to the host ESCRT pathway and facilitates
release. {ECO:0000250|UniProtKB:P03332}.
-!- FUNCTION: 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 pre-integration complex.
{ECO:0000250|UniProtKB:P03332}.
-!- FUNCTION: RNA-binding phosphoprotein p12: Constituent of the pre-
integration complex (PIC) which tethers the latter to mitotic
chromosomes. This allows the integration of the viral genome into
the host DNA. {ECO:0000250|UniProtKB:P03355}.
-!- FUNCTION: Capsid protein p30: Forms the spherical core of the
virion that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03336}.
-!- FUNCTION: Nucleocapsid protein p10-Pol: Involved in the packaging
and encapsidation of two copies of the genome (By similarity).
Binds with high affinity to conserved UCUG elements within the
packaging signal, located near the 5'-end of the genome (By
similarity). This binding is dependent on genome dimerization (By
similarity). Acts as a nucleic acid chaperone which is involved in
rearrangement of nucleic acid secondary structures during gRNA
retrotranscription (By similarity). {ECO:0000250|UniProtKB:P03332,
ECO:0000250|UniProtKB:P03355}.
-!- FUNCTION: Protease: 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 (Potential). Cleaves the translation initiation factor eIF4G
leading to the inhibition of host cap-dependent translation (By
similarity). {ECO:0000250|UniProtKB:P03332, ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: RT 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.
{ECO:0000255}.
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:P03355}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
Note=The RT polymerase active site binds 2 magnesium ions.
{ECO:0000255|PROSITE-ProRule:PRU00405};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P03355};
Note=Binds 1 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250|UniProtKB:P03355};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P03355};
Note=Magnesium ions are required for integrase activity. Binds at
least 1, maybe 2 magnesium ions. {ECO:0000250|UniProtKB:P03355};
-!- ACTIVITY REGULATION: Protease: Most efficiently inhibited by
Amprenavir, which is able to block Gag-Pol processing in infected
cells. {ECO:0000250|UniProtKB:P03355}.
-!- SUBUNIT: Capsid protein p30: Homohexamer; further associates as
homomultimer (By similarity). Capsid protein p30: The virus core
is composed of a lattice formed from hexagonal rings, each
containing six capsid monomers (By similarity). Capsid protein
p30: Interacts with mouse UBE2I and mouse PIAS4 (By similarity).
Gag-Pol polyprotein: Interacts (via PPXY motif) with host NEDD4
(By similarity). Gag-Pol polyprotein: Interacts (via PSAP motif)
with host TSG101 (By similarity). Gag-Pol polyprotein: Interacts
(via LYPX(n)L motif) with host PDCD6IP (By similarity). Reverse
transcriptase/ribonuclease H: The reverse transcriptase is a
monomer (Potential). Reverse transcriptase/ribonuclease H:
Interacts (via RNase domains) with host release factor ETF1; this
interaction is essential for translational readthrough of amber
codon between viral gag and pol genes, as well as for viral
replication (By similarity). Integrase: Homodimer (By similarity).
{ECO:0000250|UniProtKB:P03355, ECO:0000255|PROSITE-
ProRule:PRU00405}.
-!- SUBCELLULAR LOCATION: Gag-Pol polyprotein: Virion
{ECO:0000250|UniProtKB:P03332}. Host cell membrane
{ECO:0000250|UniProtKB:P03332}; Lipid-anchor
{ECO:0000250|UniProtKB:P03332}. Host late endosome membrane
{ECO:0000250|UniProtKB:P03332}; Lipid-anchor
{ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P26807}. Note=These locations are
probably linked to virus assembly sites.
{ECO:0000250|UniProtKB:P03355}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion
{ECO:0000250|UniProtKB:P03355}.
-!- SUBCELLULAR LOCATION: Capsid protein p30: Virion
{ECO:0000250|UniProtKB:P03355}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p10-Pol: Virion
{ECO:0000250|UniProtKB:P03355}.
-!- SUBCELLULAR LOCATION: Protease: Virion
{ECO:0000250|UniProtKB:P03355}.
-!- SUBCELLULAR LOCATION: RNA-binding phosphoprotein p12: Host
cytoplasm {ECO:0000250|UniProtKB:P03355}. Note=Localizes to the
host cytoplasm early in infection and binds to the mitotic
chromosomes later on. {ECO:0000250|UniProtKB:P03355}.
-!- DOMAIN: Gag-Pol polyprotein: 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.
{ECO:0000250|UniProtKB:P03332}.
-!- PTM: Gag-Pol polyprotein: Ubiquitinated by ITCH. Gag can recruit
the ubiquitin ligase Itch in an L domain-independent manner to
facilitate virus release via a mechanism that involves Gag
ubiquitination. {ECO:0000250|UniProtKB:P03332}.
-!- PTM: Gag-Pol polyprotein: 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.
{ECO:0000250|UniProtKB:P03355}.
-!- PTM: Capsid protein p30: Sumoylated; which is required for virus
replication. {ECO:0000250|UniProtKB:P03355}.
-!- PTM: RNA-binding phosphoprotein p12: Phosphorylated on serine
residues. {ECO:0000250|UniProtKB:P03355}.
-!- MISCELLANEOUS: Gag-Pol polyprotein: 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 537-Asp and 539-Gly.
{ECO:0000250|UniProtKB:P03355}.
-!- MISCELLANEOUS: Nucleocapsid protein p10-Pol: Nucleocapsid protein
p10-Pol released from Pol polyprotein (NC-pol) is a few amino
acids shorter than the nucleocapsid protein p10 released from Gag
polyprotein (NC-gag). {ECO:0000250|UniProtKB:P03355}.
-!- MISCELLANEOUS: Reverse transcriptase/ribonuclease H: 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. {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
{ECO:0000305}.
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EMBL; K03363; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PIR; B26183; GNMVRV.
ProteinModelPortal; P11227; -.
PRIDE; P11227; -.
OrthoDB; VOG0900018N; -.
Proteomes; UP000007778; Genome.
GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; IEA:InterPro.
CDD; cd06095; RP_RTVL_H_like; 1.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR036946; G_retro_matrix_sf.
InterPro; IPR002079; Gag_p12.
InterPro; IPR003036; Gag_P30.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR034145; RP_RTVL-H-like.
InterPro; IPR000477; RT_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF01141; Gag_p12; 1.
Pfam; PF02093; Gag_p30; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
3: Inferred from homology;
Aspartyl protease; Capsid protein; Coiled coil; Complete proteome;
DNA integration; DNA recombination; DNA-binding;
DNA-directed DNA polymerase; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cell membrane;
Host cytoplasm; Host endosome; Host gene expression shutoff by virus;
Host membrane; Host-virus interaction; Hydrolase; Lipoprotein;
Magnesium; Membrane; Metal-binding; Multifunctional enzyme; Myristate;
Nuclease; Nucleotidyltransferase; Phosphoprotein; Protease;
RNA suppression of termination; RNA-binding;
RNA-directed DNA polymerase; Transferase; Ubl conjugation;
Viral genome integration; Viral matrix protein; Viral nucleoprotein;
Virion; Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 1734 Gag-Pol polyprotein.
/FTId=PRO_0000259739.
CHAIN 2 129 Matrix protein p15.
/FTId=PRO_0000442903.
CHAIN 130 214 RNA-binding phosphoprotein p12.
/FTId=PRO_0000442904.
CHAIN 215 477 Capsid protein p30.
{ECO:0000250|UniProtKB:P03355}.
/FTId=PRO_0000442905.
CHAIN 478 533 Nucleocapsid protein p10-Pol.
/FTId=PRO_0000442906.
CHAIN 534 658 Protease.
/FTId=PRO_0000026134.
CHAIN 659 1329 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000259740.
CHAIN 1330 1734 Integrase.
/FTId=PRO_0000259741.
DOMAIN 560 630 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 740 931 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1173 1319 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1443 1601 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 501 518 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1386 1426 HHCC-type.
{ECO:0000250|UniProtKB:P03355}.
REGION 344 392 Interaction with host PIAS4.
{ECO:0000250|UniProtKB:P03332}.
REGION 429 434 Interaction with host UBE2I.
{ECO:0000250|UniProtKB:P03332}.
COILED 437 477 {ECO:0000255}.
MOTIF 109 112 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P03332}.
MOTIF 128 132 LYPX(n)L motif.
{ECO:0000250|UniProtKB:P03332}.
MOTIF 161 164 PPXY motif.
{ECO:0000250|UniProtKB:P03332}.
COMPBIAS 71 172 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 439 471 Arg-rich. {ECO:0000255|PROSITE-
ProRule:PRU00002}.
ACT_SITE 565 565 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 808 808 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 882 882 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 883 883 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1182 1182 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1220 1220 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1241 1241 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1311 1311 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1454 1454 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1513 1513 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
SITE 129 130 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
SITE 214 215 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
SITE 477 478 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
SITE 533 534 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
SITE 658 659 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
SITE 1329 1330 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03355}.
MOD_RES 191 191 Phosphoserine; by host.
{ECO:0000250|UniProtKB:P03355}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
SEQUENCE 1734 AA; 194217 MW; 3D609ED9858D3120 CRC64;
MGQTVTTPLS LTLEHWGDVQ RIASNQSVEV KKRRRVTFCP AEWPTFDVGW PQDGTFNLDI
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPSWVKPF VSPKLSLSPT APILPSGPST
QPPPRSALYP ALTPSIKPRP SKPQVLSDNG GPLIDLLTED PPPYGEQGPS SPDGDGDREE
ATYTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP
TQLPNEVNSA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP
NESPSAFLER LKEAYRRYTP YDPEDHGQET SVSMSFIWQS APDIGRKLER LEDLKSKTLR
DLVREAEKIF NKRETPEERE ERFRRETEEN EERRRAEDEQ REKERDRRRQ REMSKLLATV
VTGQRQDRQG GERKRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDDQGG
QGQEPPPEPR ITLKVGGQPV TFLVDTGAQH SVLTQNPGPL SDRSAWVQGA TGGKRYRWTT
DRKVHLATGK VTHSFLHVPD CPYPLLGRDL LTKLKAQIHF KGSGAQIVGP MGQPLQVLTL
NIEDEYRLHE ISTEPDVSPG STWLSDFPQA WAETGGMGLA VRQAPLIIPL KATSTPVSIK
QYPMSQEAKL GIKPHIQRLL DQGILVPCQS PWNTPLLPVK KPGTNDYRPV QGLREVNKRV
EDIHPTVPNP YNLLSGLPTS HRWYTVLDLK DAFFCLRLHP TSQPLFASEW RDPGMGISGQ
LTWTRLPQGF KNSPTLFDEA LHRGLADFRI QHPDLILLQY VDDLLLAATS ELDCQQGTRA
LLKTLGNLGY RASAKKAQIC QKQVKYLGYL LREGQRWLTE ARKETVMGQP TPKTPRQLRE
FLGTAGFCRL WIPRFAEMAA PLYPLTKTGT LFNWGPDQQK AYHEIKQALL TAPALGLPDL
TKPFELFVDE KQGYAKGVLT QKLGPWRRPV AYLSKKLDPV AAGWPPCLRM VAAIAVLTKD
AGKLTMGQPL VILAPHAVEA LVKQPPDRWL SNARMTHYQA MLLDTDRVQF GPVVALNPAT
LLPLPEEGAP HDCLEILAET HGTEPDLTDQ PIPDADHTWY TDGSSFLQEG QRKAGAAVTT
ETEVIWARAL PAGTSAQRAE LIALTQALKM AEGKRLNVYT DSRYAFATAH IHGEIYKRRG
LLTSEGREIK NKSEILALLK ALFLPKRLSI IHCLGHQKGD SAEARGNRLA DQAAREAAIK
TPPDTSTLLI EDSTPYTPAY FHYTETDLKK LRELGATYNQ SKGYWVFQGK PVMPDQFVFE
LLDSLHRLTH LGYQKMKALL DRGESPYYML NRDKTLQYVA DSCTVCAQVN ASKAKIGAGV
RVRGHRPGTH WEIDFTEVKP GLYGYKYLLV FVDTFSGWVE AFPTKHETAK IVTKKLLEEI
FPRFGMPQVL GTDNGPAFVS QVSQSVAKLL GIDWKLHCAY RPQSSGQVER MNRTIKETLT
KLTLATGTRD WVLLLPLALY RARNTPGPHG LTPYEILYGA PPPLVNFHDP EMSKFTNSPS
LQAHLQALQA VQREVWKPLA AAYQDQLDQP VIPHPFRVGD TVWVRRHQTK NLEPRWKGPY
TVLLTTPTAL KVDGISAWIH AAHVKAATTP PIRPSWRVQR SQNPLKIRLT RGAP


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