ID   POL_BLVJ                Reviewed;        1416 AA.
AC   P03361;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 2.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Gag-Pro-Pol polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=Capsid protein p24;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p12-pro;
DE   Contains:
DE     RecName: Full=Protease;
DE              EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H;
DE              Short=RT;
DE              EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
DE   Contains:
DE     RecName: Full=Integrase;
DE              Short=IN;
DE              EC=2.7.7.- {ECO:0000250|UniProtKB:P03363};
DE              EC=3.1.-.- {ECO:0000250|UniProtKB:P03363};
GN   Name=pol;
OS   Bovine leukemia virus (isolate Japanese BLV-1) (BLV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus;
OC   Deltaretrovirus bovleu; Bovine leukemia virus.
OX   NCBI_TaxID=11907;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2983308; DOI=10.1073/pnas.82.3.677;
RA   Sagata N., Yasunaga T., Tsuzuku-Kawamura J., Ohishi K., Ogawa Y., Ikawa Y.;
RT   "Complete nucleotide sequence of the genome of bovine leukemia virus: its
RT   evolutionary relationship to other retroviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:677-681(1985).
CC   -!- FUNCTION: Gag-Pro polyprotein: The matrix domain targets Gag, Gag-Pro
CC       and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite
CC       membrane binding signal, that includes its myristoylated N-terminus.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Matrix protein p15]: Matrix protein.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus
CC       that encapsulates the genomic RNA-nucleocapsid complex.
CC       {ECO:0000250|UniProtKB:P03362}.
CC   -!- FUNCTION: [Nucleocapsid protein p12-pro]: Binds strongly to viral
CC       nucleic acids and promote their aggregation. Also destabilizes the
CC       nucleic acids duplexes via highly structured zinc-binding motifs.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC       cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC       release of the virion from the plasma membrane. Cleavages take place as
CC       an ordered, step-wise cascade to yield mature proteins. This process is
CC       called maturation. Displays maximal activity during the budding process
CC       just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC       ProRule:PRU00275}.
CC   -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a
CC       multifunctional enzyme that converts the viral RNA genome into dsDNA in
CC       the cytoplasm, shortly after virus entry into the cell. This enzyme
CC       displays a DNA polymerase activity that can copy either DNA or RNA
CC       templates, and a ribonuclease H (RNase H) activity that cleaves the RNA
CC       strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'-
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires
CC       many steps. A tRNA-Pro binds to the primer-binding site (PBS) situated
CC       at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer
CC       to perform a short round of RNA-dependent minus-strand DNA synthesis.
CC       The reading proceeds through the U5 region and ends after the repeated
CC       (R) region which is present at both ends of viral RNA. The portion of
CC       the RNA-DNA heteroduplex is digested by the RNase H, resulting in a
CC       ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes
CC       with the identical R region situated at the 3' end of viral RNA. This
CC       template exchange, known as minus-strand DNA strong stop transfer, can
CC       be either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthesized short ssDNA to perform the RNA-dependent minus-strand DNA
CC       synthesis of the whole template. RNase H digests the RNA template
CC       except for a polypurine tract (PPT) situated at the 5' end of the
CC       genome. It is not clear if both polymerase and RNase H activities are
CC       simultaneous. RNase H probably can proceed both in a polymerase-
CC       dependent (RNA cut into small fragments by the same RT performing DNA
CC       synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC       fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC       DNA synthesis using the PPT that has not been removed by RNase H as
CC       primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5'
CC       ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC       Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC       blunt ended, linear dsDNA copy of the viral genome that includes long
CC       terminal repeats (LTRs) at both ends. {ECO:0000250}.
CC   -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC       chromosome, by performing a series of DNA cutting and joining
CC       reactions. {ECO:0000250|UniProtKB:P03362}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC       Note=The RT polymerase active site binds 2 magnesium ions.
CC       {ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- SUBUNIT: [Gag-Pro-Pol polyprotein]: Homodimer; the homodimers are part
CC       of the immature particles. Interacts with human TSG101 and NEDD4; these
CC       interactions are essential for budding and release of viral particles.
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBUNIT: [Matrix protein p15]: Homodimer; further assembles as
CC       homohexamers. {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion
CC       {ECO:0000250|UniProtKB:P03345}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=3;
CC       Name=Gag-Pro-Pol polyprotein;
CC         IsoId=P03361-1; Sequence=Displayed;
CC       Name=Gag polyprotein;
CC         IsoId=P03344-1; Sequence=External;
CC       Name=Gag-Pro polyprotein;
CC         IsoId=P0DOI0-1; Sequence=External;
CC   -!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are short
CC       sequence motifs essential for viral particle release. They can occur
CC       individually or in close proximity within structural proteins. They
CC       interacts with sorting cellular proteins of the multivesicular body
CC       (MVB) pathway. Most of these proteins are class E vacuolar protein
CC       sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC       Matrix protein p15 contains one L domain: a PPXY motif which binds to
CC       the WW domains of the ubiquitin ligase NEDD4.
CC       {ECO:0000250|UniProtKB:P25059}.
CC   -!- PTM: [Matrix protein p15]: Phosphorylation of the matrix protein p15 by
CC       MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.
CC   -!- PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the
CC       matrix (MA) domain mediates the transport and binding of Gag
CC       polyproteins to the host plasma membrane and is required for the
CC       assembly of viral particles. {ECO:0000250|UniProtKB:P03345}.
CC   -!- PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages by the
CC       viral protease yield mature proteins. The polyprotein is cleaved during
CC       and after budding, this process is termed maturation. The protease is
CC       autoproteolytically processed at its N- and C-termini.
CC       {ECO:0000250|UniProtKB:P03362}.
CC   -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: The reverse
CC       transcriptase is an error-prone enzyme that lacks a proof-reading
CC       function. High mutations rate is a direct consequence of this
CC       characteristic. RT also displays frequent template switching leading to
CC       high recombination rate. Recombination mostly occurs between homologous
CC       regions of the two copackaged RNA genomes. If these two RNA molecules
CC       derive from different viral strains, reverse transcription will give
CC       rise to highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
CC       ProRule:PRU00405}.
CC   -!- MISCELLANEOUS: [Isoform Gag-Pro-Pol polyprotein]: Produced by -1
CC       ribosomal frameshiftings between gag-pro and pro-pol. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; K02120; AAA42785.1; ALT_SEQ; Genomic_RNA.
DR   PIR; A03960; GNLJGB.
DR   SMR; P03361; -.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   FunFam; 4.10.60.10:FF:000119; Gag polyprotein; 1.
DR   FunFam; 1.10.375.10:FF:000005; Gag-pro-pol polyprotein; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR003139; D_retro_matrix.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR001037; Integrase_C_retrovir.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR018061; Retropepsins.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF02228; Gag_p19; 1.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF00552; IN_DBD_C; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51027; INTEGRASE_DBD; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Capsid protein; DNA integration; DNA recombination; DNA-binding;
KW   Endonuclease; Host-virus interaction; Hydrolase; Lipoprotein; Magnesium;
KW   Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW   Nucleotidyltransferase; Phosphoprotein; Repeat; Ribosomal frameshifting;
KW   RNA-directed DNA polymerase; Transferase; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral genome integration;
KW   Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW   Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..1416
FT                   /note="Gag-Pro-Pol polyprotein"
FT                   /id="PRO_0000125482"
FT   CHAIN           2..109
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000442558"
FT   CHAIN           110..321
FT                   /note="Capsid protein p24"
FT                   /id="PRO_0000442559"
FT   CHAIN           322..419
FT                   /note="Nucleocapsid protein p12-pro"
FT                   /id="PRO_0000442560"
FT   CHAIN           420..545
FT                   /note="Protease"
FT                   /id="PRO_0000442561"
FT   CHAIN           546..1120
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000442562"
FT   CHAIN           1121..1416
FT                   /note="Integrase"
FT                   /id="PRO_0000442563"
FT   DOMAIN          447..525
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          586..776
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          996..1126
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          1179..1343
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         345..362
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         370..387
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   DNA_BIND        1352..1400
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT   MOTIF           100..103
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P25059"
FT   ACT_SITE        452
FT                   /note="Protease; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   BINDING         652
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         727
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         728
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         1005
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1036
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1057
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   BINDING         1247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   SITE            109..110
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   SITE            322..323
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   SITE            419..420
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   SITE            544..545
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   SITE            1120..1121
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03345"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1416 AA;  156397 MW;  4840617B29D4A098 CRC64;
     MGNSPSYNPP AGISPSDWLN LLQSAQRLNP RPSPSDFTDL KNYIHWFHKT QKKPWTFTSG
     GPTSCPPGRF GRVPLVLATL NEVLSNEGGA PGASAPEEQP PPYDPPAILP IISEGNRNRH
     RAWALRELQD IKKEIENKAP GSQVWIQTLR LAILQADPTP ADLEQLCQYI ASPVDQTAHM
     TSLTAAIAAA EAANTLQGFN PKTGTLTQQS AQPNAGDLRS QYQNLWLQAG KNLPTRPSAP
     WSTIVQGPAE SSVEFVNRLQ ISLADNLPDG VPKEPIIDSL SYANANRECQ QILQGRGPVA
     AVGQKLQACA QWAPKNKQPA LLVHTPGPKM PGPRQPAPKR PPPGPCYRCL KEGHWARDCP
     TKATGPPPGP CPICKDPSHW KRDCPTLKSK NKLIEGGLSA PQTITPITDS LSEAELECLL
     SIPLARSRPS VAVYLSGPWL QPSQNQALML VDTGAENTVL PQNWLVRDYP RIPAAVLGAG
     GVSRNRYNWL QGPLTLALKP EGPFITIPKI LVDTSDKWQI LGRDVPSRLQ ASISIPEEVR
     PPVVGVLDTP PSHIGLEHLP PPPEVPQFPL NLERLQALQD LVHRSLEAGY ISPWDGPGNN
     PVFPVRKPNG AWRFVHDLRA TNALTKPIPA LSPGPPDLTA IPTHPPHIIC LDLKDAFFQI
     PVEDRFRFYL SFTLPSPGGL QPHRRFAWRV LPQGFINSPA LFERALQEPL RQVSAAFSQS
     LLVSYMDDIL YASPTEEQRS QCYQALAARL RDLGFQVASE KTSQTPSPVP FLGQMVHEQI
     VTYQSLPTLQ ISSPISLHQL QAVLGDLQWV SRGTPTTRRP LQLLYSSLKR HHDPRAIIQL
     SPEQLQGIAE LRQALSHNAR SRYNEQEPLL AYVHLTRAGS TLVLFQKGAQ FPLAYFQTPL
     TDNQASPWGL LLLLGCQYLQ TQALSSYAKP ILKYYHNLPK TSLDNWIQSS EDPRVQELLQ
     LWPQISSQGI QPPGPWKTLI TRAEVFLTPQ FSPDPIPAAL CLFSDGATGR GAYCLWKDHL
     LDFQAVPAPE SAQKGELAGL LAGLAAAPPE PVNIWVDSKY LYSLLRTLVL GAWLQPDPVP
     SYALLYKSLL RHPAIVVGHV RSHSSASHPI ASLNNYVDQL LPLETPEQWH KLTHCNSRAL
     SRWPNPRISA WDPRSPATLC ETCQKLNPTG GGKMRTIQRG WAPNHIWQAD ITHYKYKQFT
     YALHVFVDTY SGATHASAKR GLTTQTTIEG LLEAIVHLGR PKKLNTDQGA NYTSKTFVRF
     CQQFGVSLSH HVPYNPTSSG LDERTNGLLK LLLSKYHLDE PHLPMTQALS RALWTHNQIN
     LLPILKTRWE LHHSPPLAVI SEGGETPKGS DKLFLYLLPG QNNRRWLGPL PALVEASGGA
     LLATDPPVWV PWRLLKAFKC LKNDGPEDAH NRSSDG
//