POL_BLVAU
ID POL_BLVAU Reviewed; 1416 AA.
AC P25059;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 106.
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 Australian) (BLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus.
OX NCBI_TaxID=11903;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167927; DOI=10.1099/0022-1317-71-8-1737;
RA Coulston J., Naif H., Brandon R., Kumar S., Khan S., Daniel R.C.W.,
RA Lavin M.F.;
RT "Molecular cloning and sequencing of an Australian isolate of proviral
RT bovine leukaemia virus DNA: comparison with other isolates.";
RL J. Gen. Virol. 71:1737-1746(1990).
RN [2]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=6094258; DOI=10.1016/0014-5793(84)81244-2;
RA Sagata N., Yasunaga T., Ikawa Y.;
RT "Identification of a potential protease-coding gene in the genomes of
RT bovine leukemia and human T-cell leukemia viruses.";
RL FEBS Lett. 178:79-82(1984).
RN [3]
RP DOMAIN LATE-BUDDING, AND MUTAGENESIS OF 100-PRO--TYR-103.
RX PubMed=12134053; DOI=10.1128/jvi.76.16.8485-8493.2002;
RA Wang H., Norris K.M., Mansky L.M.;
RT "Analysis of bovine leukemia virus gag membrane targeting and late domain
RT function.";
RL J. Virol. 76:8485-8493(2002).
CC -!- FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag,
CC Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
CC multipartite membrane binding signal, that includes its myristoylated
CC N-terminus. {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=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-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=P25059-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P25058-1; Sequence=External;
CC Name=Gag-Pro polyprotein;
CC IsoId=P0DOI1-1; Sequence=External;
CC -!- DOMAIN: [Gag-Pro-Pol polyprotein]: Late-budding domains (L domains) are
CC short sequence motifs essential for viral particle release. They can
CC occur individually or in close proximity within structural proteins.
CC They interacts with sorting cellular proteins of the multivesicular
CC body (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:0000269|PubMed:12134053}.
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 swiching 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.
CC {ECO:0000269|PubMed:6094258}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00544.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D00647; BAA00544.1; ALT_SEQ; Genomic_DNA.
DR PIR; JQ0555; GNLJGA.
DR SMR; P25059; -.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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:InterPro.
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:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR003139; D_retro_matrix.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
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 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; 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; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 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 1: Evidence at protein level;
KW Aspartyl protease; Capsid protein; DNA integration; DNA recombination;
KW DNA-binding; Endonuclease; Host-virus interaction; Hydrolase; Lipoprotein;
KW Magnesium; Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW Nucleotidyltransferase; Phosphoprotein; Protease; Repeat;
KW Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral genome integration; Viral matrix protein; Viral nucleoprotein;
KW Viral release from host cell; Virion; Virus entry into host cell; Zinc;
KW 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_0000125481"
FT CHAIN 2..109
FT /note="Matrix protein p15"
FT /id="PRO_0000442552"
FT CHAIN 110..323
FT /note="Capsid protein p24"
FT /id="PRO_0000442553"
FT CHAIN 324..419
FT /note="Nucleocapsid protein p12-pro"
FT /id="PRO_0000442554"
FT CHAIN 420..545
FT /note="Protease"
FT /id="PRO_0000442555"
FT CHAIN 546..1120
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000442556"
FT CHAIN 1121..1416
FT /note="Integrase"
FT /id="PRO_0000442557"
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:0000269|PubMed:12134053"
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 323..324
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"
FT MUTAGEN 100..103
FT /note="PPPY->AAAA: Greatly reduced release of new viral
FT particles."
FT /evidence="ECO:0000269|PubMed:12134053"
SQ SEQUENCE 1416 AA; 156937 MW; 43542CE5D408581A CRC64;
MGNSPSYNPP AGISPSDWLN LLQSAQRLNP RPSPSDFTDL KNYIHWFHKT QKKPWTFTSG
GPASCPPGKF GRVPLVLATL NEVLSNDEGA PGASAPEEQP PPYDPPAVLP IISEGNRNRH
RAWALRELQD IKKEIENKAP GSQVWIQTLR LAILQADPTP ADLEQLCQYI ASPVDQTAHM
TSLTAAIAAE AANTLQGFNP QNGTLTQQSA QPNAGDLRSQ YQNLWLQAWK NLPTRPSVQP
WSTIVQGPAE SYVEFVNRLQ ISLADNLPDG VPKEPIIDSL SYANANKECQ QILQGRGLVA
APVGQKLQAC AHWAPKTKQP AILVHTPGPK MPGPRQPAPK RPPPGPCYRC LKEGHWARDC
PTKTTGPPPG PCPICKDPSH WKRDCPTLKS KKLIEGGPSA PQIITPITDS LSEAELECLL
SIPLARSRPS VAVYLSGPWL QPSQNQALML VDTGAENTVL PQNWLVRDYP RTPAAVLGAG
GISRNRYNWL QGPLTLALKP EGPFITIPKI LVDTFDKWQI LGRDVLSRLQ ASISIPEEVH
PPVVGVLDAP PSHIGLEHLP PPPEVPQFPL NLERLQALQD LVHRSLEAGY ISPWDGPGNN
PVFPVRKPNG AWRFVHDLRV TNALTKPIPA LSPGPPDLTA IPTHLPHIIC LDLKDAFFQI
PVEDRFRSYF AFTLPTPGGL QPHRRFAWRV LPQGFINSPA LFERALQEPL RQVSAAFSQS
LLVSYMDDIL YVSPTEEQRL QCYQTMAAHL RDLGFQVASE KTRQTPSPVP FLGQMVHERM
VTYQSLPTLQ ISSPISLHQL QTVLGDLQWV SRGTPTTRRP LQLLYSSLKG IDDPRAIIHL
SPEQQQGIAE LRQALSHNAR SRYNEQEPLL AYVHLTRAGS TLVLFQKGAQ FPLAYFQTPL
TDNQASPWGL LLLLGCQYLQ AQALSSYAKT ILKYYHNLPK TSLDNWIQSS EDPRVQELLQ
LWPQISSQGI QPPGPWKTLV TRAEVFLTPQ FSPEPIPAAL CLFSDGAARR GAYCLWKDHL
LDFQAVPAPE SAQKGELAGL LAGLAAAPPE PLNIWVDSKY LYSLLRTLVL GAWLQPDPVP
SYALLYKSLL RHPAIFVGHV RSHSSASHPI ASLNNYVDQL LPLETPEQWH KLTHCNSRAL
SRWPNPRISA WDPRSPATLC ETCQRLNPTG GGKMRTIQRG WAPNHIWQAD ITHYKYKQFT
YALHVFVDTY SGATHASAKR GLTTQTTIEG LLEAIVHLGR PKKLNTDQGA NYTSKTFVRF
CQQFGISLSH HVPYNPTSSG LVERTNGLLK LLLSKYHLDE PHLPMTQALS RALWTHNQIN
LLPILKTRWE LHHSPPLAVI SEGGETPKGS DKLFLYKLPG QNNRRWLGPL PALVEASGGA
LLATNPPVWV PWRLLKAFKC LKNDGPEDAP NRSSDG
