POL_BIV29
ID POL_BIV29 Reviewed; 1475 AA.
AC P19560; P19561; Q65593;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Gag-Pol polyprotein;
DE AltName: Full=Pr170Gag-Pol;
DE Contains:
DE RecName: Full=Matrix protein p16;
DE Short=MA;
DE Contains:
DE RecName: Full=p2L;
DE Contains:
DE RecName: Full=Capsid protein p26;
DE Short=CA;
DE Contains:
DE RecName: Full=p3;
DE Contains:
DE RecName: Full=Transframe peptide;
DE AltName: Full=p11;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.-;
DE AltName: Full=P119;
DE AltName: Full=Retropepsin;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=2.7.7.7;
DE EC=3.1.26.13;
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE AltName: Full=P72;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=gag-pol;
OS Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
OS immunodeficiency-like virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=417296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate R29-106, and Isolate R29-127;
RX PubMed=2183467; DOI=10.1016/0042-6822(90)90424-p;
RA Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
RT "Nucleotide sequence and genome organization of biologically active
RT proviruses of the bovine immunodeficiency-like virus.";
RL Virology 175:391-409(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate R29-Nadin;
RA Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
RT "Isolation and characterization of cDNAs encoding rev and tat of bovine
RT immunodeficiency-like virus.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP RIBOSOMAL FRAMESHIFT, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RC STRAIN=Isolate R29-127;
RX PubMed=1331499; DOI=10.1128/jvi.66.12.6868-6877.1992;
RA Battles J.K., Hu M.Y., Rasmussen L., Tobin G.J., Gonda M.A.;
RT "Immunological characterization of the gag gene products of bovine
RT immunodeficiency virus.";
RL J. Virol. 66:6868-6877(1992).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST DYNLL1.
RX PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
RA Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
RA Chen Q.;
RT "Microtubule-dependent retrograde transport of bovine immunodeficiency
RT virus.";
RL Cell. Microbiol. 12:1098-1107(2010).
CC -!- FUNCTION: Matrix protein p16 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p26 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. Interaction between
CC incoming particle-associated Gag proteins and host dynein allows
CC intracellular microtubule-dependent virus transport toward the
CC perinuclear region, prior to nucleus translocation and integration into
CC host genome. {ECO:0000269|PubMed:20148896}.
CC -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
CC and Gag-Pol polyproteins during or shortly after the release of the
CC virion from the plasma membrane. Cleavages take place as an ordered,
CC step-wise cascade to yield mature proteins. This process is called
CC maturation. Displays maximal activity during the budding process just
CC 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 binds to the primer-binding site (PBS) situated at
CC the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to
CC perform a short round of RNA-dependent minus-strand DNA synthesis. The
CC reading proceeds through the U5 region and ends after the repeated (R)
CC region which is present at both ends of viral RNA. The portion of the
CC RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA
CC product attached to the tRNA primer. This ssDNA/tRNA hybridizes with
CC 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 (By similarity). {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. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA (By
CC similarity). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2;
CC -!- SUBUNIT: Interacts with host light chain cytoplasmic dynein DYNLL1;
CC this interaction is critical for intracellular microtubule-dependent
CC viral genome transport. {ECO:0000269|PubMed:20148896}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p26]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=This strategy of translation probably allows the virus to
CC modulate the quantity of each viral protein.;
CC Name=Gag-Pol polyprotein;
CC IsoId=P19560-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P19558-1; Sequence=External;
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The protease is released by autocatalytic cleavage. The
CC polyprotein is cleaved during and after budding, this process is termed
CC maturation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that
CC lacks a proof-reading function. High mutations rate is a direct
CC consequence of this characteristic. RT also displays frequent template
CC switching leading to high recombination rate. Recombination mostly
CC occurs between homologous regions of the two copackaged RNA genomes. If
CC these two RNA molecules derive from different viral strains, reverse
CC transcription will give rise to highly recombinated proviral DNAs (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting at the gag-pol genes boundary.
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DR EMBL; M32690; AAA91271.1; ALT_SEQ; Genomic_RNA.
DR EMBL; L04972; AAA42767.1; ALT_SEQ; Genomic_DNA.
DR PIR; B34742; GNLJBT.
DR PDB; 3KKR; X-ray; 2.45 A; A=1257-1405.
DR PDB; 3KKS; X-ray; 2.20 A; A/B=1257-1405.
DR PDBsum; 3KKR; -.
DR PDBsum; 3KKS; -.
DR SMR; P19560; -.
DR MEROPS; A02.005; -.
DR EvolutionaryTrace; P19560; -.
DR PRO; PR:P19560; -.
DR GO; GO:0043657; C:host cell; IEA:GOC.
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-KW.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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; 1.10.10.200; -; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
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; 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; IPR010661; RVT_thumb.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 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; PF06817; RVT_thumb; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
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; 2.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; Coiled coil;
KW Cytoplasmic inwards viral transport; DNA integration; DNA recombination;
KW DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Host-virus interaction; Hydrolase; Magnesium; Metal-binding;
KW Microtubular inwards viral transport; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Protease; Repeat; Ribosomal frameshifting;
KW RNA-binding; RNA-directed DNA polymerase; Transferase;
KW Viral genome integration; Viral matrix protein; Viral nucleoprotein;
KW Viral release from host cell; Virion; Virion maturation;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..1475
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000272324"
FT CHAIN 1..126
FT /note="Matrix protein p16"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272325"
FT PEPTIDE 127..148
FT /note="p2L"
FT /evidence="ECO:0000250"
FT /id="PRO_0000272326"
FT CHAIN 149..367
FT /note="Capsid protein p26"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272327"
FT PEPTIDE 368..392
FT /note="p3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000272328"
FT CHAIN 393..472
FT /note="Transframe peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272329"
FT CHAIN 473..562
FT /note="Protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038823"
FT CHAIN 563..1193
FT /note="Reverse transcriptase/ribonuclease H"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038824"
FT CHAIN 1194..1475
FT /note="Integrase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038825"
FT DOMAIN 492..565
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 619..806
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 999..1119
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1248..1400
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 403..420
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 421..438
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1199..1240
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1419..1465
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT REGION 130..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 1208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT SITE 126..127
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 148..149
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 367..368
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 392..393
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 472..473
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 562..563
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 1193..1194
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT VARIANT 17
FT /note="P -> L (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 117
FT /note="D -> E (in strain: Isolate R29-106)"
FT VARIANT 454
FT /note="T -> I (in strain: Isolate R29-Nadin)"
FT VARIANT 577
FT /note="V -> I (in strain: Isolate R29-Nadin)"
FT VARIANT 645
FT /note="R -> K (in strain: Isolate R29-Nadin)"
FT VARIANT 729
FT /note="V -> I (in strain: Isolate R29-Nadin)"
FT VARIANT 1095
FT /note="V -> I (in strain: Isolate R29-Nadin)"
FT VARIANT 1226
FT /note="K -> R (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 1244
FT /note="T -> A (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT STRAND 1257..1265
FT /evidence="ECO:0007829|PDB:3KKS"
FT STRAND 1268..1275
FT /evidence="ECO:0007829|PDB:3KKS"
FT TURN 1276..1278
FT /evidence="ECO:0007829|PDB:3KKS"
FT STRAND 1281..1289
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1291..1304
FT /evidence="ECO:0007829|PDB:3KKS"
FT STRAND 1308..1312
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1316..1319
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1321..1329
FT /evidence="ECO:0007829|PDB:3KKS"
FT STRAND 1333..1338
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1342..1362
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1363..1365
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1369..1382
FT /evidence="ECO:0007829|PDB:3KKS"
FT HELIX 1392..1401
FT /evidence="ECO:0007829|PDB:3KKS"
SQ SEQUENCE 1475 AA; 168063 MW; 4D249DCBB6158A78 CRC64;
MKRRELEKKL RKVRVTPQQD KYYTIGNLQW AIRMINLMGI KCVCDEECSA AEVALIITQF
SALDLENSPI RGKEEVAIKN TLKVFWSLLA GYKPESTETA LGYWEAFTYR EREARADKEG
EIKSIYPSLT QNTQNKKQTS NQTNTQSLPA ITTQDGTPRF DPDLMKQLKI WSDATERNGV
DLHAVNILGV ITANLVQEEI KLLLNSTPKW RLDVQLIESK VREKENAHRT WKQHHPEAPK
TDEIIGKGLS SAEQATLISV ECRETFRQWV LQAAMEVAQA KHATPGPINI HQGPKEPYTD
FINRLVAALE GMAAPETTKE YLLQHLSIDH ANEDCQSILR PLGPNTPMEK KLEACRVVGS
QKSKMQFLVA AMKEMGIQSP IPAVLPHTPE AYASQTSGPE DGRRCYGCGK TGHLKRNCKQ
QKCYHCGKPG HQARNCRSKN REVLLCPLWA EEPTTEQFSP EQHEFCDPIC TPSYIRLDKQ
PFIKVFIGGR WVKGLVDTGA DEVVLKNIHW DRIKGYPGTP IKQIGVNGVN VAKRKTHVEW
RFKDKTGIID VLFSDTPVNL FGRSLLRSIV TCFTLLVHTE KIEPLPVKVR GPGPKVPQWP
LTKEKYQALK EIVKDLLAEG KISEAAWDNP YNTPVFVIKK KGTGRWRMLM DFRELNKITV
KGQEFSTGLP YPPGIKECEH LTAIDIKDAY FTIPLHEDFR PFTAFSVVPV NREGPIERFQ
WNVLPQGWVC SPAIYQTTTQ KIIENIKKSH PDVMLYQYMD DLLIGSNRDD HKQIVQEIRD
KLGSYGFKTP DEKVQEERVK WIGFELTPKK WRFQPRQLKI KNPLTVNELQ QLVGNCVWVQ
PEVKIPLYPL TDLLRDKTNL QEKIQLTPEA IKCVEEFNLK LKDPEWKDRI REGAELVIKI
QMVPRGIVFD LLQDGNPIWG GVKGLNYDHS NKIKKILRTM NELNRTVVIM TGREASFLLP
GSSEDWEAAL QKEESLTQIF PVKFYRHSCR WTSICGPVRE NLTTYYTDGG KKGKTAAAVY
WCEGRTKSKV FPGTNQQAEL KAICMALLDG PPKMNIITDS RYAYEGMREE PETWAREGIW
LEIAKILPFK QYVGVGWVPA HKGIGGNTEA DEGVKKALEQ MAPCSPPEAI LLKPGEKQNL
ETGIYMQGLR PQSFLPRADL PVAITGTMVD SELQLQLLNI GTEHIRIQKD EVFMTCFLEN
IPSATEDHER WHTSPDILVR QFHLPKRIAK EIVARCQECK RTTTSPVRGT NPRGRFLWQM
DNTHWNKTII WVAVETNSGL VEAQVIPEET ALQVALCILQ LIQRYTVLHL HSDNGPCFTA
HRIENLCKYL GITKTTGIPY NPQSQGVVER AHRDLKDRLA AYQGDCETVE AALSLALVSL
NKKRGGIGGH TPYEIYLESE HTKYQDQLEQ QFSKQKIEKW CYVRNRRKEW KGPYKVLWDG
DGAAVIEEEG KTALYPHRHM RFIPPPDSDI QDGSS
