POL_VILV
ID POL_VILV Reviewed; 1506 AA.
AC P03370;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Gag-Pol polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p16;
DE Contains:
DE RecName: Full=Capsid protein p25;
DE Contains:
DE RecName: Full=Nucleocapsid protein p14;
DE Contains:
DE RecName: Full=Protease;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE AltName: Full=Retropepsin;
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 AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE Contains:
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE Short=dUTPase;
DE EC=3.6.1.23 {ECO:0000305};
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000269|PubMed:8189495};
DE EC=3.1.-.- {ECO:0000269|PubMed:8189495};
GN Name=pol;
OS Maedi visna virus (strain 1514) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11742;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2410140; DOI=10.1016/s0092-8674(85)80132-x;
RA Sonigo P., Alizon M., Staskus K., Klatzmann D., Cole S., Danos O.,
RA Retzel E., Tiollais P., Haase A., Wain-Hobson S.;
RT "Nucleotide sequence of the visna lentivirus: relationship to the AIDS
RT virus.";
RL Cell 42:369-382(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2824836; DOI=10.1128/jvi.61.12.4046-4054.1987;
RA Braun M.J., Clements J.E., Gonda M.A.;
RT "The visna virus genome: evidence for a hypervariable site in the env gene
RT and sequence homology among lentivirus envelope proteins.";
RL J. Virol. 61:4046-4054(1987).
RN [3]
RP FUNCTION (INTEGRASE), AND CATALYTIC ACTIVITY (INTEGRASE).
RX PubMed=8189495; DOI=10.1128/jvi.68.6.3558-3569.1994;
RA Katzman M., Sudol M.;
RT "In vitro activities of purified visna virus integrase.";
RL J. Virol. 68:3558-3569(1994).
CC -!- FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the
CC essential events in virion assembly, including binding the plasma
CC membrane, making the protein-protein interactions necessary to create
CC spherical particles, recruiting the viral Env proteins, and packaging
CC the genomic RNA via direct interactions with the RNA packaging
CC sequence. {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Matrix protein p16]: Targets the polyprotein to the plasma
CC membrane. {ECO:0000250|UniProtKB:P12497}.
CC -!- FUNCTION: [Capsid protein p25]: Forms the core that encapsulates the
CC genomic RNA-nucleocapsid complex in the virion.
CC {ECO:0000250|UniProtKB:P04585}.
CC -!- FUNCTION: [Nucleocapsid protein p14]: Encapsulates and protects viral
CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC fingers. Acts as a nucleic acid chaperone which is involved in
CC rearrangement of nucleic acid secondary structure during gRNA
CC retrotranscription. Also facilitates template switch leading to
CC recombination. {ECO:0000250|UniProtKB:P04585}.
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 dimeric RNA genome into
CC dsDNA in the cytoplasm, shortly after virus entry into the cell. This
CC enzyme displays a DNA polymerase activity that can copy either DNA or
CC RNA templates, and a ribonuclease H (RNase H) activity that cleaves the
CC RNA 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-Trp 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 perfom 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 perfom 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 primers. PPT and tRNA primers are then removed by RNase H. The 3' and
CC 5' 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:0000255|PROSITE-
CC ProRule:PRU00405}.
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. {ECO:0000269|PubMed:8189495}.
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=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
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: [Integrase]: Homotetramer; further associates as a
CC homohexadecamer. {ECO:0000250|UniProtKB:P35956}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Gag-Pol polyprotein;
CC IsoId=P03370-1; Sequence=Displayed;
CC Name=Gag polyprotein;
CC IsoId=P03352-1; Sequence=External;
CC -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. {ECO:0000305}.
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 swiching 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.
CC {ECO:0000255|PROSITE-ProRule:PRU00405}.
CC -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by a -1
CC ribosomal frameshifting between gag and pol.
CC {ECO:0000250|UniProtKB:P35956}.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA48354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M10608; AAA17521.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; M51543; AAA48354.1; ALT_SEQ; Genomic_RNA.
DR PIR; A03969; GNLJVS.
DR SMR; P03370; -.
DR MEROPS; A02.006; -.
DR GO; GO:0019028; C:viral capsid; 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:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004533; F:exoribonuclease H 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: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:0009117; P:nucleotide metabolic process; 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 CDD; cd07557; trimeric_dUTPase; 1.
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; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
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; IPR010659; RVT_connect.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_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; PF06815; RVT_connect; 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; SSF51283; SSF51283; 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 Aspartyl protease; Capsid protein; DNA integration; DNA recombination;
KW DNA-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide metabolism;
KW Nucleotidyltransferase; Protease; Repeat; Ribosomal frameshifting;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..1506
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000443358"
FT CHAIN 1..143
FT /note="Matrix protein p16"
FT /id="PRO_0000443359"
FT CHAIN 144..363
FT /note="Capsid protein p25"
FT /id="PRO_0000443360"
FT CHAIN 364..442
FT /note="Nucleocapsid protein p14"
FT /id="PRO_0000443361"
FT CHAIN 443..540
FT /note="Protease"
FT /id="PRO_0000038857"
FT CHAIN 541..1111
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000038858"
FT CHAIN 1112..1225
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000038859"
FT CHAIN 1226..1506
FT /note="Integrase"
FT /id="PRO_0000038860"
FT DOMAIN 459..530
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 587..776
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 971..1093
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1270..1430
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 385..402
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 404..421
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1228..1269
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1447..1499
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT ACT_SITE 464
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; for reverse transcriptase
FT activity"
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; for reverse transcriptase
FT activity"
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; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 980
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1012
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1032
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1085
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RNase H activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 1237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 1291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT BINDING 1379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000305"
FT SITE 363..364
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P35955"
SQ SEQUENCE 1506 AA; 171940 MW; 285DF72886A25EC2 CRC64;
MAKQGSKEKK GYPELKEVIK ATCKIRVGPG KETLTEGNCL WALKTIDFIF EDLKTEPWTI
TKMYTVWDRL KGLTPEETSK REFASLQATL ACIMCSQMGM KPETVQAAKG IISMKEGLHE
NKEAKGEKVE QLYPNLEKHR EVYPIVNLQA GGRSWKAVES VVFQQLQTVA MQHGLVSEDF
ERQLAYYATT WTSKDILEVL AMMPGNRAQK ELIQGKLNEE AERWVRQNPP GPNVLTVDQI
MGVGQTNQQA SQANMDQARQ ICLQWVITAL RSVRHMSHRP GNPMLVKQKN TESYEDFIAR
LLEAIDAEPV TDPIKTYLKV TLSYTNASTD CQKQMDRTLG TRVQQATVEE KMQACRDVGS
EGFKMQLLAQ ALRPQGKAGH KGVNQKCYNC GKPGHLARQC RQGIICHHCG KRGHMQKDCR
QKKQQGKQQE GATCGAVRAP YVVTEAPPKI EIKVGTRWKK LLVDTGADKT IVTSHDMSGI
PKGRIILQGI GGIIEGEKWE QVHLQYKDKM IKGTIVVLAT SPVEVLGRDN MRELGIGLIM
ANLEEKKIPS TRVRLKEGCK GPHIAQWPLT QEKLEGLKEI VDRLEKEGKV GRAPPHWTCN
TPIFCIKKKS GKWRMLIDFR ELNKQTEDLA EAQLGLPHPG GLQRKKHVTI LDIGDAYFTI
PLYEPYRQYT CFTMLSPNNL GPCVRYYWKV LPQGWKLSPA VYQFTMQKIL RGWIEEHPMI
QFGIYMDDIY IGSDLGLEEH RGIVNELASY IAQYGFMLPE DKRQEGYPAK WLGFELHPEK
WKFQKHTLPE ITEGPITLNK LQKLVGDLVW RQSLIGKSIP NILKLMEGDR ALQSERYIES
IHVREWEACR QKLKEMEGNY YDEEKDIYGQ LDWGNKAIEY IVFQEKGKPL WVNVVHSIKN
LSQAQQIIKA AQKLTQEVII RTGKIPWILL PGREEDWILE LQMGNINWMP SFWSCYKGSV
RWKKRNVIAE LVPGPTYYTD GGKKNGRGSL GYIASTGEKF RIHEEGTNQQ LELRAIEEAC
KQGPEKMNIV TDSRYAYEFM LRNWDEEVIR NPIQARIMEL VHNKEKIGVH WVPGHKGIPQ
NEEIDRYISE IFLAKEGRGI LQKRAEDAGY DLICPQEISI PAGQVKRIAI DLKINLKKDQ
WAMIGTKSSF ANKGVFVQGG IIDSGYQGTI QVVIYNSNNK EVVIPQGRKF AQLILMPLIH
EELEPWGETR KTERGEQGFG STGMYWIENI PLAEEEHNKW HQDAVSLHLE FGIPRTAAED
IVQQCDVCQE NKMPSTLRGS NKRGIDHWQV DYTHYEDKII LVWVETNSGL IYAERVKGET
GQEFRVQTMK WYAMFAPKSL QSDNGPAFVA ESTQLLMKYL GIEHTTGIPW NPQSQALVER
THQTLKNTLE KLIPMFNAFE SALAGTLITL NIKRKGGLGT SPMDIFIFNK EQQRIQQQSK
SKQEKIRFCY YRTRKRGHPG EWQGPTQVLW GGDGAIVVKD RGTDRYLVIA NKDVKFIPPP
KEIQKE
