GenomeNet

Database: UniProt
Entry: B1PVV8_9FLAV
LinkDB: B1PVV8_9FLAV
Original site: B1PVV8_9FLAV 
ID   B1PVV8_9FLAV            Unreviewed;      3898 AA.
AC   B1PVV8;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS   Classical swine fever virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Pestivirus; Pestivirus suis.
OX   NCBI_TaxID=11096 {ECO:0000313|EMBL:ACA60749.1, ECO:0000313|Proteomes:UP000099917};
RN   [1] {ECO:0000313|EMBL:ACA60749.1, ECO:0000313|Proteomes:UP000099917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL1 {ECO:0000313|EMBL:ACA60749.1};
RA   Qiu H.-J., Jin M.-L., Chen D., Sun Y.;
RT   "Isolation and characterization of Classical swine fever virus strain
RT   JL1(06).";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a cofactor for the NS3 protease activity.
CC       {ECO:0000256|ARBA:ARBA00023576}.
CC   -!- FUNCTION: Packages viral RNA to form a viral nucleocapsid and thereby
CC       protects viral RNA. Also plays a role in transcription regulation.
CC       Protects the incoming virus against IFN-induced effectors.
CC       {ECO:0000256|ARBA:ARBA00034097}.
CC   -!- FUNCTION: Plays a role in the regulation of viral RNA replication.
CC       {ECO:0000256|ARBA:ARBA00023574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC         Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC         whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC         and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC         Evidence={ECO:0000256|ARBA:ARBA00001160};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001491};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004650}.
CC   -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00010133}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU497410; ACA60749.1; -; Genomic_RNA.
DR   IntAct; B1PVV8; 2.
DR   MEROPS; S31.001; -.
DR   Proteomes; UP000099917; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd17931; DEXHc_viral_Ns3; 1.
DR   CDD; cd23201; Pestivirus_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.60.40.4200; Pestivirus envelope glycoprotein E2, C-terminal domain; 1.
DR   Gene3D; 2.60.320.20; Pestivirus envelope glycoprotein E2, domain A; 1.
DR   Gene3D; 2.60.40.3000; Pestivirus envelope glycoprotein E2, domain B; 1.
DR   Gene3D; 2.30.140.40; Pestivirus Npro endopeptidase C53, interaction domain; 1.
DR   Gene3D; 3.90.730.10; Ribonuclease T2-like; 1.
DR   InterPro; IPR021824; Capsid-C_pestivirus.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR011492; Flavi_DEAD.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR022120; NS2.
DR   InterPro; IPR030399; NS2_C74.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008751; Peptidase_C53.
DR   InterPro; IPR042542; Peptidase_C53_interaction.
DR   InterPro; IPR032521; Pestivirus_E2.
DR   InterPro; IPR042309; Pestivirus_E2_A.
DR   InterPro; IPR042310; Pestivirus_E2_B.
DR   InterPro; IPR042311; Pestivirus_E2_D.
DR   InterPro; IPR000280; Pestivirus_NS3_S31.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF11889; Capsid_pestivir; 1.
DR   Pfam; PF20907; Flav_NS3-hel_C; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF05550; Peptidase_C53; 1.
DR   Pfam; PF12387; Peptidase_C74; 1.
DR   Pfam; PF05578; Peptidase_S31; 1.
DR   Pfam; PF16329; Pestivirus_E2; 1.
DR   Pfam; PF00998; RdRP_3; 1.
DR   PRINTS; PR00729; CDVENDOPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR   PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51876; PV_NPRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|ARBA:ARBA00022506};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00868};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|PROSITE-ProRule:PRU01224};
KW   Inhibition of host IRF3 by virus {ECO:0000256|ARBA:ARBA00022931,
KW   ECO:0000256|PROSITE-ProRule:PRU01224};
KW   Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482,
KW   ECO:0000256|PROSITE-ProRule:PRU01224};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00868};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00868};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU01224}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW   Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   TRANSMEM        1031..1055
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1076..1095
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1115..1133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1145..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1189..1208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1220..1238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1250..1271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1283..1304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..168
FT                   /note="Peptidase C53"
FT                   /evidence="ECO:0000259|PROSITE:PS51876"
FT   DOMAIN          1441..1589
FT                   /note="Peptidase C74"
FT                   /evidence="ECO:0000259|PROSITE:PS51692"
FT   DOMAIN          1590..1763
FT                   /note="Peptidase S31"
FT                   /evidence="ECO:0000259|PROSITE:PS51535"
FT   DOMAIN          1802..1960
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1978..2179
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          3519..3642
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          170..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        49
FT                   /note="For N-terminal protease activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
FT   ACT_SITE        69
FT                   /note="For N-terminal protease activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
FT   ACT_SITE        1658
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1695
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1752
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT   SITE            168..169
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
SQ   SEQUENCE   3898 AA;  437893 MW;  09E540B043FEDCA3 CRC64;
     MELNHFELLY KTNKQKPMGV EEPVYDVTGR PLFGDPSEVH PQSTLKLPHD RGRGNIKTTL
     NNLPRKGDCR SGNHLGPVSG IYVKPGPVFY QDYMGPVYHR APLEFFNETQ FCEVTKRIGR
     VTGSDGKLYH MYVCIDGCIL LKLAKRGEPR TLKWIRNFTD CPLWVTSCSD DGASGSKEKK
     PDRINKGKLK IAPKEHEKDS RTKPPDATIV VEGVKYQVKK KGKVKGKNTQ DGLYHNKNKP
     PESRKKLEKA LLAWAVITIM LYQPVEAENI TQWNLSDNGT NGIQHAMYLR GVSRSLHGIW
     PEKICKGVPT YLATDTELKE IQGMMDASEG TNYTCCKLQR HEWNKHGWCN WYNIDPWVQL
     MNRTQANLAE GPPAKECAVT CRYDKDADIN VVTQARNRPT TLTGCKKGKN FSFAGTIIEG
     PCNFNVSVED ILYGDHECGS LLQDTALYLV DGMTNTIENA RQGAARVTSW LGRQLSTAGK
     RLEGRSKTWF GAYALSPYCN VTSKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
     LHEMGGHLSE FLLLSLVVLS DFAPETASAL YLILHYVIPQ SYEEPEGCDT NQLNLTVELR
     TEDVIPSSVW NVGKYVCVRP DWWPYETKVA LLFEEAGQVV KLALRALRDL TRVWNSASTT
     AFLICLIKVL RGQIVQGVIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAGGLTTTWK
     EYSHDLQLND GTVKAICVAG SFKVTALNVV SRRYLASLHK GALLTSVTFE LLFDGTNPST
     EEMGDDFGFG LCPFDTSPVV KGKYNTTLLN GSAFYLVCPI GWTGVIECTA VSPTTLRTEV
     VKTFRREKPF PHRMDCVTTT VENEDLFYCK LGGNWTCVKG EPVVYTGGQV KQCKWCGFDF
     NEPDGLPHYP IGKCILANET GYRIVDSTDC NRDGVVISAE GSHECLIGNT TVKVHASDER
     LGPMPCRPKE IVSSAGPVRK TSCTFNYAKT LKNKYYEPRD SYFQQYMLKG EYQYWFDLDV
     TDRHSDYFAE FVVLVVVALL GGRYVLWLIV TYIVLTEQLA AGLPLGQGEV VLIGNLITHT
     DIEVVVYFLL LYLVMRDEPI KKWILLLFHA MTNNPVKTIT VALLMVSGVA KGGKIDGGWQ
     RLPETSFDIQ LALTVIVVAV MLLAKRDPTT VPLVITVATL RTAKMTNGLS TDIAIATVST
     ALLTWTYISD YYRYKTWLQY LISTVTGIFL IRVLKGIGEL DLHTPTLPSY RPLFFILVYL
     ISTAVVTRWN LDIAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
     RGWLWKTNFK RVNDIYEVDQ AGEGVYLFPS KQKTSSITGT MLPLIKAILI SCISNKWQFI
     YLLYLIFEVS YYLHKKIIDE IAGGTNFISR LVAALIEANW AFDNEEVRGL KKFFLLSSRV
     KELIIKHKVR NEVMVHWFGD EEVYGMPKLV GLVKAATLSK NKHCILCTVC EDREWKGETC
     PKCGRFGPPM TCGMTLADFE EKHYKRIFFR EDQSEGPVRE EYAGYLQYRA RGQLFLRNLP
     VLATKVKMLL VGNLGTEVGD LEHLGWVLRG PAVCKKVTEH EKCTTSIMDK LTAFFGVMPR
     GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
     NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
     AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK STTDLTEMVK
     KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
     PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSFIFLD EYHCATPEQL
     AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK
     IPVEEMKSNM LVFVPTRNMA VETAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
     NAIESGVTLP DLDVVVDTGL KCEKRIRLSS KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
     PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
     ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDSYDNYTF
     LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
     VALFGYVGYQ ALSKRHIPVV TDIYSIEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
     VQRCVEAMTN YAREGIQFMK SQALKVKETP TYKETMDTVT DYVKKFMEAL KDSKEDIMKY
     GLWGTHTALY KSISARLGSE TAFATLVVKW LAFGGESIAD HVKQAATDLV VYYIINRPQF
     PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA TALKLFAPTR
     LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
     AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEALQTVGN PLRLVYHLYG
     VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDSIK
     SSVREMAISW APAPFSCDWT PTDNRIGLPQ DNFLQVETKC PCGYKMKAVK NCAGELRLLE
     EEGSFLCRNK FGRGSRNYKV TKYYDDNLSE IKPVIKMEGH VELYYKGATI KLDFNNSKTI
     LATDKWEVDH STLVRVLKRH TGAGYNGAYL GEKPNHKHLI ERDCATITKD KVCFLKMKRG
     CAFTYDLSLH NLTRLIELVH KNNLEDKEIP AVTVTTWLAY TFVNEDIGTI RPAFGEKVTP
     EMQEEITLQP AVVVDTTDVT VTVVGEAPTM TTGETPTAFT SSGSDPKGQQ VLKLGVGEGQ
     YPGTNPQRAS LHEAIQGADE RPSVLILGSD KATSNRVKTA KNVKVYRGRD PLEVRDMMRR
     GKILVIALSR VDNALLKFVD YKGTFLTRET LEALSLGRPK KKDITKAEAQ WLLCLEDQME
     ELPDWFAAGE PIFLEANIKH DRYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
     SNWVMQEENK QGNLTPLFEE LLQQCPPGGQ NKTAHMVSAY QLAQGNWMPT SCHVFMGTIS
     ARRIKTHPYE AYVKLRELVE EHKMKTLCPG SSLGKHNDWI IGKIKYQGNL RTKHMLNPGK
     VAEQLCREGH RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
     TPGLHKKLME VFNALKRPEL ESSYDAVEWE ELERGINRKG AAGFFERKNI GEILDSEKNK
     VEEIIDNLKK GRNIKYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
     VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTKDLEL
     IKDIQKYYFK KKWHKFIDTL TMHMTEVPVI CADGEVYIRK GQRGSGQPDT SAGNSMLNVL
     TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
     EGDKMKVAYQ FDDIEFCSHT PIQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
     YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVKPGKSTT YYYEGDPISA YKEVIGHNLF
     DLKRTSFEKL AKLNLSMSVL GAWTRHTSKR LLQDCVNMGV KEGNWLVNAD RLVSSKTGNR
     YIPGEGHTLQ GRHYEELVLA RKQINNFQGT DRYNLGPIVN MVLRRLRVMM MTLIGRGV
//
DBGET integrated database retrieval system