GenomeNet

Database: UniProt
Entry: X2FTB9_9FLAV
LinkDB: X2FTB9_9FLAV
Original site: X2FTB9_9FLAV 
ID   X2FTB9_9FLAV            Unreviewed;      3897 AA.
AC   X2FTB9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS   Bovine viral diarrhea virus 2.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Pestivirus; Pestivirus tauri.
OX   NCBI_TaxID=54315 {ECO:0000313|EMBL:AHN05530.1, ECO:0000313|Proteomes:UP000142864};
RN   [1] {ECO:0000313|EMBL:AHN05530.1, ECO:0000313|Proteomes:UP000142864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=108 {ECO:0000313|EMBL:AHN05530.1};
RX   PubMed=24708266; DOI=10.1186/1297-9716-45-38;
RA   Passler T., Riddell K.P., Edmondson M.A., Chamorro M.F., Neill J.D.,
RA   Brodersen B.W., Walz H.L., Galik P.K., Zhang Y., Walz P.H.;
RT   "Experimental infection of pregnant goats with bovine viral diarrhea virus
RT   (BVDV) 1 or 2.";
RL   Vet. Res. 45:38-38(2014).
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}.
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DR   EMBL; KF835701; AHN05530.1; -; Genomic_RNA.
DR   Proteomes; UP000142864; 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        656..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1033..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1072..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1108..1132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1144..1162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1183..1206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1212..1229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1250..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1275..1299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1358..1385
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          1439..1587
FT                   /note="Peptidase C74"
FT                   /evidence="ECO:0000259|PROSITE:PS51692"
FT   DOMAIN          1588..1761
FT                   /note="Peptidase S31"
FT                   /evidence="ECO:0000259|PROSITE:PS51535"
FT   DOMAIN          1800..1958
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1971..2141
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          3517..3640
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          169..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..206
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        1656
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1693
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1750
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   3897 AA;  438195 MW;  B7305F8786DC7D1C CRC64;
     MELFSNELLY KTYKQKPAGV VEPVYDVNGR PLFGEGSDLH PQSTLKLPHQ RGSANILTNA
     RSLPRKGDCR RGNVNGAVSG IYIKPGPIYY QDYMGPVYHR APLELCREAS MCETTRRVGR
     VTGSDGKLYH IYICIDGCIL LKRATRNQPE VLKWVYNRLN CPLWVTSCSD EGSKGATSKK
     QPKPDRIEKG KMKIAPKETE KDCKTRPPDA TIVVEGVKYQ VKKKGKVRGK NTQDGLYHNK
     NKPPESRKKL EKALLAWAIL AAVLLQLVTG ENITQWNLMD NGTKGIQQAM FLRGVNRSLH
     GIWPEKICTG VPTHLATDYE LKEIVGMMDA SERTNYTCCR LQRHEWNKHG WCNWFHIEPW
     IWLMNKTQNN LTEGQPLREC AVTCRYDKEA ELNIVTQARD RPTTLTGCKK GKNFSFAGVV
     LDGPCNFKVS VEDVLFKEHD CGNMLQETAI QLLDGATNTI EGARVGTAKL TTWLGKQLGI
     LGKKLENKSK AWFGAHAASP YCGVERKVGY VWYTKNCTPA CLPRNTKIIG PGKFDTNAED
     GKILHEMGGH LSEFALLSLV VLSDFAPETA SVIYLVLHFA IPQSHVDVDT CDKNQLNLTV
     ATTVAEVIPG TVWNLGKYVC IRPDWWPYET TTVFVLEEAG QVIKLGLRAI RDLTRIWNAA
     TTTAFLIFLV KALRGQLIQG LLWLMLITGA QGFPECKEGF QYAISKDRKM GLLGPESLTT
     TWHLPTKKLV DSMVQVWCEG KDLKILKTCT KEERYLVAVH ERALPTSAEF MQISDGTIGP
     DVIDMPDDFE FGLCPCDSKP VIKGKFNASL LNGPAFQMVC PQGWTGRIEC TLANQDTLDT
     TVVRTYRRTT PFQRRKWCTY EKIIGEDIHE CVLGGNWTCI TGDHSRLKDG PIKKCKWCGY
     DFVNSEGLPH YPIGKCMHIN ESGYRYVDDT SCDRGGVAIV PTGTVKCRIG NVTVQVIATN
     NDLGPMPCSP AEVIASEGPV EKTACTFNYS KTLPNKYYEP RDRYFQQYML KGEWQYWFDL
     DSVDHHKDYF SEFIIIAVVA LLGGKYVLWL LITYTILSEQ MAMGAGVNTE EIVMIGNLLT
     HSDIEVVVYF LLLYLIVKEE LVRKWIILVY HILVANPMKT IGVILLMLGG VVKASRISAD
     DQSAMDPCFL LVTGLVAVLM IARREPATLP LIVALLAIRT SGFLLPTSID ITVAVVLIVL
     LLASYVTDYF RYKKWLQFSF SLIAGIFIIR SLKHINQMEV PEISMPSWRP LALVIFYIIS
     TAITTNWDID LAGFLLQWAP AVIMMATMWA DFLTLIIVLP SYELSKLYFL KNVRTDVEKN
     WLGKVKYRQI SSVYDICDSE EAVYLFPSRH KSGSRPDFIL PFLKAVLISC ISSQWQVVYI
     SYLILEITYY MHRKIIDEVS GGANFLSRLI AAIIELNWAI DDEECKGLKK LYLLSGRVKN
     LIVKHKVRNE AVHRWFGEEE IYGAPKVITI IKASTLSKNR HCIICTICEG KDWNGANCPK
     CGRQGKPITC GMTLADFEEK HYKKIFIREG CHDGPFREEY KGYIQYTARG QLFLRNLPIL
     ATKMKLLMVG NLGAEIGDLE HLGWVLRGPA VCKKITNHEK CHVNIMDKLT AFFGIMPRGT
     TPRAPVRFPT ALLKVRRGLE TGWAYTHQGG ISSVDHVTAG KDLLVCDSMG RTRVVCHSNN
     KMTDETEYGI KTDSGCPEGA RCYVLNPEAV NISGTKGAMV HLQKTGGEFT CVTASGTPAF
     FDLKNLKGWS GLPIFEASSG RVVGRVKVGK NEDSKPTKLM SGIQTVSKNQ TDLVDIVKKL
     ASMNRGEFKQ ITLATGAGKT TELPRSVIEE IGRHKRVLVL IPLRAAAESV YQYMRVKYPS
     ISFNLRIGDM KEGDMATGIT YASYGYFCQL PQPKLRAAMV EYSYIFLDEY HCATPEQLAI
     IGKIHRFAEN LRVVAMTATP AGTVTTTGQK HPIEEFIAPE VMKGEDLGSE YLDIAGLKIP
     TEEMKGNMLV FVPTRNMAVE TAKKLKAKGY NSGYYYSGEN PENLRVVTSQ SPYVVVATNA
     IESGVTLPDL DTVVDTGLKC EKRVRISSKM PFIVTGLKRM AVTIGEQAQR RGRVGRVKPG
     RYYRSQETAS GSKDYHYDLL QAQRYGIEDG INVTKSFREM NYDWSLYEED SLMITQLEVL
     NNLLISEDLP AAVKNIMART DHPEPIQLAY NSYENQIPVL FPKIKNGEVT DSYENYTYLN
     ARKLGEDVPA YVYATEDEDL AVDLLGMDWP DPGNQQVVET GRALKQVTGL STAENALLIA
     LFGYVGYQTL SKRHIPMITD IYTLEDHRLE DTTHLQFAPN AIRTDGKDSE LKELAVGDLD
     KYVDALVDYS KQGMKFIKVQ AEKVKDSQST KEGLHTIKEY VDKFIQSLTE NKEEIIRYGL
     WGAHTALYKS LAARLGHETA FATLVVKWLA FGGETVSAHI KQAAVDLVVY YIINKPSFPG
     DTETQQEGRR FVASLFISAL ATYTYKTWNY NNLQRVVEPA LAYLPYATSA LKLFAPTRLE
     SVVILSSTIY KTYLSIRKGK SDGLLGTGIS AAMEILNQNP ISVGISVMLG VGAIAAHNAI
     ESSEQKRTLL MKVFVKNFLD QAATDELVKE NPEKIIMALF EAVQTIGNPL RLIYHLYGVY
     YKGWEAKELA EKTAGRNLFT LIMFEAFELL GMDSEGKIRN LSGNYILDLI FNLHNKLNKG
     IKKLVLGWAP APFSCDWTPS DERISLPHNN YLRVETRCPC GYEMKAIKNV AGKLTKVEEK
     GPFLCRNRLG RGPPNFKVTK FYDDNLIEVK PVARLEGQVD LYYKGVTARL DYNNGKVLLA
     TNKWEVDHAF LTRLVKKHTG IGFKGAYLGD RPDHQDLVDR DCATITKNSV QFLKMKKGCA
     FTYDLTISNL VRLIELVHKN NLQEREIPTV TVTTWLAYSF VNEDLGTIKP VLGEKVIPEP
     PTELSLQPTV GLVTTETAIT ITGEAELMTT GITPVVEMKE ELQLDHQSTT LKVGLKEGEY
     PGPGVNPNHL VEVIDEKDDR PFVLIIGNKG STSNRARTAK NIRLYKGNNP REIRDLMSQG
     RILTVALKEL DPELKELVDY KGTFLNREAL EALSLGKPIK RKTTTAMIRR LIEPEVEEEL
     PDWFQAEEPL FLEAKIQADL YHLIGSVDSI KSKAKELGAT DNTKIVKEVG ARTYTMKLSS
     WSTQVTKKQM SLAPLFEELL LKCPPCSKIS KGHMVSAYQL AQGNWEPLGC GVYMGTIPAR
     RLKIHPYEAY LKLKELVEVE LSRTTVKESI IREHNTWILR KVRHEGNLRT KSMINPGKIS
     DQLCRDGHKR NIYNKIIGST MASAGIRLEK LPVVRAQTDT TSFHQAIREK IDKPENKQTP
     ELHEELMKVF DCLKIPELKE SYDEVSWEQL EAGINRKGAA GYLESKNIGE VLDTEKHIVE
     QLIKDLRKGK KIRYYETASP KNEKRDVSDD WEAGEFVDEK KPRVIQYPDA KVRLAIAKVM
     YKWVKQKPVV IPGYEGKTPL FDIFNKVKKE WDSFQDPVAV SFDTKAWDTQ VTSRDLMLIK
     DIQKYYFKRS THKFLDTITE HMVEVPVITA DGEVYIRSGQ RGSGQPDTSA GNSMLNVLTM
     IYAFCKSTGI PYRGFSRVAR IHVCGDDGFL ITERGLGLKF SEKGMQILHE AGKPQKITEG
     DKMKVAYRFE DIEFCSHTPV PVRWADNTSS YMAGRSTATI LAKMATRLDS SGERGSTAYE
     KAVAFSFLLM YSWNPVVRRI CLLVLSQFPE ISPSKNTIYY YQGDPIAAYR EVIGKQLCEL
     KRTGFEKLAS LNLSMTTLGI WTKHTSKRLI QDCVEVGKRE GNWLVNADRL IAGKTGKFYI
     PSTGVTLLGK HYEEINLKQK ATQPPIEGVD RYKLGPIVNV ILRRLRVMLM TVASGSW
//
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