PKSL_BACSU
ID PKSL_BACSU Reviewed; 4538 AA.
AC Q05470;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Polyketide synthase PksL;
DE Short=PKS;
GN Name=pksL; Synonyms=outG, pksA, pksX; OrderedLocusNames=BSU17190;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / PB1424;
RX PubMed=8344529; DOI=10.1016/0378-1119(93)90347-6;
RA Scotti C., Piatti M., Cuzzoni A., Perani P., Tognoni A., Grandi G.,
RA Galizzi A., Albertini A.M.;
RT "A Bacillus subtilis large ORF coding for a polypeptide highly similar to
RT polyketide synthases.";
RL Gene 130:65-71(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP SEQUENCE REVISION TO 2299-2300; 2398; 3384; 4141 AND 4232.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3730-4538.
RC STRAIN=168 / PB1424;
RA Grandi G.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [7]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000269|PubMed:17234808}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85145.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA78479.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U11039; AAA85145.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB13602.3; -; Genomic_DNA.
DR EMBL; Z14098; CAA78479.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35133; CAA84504.1; -; Genomic_DNA.
DR PIR; S25021; PN0637.
DR RefSeq; NP_389600.3; NC_000964.3.
DR RefSeq; WP_010886513.1; NZ_JNCM01000035.1.
DR PDB; 5E1V; X-ray; 1.87 A; A/B=6-279.
DR PDB; 5E5N; X-ray; 2.00 A; A/B/C/D=2870-3466.
DR PDB; 5E6K; X-ray; 2.16 A; A/B=2870-3466.
DR PDB; 5ENY; X-ray; 4.00 A; A/B/C/D/E/F/G/H=2719-3462.
DR PDB; 5ERF; X-ray; 3.10 A; A/B=2870-3466.
DR PDBsum; 5E1V; -.
DR PDBsum; 5E5N; -.
DR PDBsum; 5E6K; -.
DR PDBsum; 5ENY; -.
DR PDBsum; 5ERF; -.
DR SMR; Q05470; -.
DR STRING; 224308.BSU17190; -.
DR PaxDb; Q05470; -.
DR PRIDE; Q05470; -.
DR EnsemblBacteria; CAB13602; CAB13602; BSU_17190.
DR GeneID; 940032; -.
DR KEGG; bsu:BSU17190; -.
DR PATRIC; fig|224308.43.peg.1815; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0300; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR eggNOG; COG4221; Bacteria.
DR InParanoid; Q05470; -.
DR OMA; ITGLEWI; -.
DR BioCyc; BSUB:BSU17190-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 5.
DR Gene3D; 3.10.129.110; -; 2.
DR Gene3D; 3.40.47.10; -; 4.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR011254; Prismane-like_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF16197; KAsynt_C_assoc; 3.
DR Pfam; PF00109; ketoacyl-synt; 4.
DR Pfam; PF02801; Ketoacyl-synt_C; 4.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF00550; PP-binding; 5.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 4.
DR SMART; SM00823; PKS_PP; 5.
DR SUPFAM; SSF47336; SSF47336; 4.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF53901; SSF53901; 4.
DR SUPFAM; SSF56821; SSF56821; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis; Cytoplasm;
KW Multifunctional enzyme; NADP; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..4538
FT /note="Polyketide synthase PksL"
FT /id="PRO_0000180299"
FT DOMAIN 320..394
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1800..1873
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2597..2674
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2738..2815
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3960..4037
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 289..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..874
FT /note="Beta-ketoacyl synthase 1"
FT REGION 1048..1226
FT /note="Dehydratase"
FT REGION 1520..1713
FT /note="Beta-ketoacyl reductase 1"
FT REGION 1929..2368
FT /note="Beta-ketoacyl synthase 2"
FT REGION 2546..2568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2828..2854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2876..3297
FT /note="Beta-ketoacyl synthase 3"
FT REGION 3686..3887
FT /note="Beta-ketoacyl reductase 2"
FT REGION 4085..4488
FT /note="Beta-ketoacyl synthase 4"
FT COMPBIAS 289..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 609
FT /note="For beta-ketoacyl synthase 1 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2103
FT /note="For beta-ketoacyl synthase 2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 3040
FT /note="For beta-ketoacyl synthase 3 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 4237
FT /note="For beta-ketoacyl synthase 4 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 354
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1834
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2634
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2775
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3997
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 2299..2300
FT /note="QL -> HV (in Ref. 1; AAA85145/CAA78479)"
FT /evidence="ECO:0000305"
FT CONFLICT 2398
FT /note="A -> P (in Ref. 1; AAA85145/CAA78479)"
FT /evidence="ECO:0000305"
FT CONFLICT 3384
FT /note="G -> A (in Ref. 1; AAA85145/CAA78479)"
FT /evidence="ECO:0000305"
FT CONFLICT 4041
FT /note="A -> R (in Ref. 1; AAA85145/CAA78479 and 5;
FT CAA84504)"
FT /evidence="ECO:0000305"
FT CONFLICT 4232
FT /note="V -> L (in Ref. 1; AAA85145/CAA78479 and 5;
FT CAA84504)"
FT /evidence="ECO:0000305"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 75..86
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 220..232
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:5E1V"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 265..278
FT /evidence="ECO:0007829|PDB:5E1V"
FT STRAND 2876..2885
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 2888..2890
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2891..2899
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 2905..2907
FT /evidence="ECO:0007829|PDB:5E5N"
FT TURN 2910..2912
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2915..2917
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 2933..2935
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2945..2948
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2952..2955
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2960..2976
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2980..2983
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 2988..2993
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 2998..3003
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3016..3027
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3033..3036
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3039..3041
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3042..3055
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3060..3068
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3073..3076
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3106..3114
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3115..3120
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3127..3136
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3148..3162
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3166..3168
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3171..3173
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3178..3180
FT /evidence="ECO:0007829|PDB:5E6K"
FT HELIX 3182..3195
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3204..3207
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3210..3213
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3217..3219
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3220..3233
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3244..3246
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3252..3254
FT /evidence="ECO:0007829|PDB:5E6K"
FT STRAND 3255..3259
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3275..3281
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3285..3293
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3311..3319
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3320..3336
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3342..3351
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3357..3366
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3367..3379
FT /evidence="ECO:0007829|PDB:5E5N"
FT STRAND 3386..3390
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3391..3393
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3395..3403
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3405..3416
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3420..3429
FT /evidence="ECO:0007829|PDB:5E5N"
FT HELIX 3435..3438
FT /evidence="ECO:0007829|PDB:5E5N"
SQ SEQUENCE 4538 AA; 506182 MW; 398353DEC864EBF2 CRC64;
MRWRSNVKKI TKQLTLSLKN PFIYHHVVYG QNVLPGLAYI DIIYQIFREH GFSCSELQLR
NLSIYQPLTA EQDAVIVLNI QCAEKKEGQW QITAKGIEKR DGKEASEEKL YMKADMHADS
PAIFEETLDL SQIKASAQNV VQLDDVYEQC RRQELVHSEY MKAKGCIYEE EDGVLLELSL
GSEAMLHAEG FMFHPTLIDG SGVGANHLLT SLLKGEQRLY LPLFYESFSA SALLQTDCMT
RIKRSSVRRE KELIYVTLEF FNASGEKVAE LKNFTSKLVR EAELISGKHQ DAQETQMTRA
DTAERDKPAD MVSSPVNSYS EAEQFVSQLI AEKINKPVEQ VEKQVGYYQM GLNSSGLLEV
VETISDKIGE SLSPTLLFEH TTIAELSAFL AEEYAEHFSA AGSLGQNERA RVSDSINDHK
TVEGSRPAPI EAAGDIAIIG LAGRYPKAAN IHEFWNNLKE GKDCVSEIPE SRWDWQRLEG
ITSPSGKDIS KWGGFIDDPD CFDPQFFRIT PREAETMDPQ ERLFLETCWE TIEDAGYTPK
TLAKPKGRNK RQHVGVFAGV MHKDYTLVGA EEASAENVFP LSLNYAQIAN RVSYFCNFHG
PSMAVDTVCS SSLTAVHLAL ESIRHGECDV ALAGGVNLSL HPNKYMTYGV WDMFSTDGHC
RTFGKDGDGY VPAEGIGAVL LKPLRQAEED GDRIYAVIKG SAVNHVGTVS GISVPSPVSQ
ADLIETCLEK TGIDPRTISY VEAHGTGTSL GDPIEIQGLV KAFRQYTQDR QFCSIGSVKS
NIGHAESAAG ISGLSKVALQ LHHQKLVPSL HSEELNPYVD FEKSPFYVQH ETETWKQPVI
KENGEDVPYP RRAGISSFGA TGSNAHIILE EHIPQAAEQD VSLSSDSDIS AVIPLSARNQ
ERLRVYAKRL LDFLHDGIQI RDLAYTLQVG REPMEERVSF LASGIQELSD QLKAFIEGRK
AIQHCWKGRV SRGSEPSRPA ESVHKLLEQR KLDQIAEQWA NGSGVDWKLL YEGSKPKRIS
LPTYPFERVR YWVPKAEKKT DRSKQERHIL HPLLHQNVSD ISGVRFRSAF TGREFFLKDH
VIKGEHVLPG AALLEMVRAA VERAAADQFP TGFRLRNIVW VRPFAVTEQQ KDIDVRLYPE
ENGEITFEIC RDPESAEESP IVYGQGSAVL CEAGENPVIN IEELKASYNG RTLSPFDCYE
AYTEMGIHYG DSHRAIDSLY AGENGVLVKL TMPPVISDTE DHYILHPSMI DSAFQASIGL
RLGGATSLED RKAMLPFAIQ DVRIFKGCEA SMWARITYSE GSTAGDRMQK LDIDLCNEEG
QVCVRLTSYS ARVLETDQEG PSEANDTLLF EHIWEERAAE RQELIEYDTY KVVVCDVGEQ
MESLQNHLDC TVLQHDTETI DERFEGYAIQ LFEEIKQLMH SKTGGHTFIQ VAVPALDEPQ
LLSGLTGLLK TAELENPKLT GQLIEIETGM SAGELFEILE ENRRYPRDTH IRHWQGKRFV
SKWKEVSGEH LSADMPWKDK GVYLITGGAG GLGFIFATEI ANQTNDAVVI LTGRSPLDER
KKKKLKALQK LGIQAIYRQA DLADKQTVDA LLKETQNVYG DLDGIIHSAG LIKDNFIMKK
KKEEVQTVLA PKVAGLIHLD EATKDIPLDF FILFSSGAGA VGSAGQADYA MANAFMNAFS
EYRNGQAELH KRYGKTLSVC WPLWKDGGMQ IDAETARMLK RETGMVAMET DRGIQALYHG
WTSGKPQVLV ASGVTDRIRA FLHETGHGKG QSHNIKKSSL NQEAEKADMI GEIDEEILRE
KAENYFKQVL SSVIKLPAGQ IDAEAPLEDY GIDSIMIMHV TGQLEKVFGS LSKTLFFEYQ
DIRSLTRYFI DSRREKLLDI LGFETGKPSV ERKSEPEKQE IPVIPRKSGF LPLQDKEQKQ
VREKETEEIA IIGISGRYPQ ADNIDELWEK LRDGRDCITE IPADRWDHSL YYDEDKDKPG
KTYSKWGGFM KDVDKFDPQF FHISPREAKL MDPQERLFLQ CVYETMEDAG YTREHLGRKR
DAELGGSVGV YVGVMYEEYQ LYGAQEQVRG RSLALTGNPS SIANRVSYYF DFHGPSIALD
TMCSSSLTAI HLACQSLQRG ECEAAFAGGV NVSIHPNKYL MLGQNKFMSS KGRCESFGQG
GDGYVPGEGV GAVLLKPLSK AVEDGDHIYG IIKGTAINHG GKTNGYSVPN PNAQADVIKK
AFVEAKVDPR TVSYIEAHGT GTSLGDPIEI TGLSKVFTQE TDDKQFCAIG SAKSNIGHCE
SAAGIAGVTK VLLQMKYRQL APSLHSNVLN PNIDFLNSPF KVQQELEEWK RPIISVNGKD
IELPRIAGVS SFGAGGVNAH ILIEEYAPEP VEERLPARKQ PAVIVLSAKN EERLQKRAER
LLHAIREQTY VEADLHRIAY TLQVGREAMK ERLAFVAETM QELEEKLYEC ISGTENREYV
YRGQVKSNKE AIAAFAADED MSKTIEAWLQ KGKYAKVLDL WVRGLRIDWS TLYQDQKPRR
ISLPAYPFAR DRYWIDVNAK AEEKRTEEPF APVQPVIPKP SVDREASGKP ANITLQPLMT
NQDRLERVPS DTETETITAE ALCDELTAGL AEVLYMDQNE IDPDEAFIDI GMDSITGLEW
IKAINKQYGT SLNVTKVYDY PTTRDFAVYL AHELSTQAGE KKQTETYTPI RQKTVVPAAK
PANISLQPLE HHQPVQEEAE ETIQYAAAEI SASRQYTVAI ETLHENLRES IADVLYMEPY
EVDIDEAFID IGMDSITGLE WIKAVNKQYG TSFTVTRVYD YPTIRDFAEM LKSELGTHLD
RKIEHTDSFE AAQQKPAASS HPKPAERPLQ PVQHPIKKEH EKKTVPVLQD RPEDAIAIVG
MSGRYPGARN VREYWDNLVH ARNAIRDIPT SRWDVDKYYD PVLNKKGKVY CKSMGMLDDI
EHFDPLFFNI PPSEAELMDP QHRIFLQEGY KAFEDAGYNA RTLNEKKCGV YLGIMSNEYG
VMLNRQSRAN ATGNSFAIAA ARIPYFLNLK GPAIPIDTAC SSSLVGTHLA RQALINKEID
MALVGGVSLY LTPESYMSMC EAGMLSPDGQ CKAFDNGANG FVPGEGAGAL VLKRLKDAEA
DRDHIYGIII GSGINQDGKT NGITAPSAKS QMDLERDIYE TYGIHPESIS YVEMHGTGTK
QGDPIELEAL STVFQEKTDK KQFCAIGSVK SNIGHTSAAA GVAGVQKVLL CMNHKTLVPT
LNFTTPNEHF EFEHSPLYVN TELKPWETAD GKPRRACVSS FGYSGTNAHI VIEEYQPEKR
NDRLTKQHRS ALFVLSAKKE KQLKAYAEAM KDFVTSNEDI DLEDMAYTLQ TGREAMDYRM
AFLADSREML IKALDDYLAE MPNGSIFAAH VKTKKSEIKL FETDHDAKAL LQTWIEKKRL
EKVAELWVKG LQIDWNKLYG EYTPRRISLP AYPFAEEYYW LPTQEGEPET IATAMPQFEL
MPKRCFLRKQ WQPCPIEPAE MTNQTVAILA NEETMALAEE LSAYFSTYRI FDSQELDRVS
AADYEHVAGA IDLIGCGTSH EHSMGWINWL QKLIEQGRAS KHHLTVLGVT KGLEAYANEG
VLLSGASRAG LYRMLQSEYS HLTSRHADME CEASHEELAR LIAVEYYAKS TESEVCYRNG
QRYRAYLTEQ PAEAALSHKQ VSFSTDKVLL ITGGTRGLGL LCARHFVKTY GVKRLVLIGR
EELPPRDQWN SVKISSLAEK IKAVQELEDM GAQVQVLSLD LTDRVAVEQS LKTIHETMGA
IGGVIHCAGM VNKQNPAFIR KSLEEIGQVL EPKVEGLQTL FDLLQDEPLA FFTLFSSVSA
AIPALAAGQA DYAMANAFMD YFAEAHQDKC PIVSIQWPNW KETGLGEVRS KALEQTGLIS
LTNDEGLQLL DQILSDRQYA VVLPAVPDTN VWKPDKLMQP SLPVEALSHP ETKEQTSTRN
LFPETVDWLV TLFSDELKIA AEDFETDEPF QEYGIDSIIL AQLVQQMNQQ LNGDIDPSIL
FEYPTIESFA HWLISKYDIS AVLQPSVPEK QTPLKPQSAM KQKLVPEQRP QQISHEKTAL
LAEDIAIIGL SCRFPGAETL EEYWDLIRDG RSAIAPVPPE RFGNSSSNYA GLIDEMNRFD
HDFFMMSESD VRAMDPQALA VLEESLKLWY HAGYTEKEVK GMRAGVYIGG RSQHKPDPAS
LSKAKNPIVA GGQNYLAANI SQFFDLKGPS IVLDTACSSA LVGLNMAIQA LRSGDIEAAV
VGGVSLLDAD AHRMFHERGL LCDKPSFHIF DKRADGVILG EGVGMVLVKT VNQAVEDGDS
IYAVIKAAAI NNDGRTAGPS SPNLEAQKDV MLSALEKSGK KTEEISYLEA NGSGSAVTDL
LELKAIQSIY RSESKAPLGL GSVKPNIGHP LCAEGIASLI KVALMLKHRQ LVPFLSGNEN
MPYFDIEKTD LYFSRSQAEW KETTPAAAIN CFADGGTNAH LIIEGWRDSA ERPIRRKPLP
LPELNRQPVL IKPSAQNVQK KVHSDTGASK DMFWKTFK
