PKS5_MYCS2
ID PKS5_MYCS2 Reviewed; 2111 AA.
AC A0R1E8;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Mycocerosic acid synthase-like polyketide synthase {ECO:0000303|PubMed:19181796, ECO:0000303|PubMed:26976449};
DE Short=MAS-like PKS {ECO:0000303|PubMed:19181796, ECO:0000303|PubMed:26976449};
DE EC=2.3.1.- {ECO:0000305|PubMed:19181796};
DE AltName: Full=Polyketide synthase Pks5;
DE Flags: Precursor;
GN Name=pks5 {ECO:0000303|PubMed:19181796};
GN OrderedLocusNames=MSMEG_4727 {ECO:0000312|EMBL:ABK75252.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX PubMed=19181796; DOI=10.1128/jb.01235-08;
RA Etienne G., Malaga W., Laval F., Lemassu A., Guilhot C., Daffe M.;
RT "Identification of the polyketide synthase involved in the biosynthesis of
RT the surface-exposed lipooligosaccharides in mycobacteria.";
RL J. Bacteriol. 191:2613-2621(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-2020 (CONDENSING AND MODIFYING
RP REGIONS) IN COMPLEX WITH NADP, DOMAIN, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26976449; DOI=10.1038/nature16993;
RA Herbst D.A., Jakob R.P., Zahringer F., Maier T.;
RT "Mycocerosic acid synthase exemplifies the architecture of reducing
RT polyketide synthases.";
RL Nature 531:533-537(2016).
CC -!- FUNCTION: Polyketide synthase involved in the biosynthesis of 2,4-
CC dimethyl-2-eicosenoic acid, a lipid component of the
CC lipooligosaccharides (LOS) which are not located at the bacterial
CC surface but rather in deeper compartments of the cell envelope of
CC M.smegmatis. {ECO:0000269|PubMed:19181796}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:19181796}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26976449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- DOMAIN: Is organized in a condensing KS-AT and a modifying DH-PsiKR-ER-
CC KR region, followed by a flexibly tethered ACP domain.
CC {ECO:0000269|PubMed:26976449}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene abolishes the production
CC of both 2,4-dimethyl-2-eicosenoic acid, a polymethyl-branched fatty
CC acid (PMB-FA), and lipooligosaccharides (LOS). Complementation of the
CC mutant with the wild-type gene fully restores the phenotype.
CC {ECO:0000269|PubMed:19181796}.
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DR EMBL; CP000480; ABK75252.1; -; Genomic_DNA.
DR RefSeq; WP_011730042.1; NZ_SIJM01000004.1.
DR RefSeq; YP_888986.1; NC_008596.1.
DR PDB; 5BP1; X-ray; 2.20 A; A=1-892.
DR PDB; 5BP2; X-ray; 1.75 A; A/B/C/D=884-1186.
DR PDB; 5BP3; X-ray; 1.45 A; A/B=884-1186.
DR PDB; 5BP4; X-ray; 3.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=884-2020.
DR PDBsum; 5BP1; -.
DR PDBsum; 5BP2; -.
DR PDBsum; 5BP3; -.
DR PDBsum; 5BP4; -.
DR AlphaFoldDB; A0R1E8; -.
DR SMR; A0R1E8; -.
DR STRING; 246196.MSMEI_4610; -.
DR EnsemblBacteria; ABK75252; ABK75252; MSMEG_4727.
DR KEGG; msm:MSMEG_4727; -.
DR PATRIC; fig|246196.19.peg.4616; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR OMA; KDVQHYT; -.
DR BRENDA; 2.3.1.111; 3512.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell membrane; Fatty acid metabolism;
KW Lipid metabolism; Lipoprotein; Membrane; Multifunctional enzyme; NADP;
KW Oxidoreductase; Palmitate; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..2111
FT /note="Mycocerosic acid synthase-like polyketide synthase"
FT /id="PRO_0000437077"
FT DOMAIN 2029..2104
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 6..429
FT /note="Beta-ketoacyl synthase (KS)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 430..537
FT /note="Linker domain (LD)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 538..837
FT /note="Acyltransferase (AT)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 896..1176
FT /note="Dehydratase (DH)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 1215..1391
FT /note="Pseudo beta-ketoacyl reductase (PsiKR)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 1419..1743
FT /note="Enoylreductase (ER)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT REGION 1765..2008
FT /note="Beta-ketoacyl reductase (KR)"
FT /evidence="ECO:0000305|PubMed:26976449"
FT ACT_SITE 178
FT /note="Acyl-thioester intermediate; for beta-ketoacyl
FT synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 629
FT /note="Acyl-ester intermediate; for acyltransferase
FT activity"
FT /evidence="ECO:0000305"
FT ACT_SITE 934
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03132"
FT ACT_SITE 1100
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03132"
FT BINDING 1773..1776
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1796..1799
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1824..1825
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1902..1903
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT MOD_RES 2064
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 449..457
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 502..511
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 512..523
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 563..580
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 584..589
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 600..616
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 644..658
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 674..683
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 688..696
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 699..704
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 706..717
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 723..726
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 735..740
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 741..747
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 776..784
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 808..810
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 814..823
FT /evidence="ECO:0007829|PDB:5BP1"
FT STRAND 829..833
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 841..844
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 845..854
FT /evidence="ECO:0007829|PDB:5BP1"
FT HELIX 860..863
FT /evidence="ECO:0007829|PDB:5BP1"
FT TURN 902..904
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 905..909
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 911..914
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 916..922
FT /evidence="ECO:0007829|PDB:5BP3"
FT TURN 925..927
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 929..933
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 939..941
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 944..959
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 964..969
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 981..990
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 993..1000
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1007..1016
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1028..1033
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1037..1040
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1041..1050
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1062..1067
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1074..1079
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1083..1089
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1096..1106
FT /evidence="ECO:0007829|PDB:5BP3"
FT HELIX 1110..1115
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1121..1130
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1137..1148
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1151..1160
FT /evidence="ECO:0007829|PDB:5BP3"
FT STRAND 1165..1175
FT /evidence="ECO:0007829|PDB:5BP3"
FT TURN 1180..1182
FT /evidence="ECO:0007829|PDB:5BP3"
SQ SEQUENCE 2111 AA; 223175 MW; 639D0AFB1E7E0C20 CRC64;
MTQNCVAPVA IIGMACRLPG AINSPQQLWE ALLRGDDFVT EIPTGRWDAE EYYDPEPGVP
GRSVSKWGAF LDDPAAFDPE FFGITEREAA AIDPQHRLLL ETAWEAVEHS GLNPAGLAGS
ATGVFMGLTH NDYAHLAADA KALEGPYGFT GTSFSLASGR IAYALGVHGP AITVDTACSS
SLSAIHMACR SLHDGESDVA LAGGVSVLLE PRKAAGGSAA GMLSPTGHCH AFDTAADGFV
SAEGCVVLTL KRLDDAVADG DRILAVIRGT ATNQDGRTVN IATPSADAQA KVYRMALKAA
GVEPGTVGLV EAHGTGTPVG DPLEFSSLAE VYGTDGPCAL GSIKTNFGHT QSAAGALGVM
KAVLALQHNV IPQNLHFTRL PDQMAEIETG LFVPETITPW PVREGQPRRA AVSAYGLSGT
NVHAVLEQAP ESPAETAAEA ISPKAGNALV FPVSASSADA LRSTAQHLAD WLLRSGDGNG
RGPAIDLGDL AYTLARRRGF RAARSAVLAG DRGTLVEGLR QIADGEAMPQ QAVTNDDRGP
VWVFSGQGSQ WASMGAELLD REPAFAAAIA ELEPLIAAES DFSVTEALTA SETVTGIDRV
QPTIFAVQVA LAAAMRSHGV VPGAVIGHSM GEVAASVVSG ALSLEDGVKV ICRRTRLMTR
IAGSGAMAMV ELPAQQVLSE LASRGVDDVV LSVVASPQST VVGGATASVR ELIEMWESRG
VMAREIAVDV ASHSPQVDPI LDDLIEALAD LDPAEPEIPY YSATLYDPRD YADYDAYYWA
DNLRHTVRFS AAVQAALEDG HRVFAELSPH PLLTHPVEQT ARSLDMPLAV FAAMRRQQEM
PHGLLGFVAD LHSAGAAVDF SVLYPTGRLL DAPLPAWTHS TLLLDRELES SAPGVPSVSV
HPLLGSHVVL PQEPEEHLWQ GDVGTEAHPW LSDHRVHQVA VLPGAAYCEM ALAAVTPVLG
DTGEVHDLKF HDMLLLDDAT PVWVSAAVTA PGTAEFGVET HQSGDRTQRA TAVLRGDVDA
ERPAAHSIDA LLAAHPNRVD GDELRAGFGT VGIGHGAAFA GLSEAYVATA AEPTVVAAVA
LPGPLRSGQR GYTVHPALLD ACFQSVIAHP EVQNIASGML LPLGVRRLRA YGSTRNVRYC
LSRIVKADSF GVEADLELLD ADGTVLLSAM GLQLGTGNSD KAEEERLLDE RLLTIEWQQR
ELPRPEGSET VDAGSWLVIL AGDDDENPRA AGVVSALIGA GMPTTTMAWS HDADHDAQAA
ALTARLDEQP LAGVAVIVGD SETGTDAHDV GADARRGADH VRHLVRIART LADAVGEPPR
LYVVTHRSQH VLDTDEPYLE HSGLRGLIRV VGMEHPRLRA TQIDVDDSTA HEALVRQLLS
GSPEDETAWR DGQWYAARLC PSPLRAAERR TAVADNASEG MRLVVRNPGD LESMELVTFE
RGTPGPGQIE VAVKASSINF ADVLVAFGRC PSFDGRLPEL GSEFGGVVTA VGPGVTTHRV
GDRVGGVSAN GCWSNFVTCE ADLATKLPEG ISEHEAAAVG LAYGTVWLGL TELARMSAGD
KILIHSATGG VGQAAIAVAR AAGAEIYATA GSEKRRQLLR DWGIEHVYDS RTTAFADQIR
TDTDGYGVDI VLNSVTGPAQ RAGLELLAFG GRFVEIGKRD IYADTRLGLF PFRRNLSFYA
VDLALMTVTH PQKIRDLLAT VYRLIADGTL PLPEITHYPL EEAATAIRIM GGAQHTGKLV
IDIPDTGQSQ VVVPPEQVPV FRGDGAYVIT GGLGGLGLFL AERMAAAGCG RIVVNSRSAP
STRSSEIIEL IRATGADIVV ECGDIAEPDT ALRLVAAATQ TGLPLRGVLH AAAVVEDATL
ANITDELVEH DWAPKVYGAW NLHQAVQSGG PATSELDWFC AFSSAAALVG SPGQGAYAAA
NSWLDAFMQW RRAQGLPATS IAWGAWGEIG RGTAMAEGDN AIAPDEGAYA FEAILRHDRV
YNGYAPVLGA SWLTAFAQRS PFAELFLADT QGASETRKLR SELAALPREE WPTHLRRLIA
EQVGLLLRRT VDPDRPLSEY GLDSLGHLEL RTRIETETGV RVSAMDMTTI RGLAQRLCEM
LDTDDAVSAP S
