ID PPSA_MYCTU Reviewed; 1876 AA.
AC P9WQE7; L0TCN4; Q10977;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit A {ECO:0000305};
DE EC=2.3.1.292 {ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
DE AltName: Full=(Phenol)carboxyphthiodiolenone synthase subunit A;
DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
DE AltName: Full=Phthiocerol synthesis polyketide synthase type I PpsA;
GN Name=ppsA; OrderedLocusNames=Rv2931; ORFNames=MTCY338.20;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=15749014; DOI=10.1016/j.molcel.2005.02.009;
RA Trivedi O.A., Arora P., Vats A., Ansari M.Z., Tickoo R., Sridharan V.,
RA Mohanty D., Gokhale R.S.;
RT "Dissecting the mechanism and assembly of a complex virulence mycobacterial
RT lipid.";
RL Mol. Cell 17:631-643(2005).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20553505; DOI=10.1111/j.1742-464x.2010.07688.x;
RA Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M.,
RA Guilhot C., Chalut C.;
RT "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis
RT of phthiocerol dimycocerosates and related compounds in Mycobacterium
RT tuberculosis.";
RL FEBS J. 277:2715-2725(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Part of the PpsABCDE complex involved in the biosynthesis of
CC the lipid core common to phthiocerols and phenolphthiocerols by
CC successive additions of malonyl-CoA or methylmalonyl-CoA extender units
CC (PubMed:15749014, PubMed:20553505). PpsA can accept as substrate the
CC activated forms of either icosanoyl (C20), docosanoyl (C22) or
CC lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-
CC hydroxyphenyl)-C19 fatty acyl from FadD29 (PubMed:15749014,
CC PubMed:20553505). PpsA initiates the biosynthesis and extends its
CC substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins
CC add the second and third malonyl-CoA extender units. PpsD adds an (R)-
CC methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The
CC incorporation of the methylmalonyl units results in formation of two
CC branched methyl groups in the elongated product (PubMed:15749014).
CC {ECO:0000269|PubMed:15749014, ECO:0000269|PubMed:20553505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 10 H(+) + icosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 3 malonyl-CoA + 5 NADPH =
CC C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase]
CC + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57748, Rhea:RHEA-
CC COMP:14985, Rhea:RHEA-COMP:14986, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87848, ChEBI:CHEBI:142236;
CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014,
CC ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + docosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone
CC synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57752,
CC Rhea:RHEA-COMP:14987, Rhea:RHEA-COMP:14988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142237, ChEBI:CHEBI:142238;
CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014,
CC ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C35-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57756, Rhea:RHEA-COMP:14272, Rhea:RHEA-
CC COMP:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133300,
CC ChEBI:CHEBI:142259; EC=2.3.1.292;
CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)nonadecanoyl-
CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA +
CC 5 NADPH = C37-(phenol)carboxyphthiodiolenone-
CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5
CC NADP(+); Xref=Rhea:RHEA:57760, Rhea:RHEA-COMP:14273, Rhea:RHEA-
CC COMP:14990, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133301,
CC ChEBI:CHEBI:142260; EC=2.3.1.292;
CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:15749014};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:15749014}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
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DR EMBL; AL123456; CCP45734.1; -; Genomic_DNA.
DR PIR; C70749; C70749.
DR RefSeq; NP_217447.1; NC_000962.3.
DR RefSeq; WP_010886158.1; NC_018143.2.
DR AlphaFoldDB; P9WQE7; -.
DR SMR; P9WQE7; -.
DR STRING; 83332.Rv2931; -.
DR iPTMnet; P9WQE7; -.
DR PaxDb; 83332-Rv2931; -.
DR GeneID; 888183; -.
DR KEGG; mtu:Rv2931; -.
DR PATRIC; fig|83332.111.peg.3261; -.
DR TubercuList; Rv2931; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; P9WQE7; -.
DR OrthoDB; 9778690at2; -.
DR PhylomeDB; P9WQE7; -.
DR UniPathway; UPA00094; -.
DR PHI-base; PHI:7220; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0034081; C:polyketide synthase complex; ISS:UniProtKB.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:MTBBASE.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:MTBBASE.
DR GO; GO:0000036; F:acyl carrier activity; IDA:MTBBASE.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IDA:MTBBASE.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0097041; P:phenolic phthiocerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0097040; P:phthiocerol biosynthetic process; ISS:UniProtKB.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Fatty acid metabolism; Lipid metabolism;
KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..1876
FT /note="Phenolphthiocerol/phthiocerol polyketide synthase
FT subunit A"
FT /id="PRO_0000180301"
FT DOMAIN 9..83
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 101..526
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 997..1267
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 1759..1836
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 626..950
FT /note="Acyltransferase"
FT /evidence="ECO:0000250"
FT REGION 997..1112
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1102..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1267
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1491..1728
FT /note="Beta-ketoacyl reductase"
FT /evidence="ECO:0000250"
FT COMPBIAS 1102..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 408
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 448
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 720
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1027
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1186
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT BINDING 1491..1551
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MOD_RES 43
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1796
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1876 AA; 198835 MW; D9783DBD48792110 CRC64;
MTGSISGEAD LRHWLIDYLV TNIGCTPDEV DPDLSLADLG VSSRDAVVLS GELSELLGRT
VSPIDFWEHP TINALAAYLA APEPSPDSDA AVKRGARNSL DEPIAVVGMG CRFPGGISCP
EALWDFLCER RSSISQVPPQ RWQPFEGGPP EVAAALARTT RWGSFLPDID AFDAEFFEIS
PSEADKMDPQ QRLLLEVAWE ALEHAGIPPG TLRRSATGVF AGACLSEYGA MASADLSQVD
GWSNSGGAMS IIANRLSYFL DLRGPSVAVD TACSSSLVAI HLACQSLRTQ DCHLAIAAGV
NLLLSPAVFR GFDQVGALSP TGQCRAFDAT ADGFVRGEGA GVVVLKRLTD AQRDGDRVLA
VICGSAVNQD GRSNGLMAPN PAAQMAVLRA AYTNAGMQPS EVDYVEAHGT GTLLGDPIEA
RALGTVLGRG RPEDSPLLIG SVKTNLGHTE AAAGIAGFIK TVLAVQHGQI PPNQHFETAN
PHIPFTDLRM KVVDTQTEWP ATGHPRRAGV SSFGFGGTNA HVVIEQGQEV RPAPGQGLSP
AVSTLVVAGK TMQRVSATAG MLADWMEGPG ADVALADVAH TLNHHRSRQP KFGTVVARDR
TQAIAGLRAL AAGQHAPGVV NPADGSPGPG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAV
AELEPVFVEQ AGFSLHDVLA NGEELVGIEQ IQLGLIGMQL ALTELWCSYG VRPDLVIGHS
MGEVAAAVVA GALTPAEGLR VTATRSRLMA PLSGQGGMAL LELDAPTTEA LIADFPQVTL
GIYNSPRQTV IAGPTEQIDE LIARVRAQNR FASRVNIEVA PHNPAMDALQ PAMRSELADL
TPRTPTIGII STTYADLHTQ PVFDAEHWAT NMRNPVRFQQ AIASAGSGAD GAYHTFIEIS
AHPLLTQAII DTLHSAQPGA RYTSLGTLQR DTDDVVTFRT NLNKAHTIHP PHTPHPPEPH
PPIPTTPWQH TRHWITTKYP AGSVGSAPRA GTLLGQHTTV ATVSASPPSH LWQARLAPDA
KPYQGGHRFH QVEVVPASVV LHTILSAATE LGYSALSEVR FEQPIFADRP RLIQVVADNR
AISLASSPAA GTPSDRWTRH VTAQLSSSPS DSASSLNEHH RANGQPPERA HRDLIPDLAE
LLAMRGIDGL PFSWTVASWT QHSSNLTVAI DLPEALPEGS TGPLLDAAVH LAALSDVADS
RLYVPASIEQ ISLGDVVTGP RSSVTLNRTA HDDDGITVDV TVAAHGEVPS LSMRSLRYRA
LDFGLDVGRA QPPASTGPVE AYCDATNFVH TIDWQPQTVP DATHPGAEQV THPGPVAIIG
DDGAALCETL EGAGYQPAVM SDGVSQARYV VYVADSDPAG ADETDVDFAV RICTEITGLV
RTLAERDADK PAALWILTRG VHESVAPSAL RQSFLWGLAG VIAAEHPELW GGLVDLAIND
DLGEFGPALA ELLAKPSKSI LVRRDGVVLA PALAPVRGEP ARKSLQCRPD AAYLITGGLG
ALGLLMADWL ADRGAHRLVL TGRTPLPPRR DWQLDTLDTE LRRRIDAIRA LEMRGVTVEA
VAADVGCRED VQALLAARDR DGAAPIRGII HAAGITNDQL VTSMTGDAVR QVMWPKIGGS
QVLHDAFPPG SVDFFYLTAS AAGIFGIPGQ GSYAAANSYL DALARARRQQ GCHTMSLDWV
AWRGLGLAAD AQLVSEELAR MGSRDITPSE AFTAWEFVDG YDVAQAVVVP MPAPAGADGS
GANAYLLPAR NWSVMAATEV RSELEQGLRR IIAAELRVPE KELDTDRPFA ELGLNSLMAM
AIRREAEQFV GIELSATMLF NHPTVKSLAS YLAKRVAPHD VSQDNQISAL SSSAGSVLDS
LFDRIESAPP EAERSV
//
