ID   MYCA_BACIU              Reviewed;        3971 AA.
AC   Q9R9J1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Mycosubtilin synthase subunit A;
DE            EC=2.3.1.-;
DE   Includes:
DE     RecName: Full=Glutamate-1-semialdehyde aminotransferase;
DE              Short=GSA-AT;
DE   Includes:
DE     RecName: Full=ATP-dependent asparagine adenylase 1;
DE              Short=AsnA 1;
DE     AltName: Full=Asparagine activase 1;
GN   Name=mycA;
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA   Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W.,
RA   Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA   Vater J.;
RT   "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT   multifunctional hybrid between a peptide synthetase, an amino transferase,
RT   and a fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
RN   [2]
RP   FUNCTION, AND COFACTOR OF AMINOTRANSFERASE DOMAIN.
RX   PubMed=16248612; DOI=10.1021/ja055247g;
RA   Aron Z.D., Dorrestein P.C., Blackhall J.R., Kelleher N.L., Walsh C.T.;
RT   "Characterization of a new tailoring domain in polyketide biogenesis: the
RT   amine transferase domain of MycA in the mycosubtilin gene cluster.";
RL   J. Am. Chem. Soc. 127:14986-14987(2005).
CC   -!- FUNCTION: This protein is a multifunctional enzyme, able to activate a
CC       long chain fatty acid and link it with the amino acid Asn as part of
CC       the synthesis of mycosubtilin. The activation sites consist of
CC       individual domains. {ECO:0000269|PubMed:16248612}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:16248612};
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF184956; AAF08795.1; -; Genomic_DNA.
DR   PIR; T44806; T44806.
DR   PDB; 6KFM; X-ray; 1.70 A; A/B=1470-1930.
DR   PDB; 6KFR; X-ray; 3.10 A; A/B=1470-1930.
DR   PDB; 6KFU; X-ray; 2.20 A; A=1282-1370, A=1470-1930.
DR   PDBsum; 6KFM; -.
DR   PDBsum; 6KFR; -.
DR   PDBsum; 6KFU; -.
DR   SMR; Q9R9J1; -.
DR   STRING; 483913.AN935_09470; -.
DR   SABIO-RK; Q9R9J1; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05908; A_NRPS_MycA_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 3.
DR   CDD; cd00610; OAT_like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 4.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 4.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 4.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein; Pyridoxal phosphate; Repeat;
KW   Transferase.
FT   CHAIN           1..3971
FT                   /note="Mycosubtilin synthase subunit A"
FT                   /id="PRO_0000360848"
FT   DOMAIN          578..653
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          669..1092
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          1290..1365
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2405..2480
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3442..3517
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          160..479
FT                   /note="Acyl-CoA ligase"
FT   REGION          1434..1456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1529..1856
FT                   /note="GSA-AT"
FT   REGION          1921..1942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1938..2240
FT                   /note="Condensation 1"
FT   REGION          2492..2781
FT                   /note="Condensation 2"
FT   REGION          2937..3823
FT                   /note="Domain 1 (asparagine-activating)"
FT   REGION          2967..3364
FT                   /note="Adenylation 1"
FT   REGION          3529..3818
FT                   /note="Condensation 3"
FT   ACT_SITE        843
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        974
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        1014
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   MOD_RES         613
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1324
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1759
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2440
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3477
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   HELIX           1288..1304
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1308..1310
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   STRAND          1313..1315
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1317..1320
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1324..1337
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1344..1348
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1354..1361
FT                   /evidence="ECO:0007829|PDB:6KFU"
FT   HELIX           1478..1494
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1496..1505
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   TURN            1506..1508
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1512..1515
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1520..1525
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1530..1536
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1538..1541
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1546..1551
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1552..1555
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1564..1575
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1581..1587
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1588..1599
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1602..1609
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1610..1625
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1629..1633
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1642..1644
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1658..1661
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1666..1669
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1672..1675
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1680..1689
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1690..1692
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1693..1698
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1711..1724
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1727..1731
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   TURN            1733..1738
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1743..1748
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1753..1758
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1759..1762
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1768..1772
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1774..1781
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1787..1790
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1796..1798
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   TURN            1805..1808
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1810..1826
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1828..1851
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1855..1861
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   STRAND          1864..1871
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1873..1882
FT                   /evidence="ECO:0007829|PDB:6KFM"
FT   HELIX           1901..1920
FT                   /evidence="ECO:0007829|PDB:6KFM"
SQ   SEQUENCE   3971 AA;  449268 MW;  C8BF27D87F10065B CRC64;
     MYTSQFQTLV DVIRNRSNIS DRGIRFIESD KIETFVSYRQ LFDEAQGFLG YLQHIGIQPK
     QEIVFQIQEN KSFVVAFWAC LLGGMIPVPV SIGEDNDHKL KVWRIWNILN NPFLLASETV
     LDKMKKFAAD HDLQDFHHQL IEKSDIIQDR IYDHPASQYE PEADELAFIQ FSSGSTGDPK
     GVMLTHHNLI HNTCAIRNAL AIDLKDTLLS WMPLTHDMGL IACHLVPALA GINQNLMPTE
     LFIRRPILWM KKAHEHKASI LSSPNFGYNY FLKFLKDNKS YDWDLSHIRV IANGAEPILP
     ELCDEFLTRC AAFNMKRSAI LNVYGLAEAS VGATFSNIGE RFVPVYLHRD HLNLGERAVE
     VSKEDQNCAS FVEVGKPIDY CQIRICNEAN EGLEDGFIGH IQIKGENVTQ GYYNNPESTN
     RALTPDGWVK TGDLGFIRKG NLVVTGREKD IIFVNGKNVY PHDIERVAIE LEDIDLGRVA
     ACGVYDQETR SREIVLFAVY KKSADRFAPL VKDIKKHLYQ RGGWSIKEIL PIRKLPKTTS
     GKVKRYELAE QYESGKFALE STKIKEFLEG HSTEPVQTPI HEIETALLSI FSEVMDGKKI
     HLNDHYFDMG ATSLQLSQIA ERIEQKFGCE LTVADLFTYP SIADLAAFLV ENHSEIKQTD
     TAKPSRSSSK DIAIIGMSLN VPGASNKSDF WHLLENGEHG IREYPAPRVK DAIDYLRSIK
     SERNEKQFVR GGYLDEIDRF DYSFFGLAPK TAKFMDPNQR LFLQSAWHAI EDAGYAGDTI
     SGSQLGVYVG YSKVGYDYER LLSANYPEEL HHYIVGNLPS VLASRIAYFL NLKGPAVTVD
     TACSSSLVAV HMACKALLTG DCEMALAGGI RTSLLPMRIG LDMESSDGLT KTFSKDSDGT
     GSGEGVAAVL LKPLQAAIRD GDHIYGVIKG SAINQDGTTV GITAPSPAAQ TEVIEMAWKD
     AGIAPETLSF IEAHGTGTKL GDPVEFNGLC KAFEKVTEKK QFCAIGSVKA NIGHLFEAAG
     IVGLIKSALM LNHKKIPPLA HFNKPNPLIP FHSSPFYVNQ EVMDFTPEDR PLRGGISSFG
     FSGTNAHVVL EEYTPESEYA PEDGNDPHLF VLSAHTEASL YELTHQYRQY ISDDSQSSLR
     SICYTASTGR AHLDYCLAMI VSSNQELIDK LTSLIQGERN LPQVHFGYKN IKEMQPAEKD
     NLSKQISDLM QHRPCTKDER ITWLNRIAEL YVQRAVIDWR AVYSNEVVQK TPLPLYPFER
     NRCWVEAVYE SAKERKEKGE VALDINHTKT HIESFLKTVI SNASGIRADE IDSNAHFIGF
     GLDSIMLTQV KKAIADEFNV DIPMERFFDT MNNIESVVDY LAENVPSAAS TPPQESVTAQ
     EELVISGAQP ELEHQEHMLD KIIASQNQLI QQTLQAQLDS FNLLRNNSHF VSKESEISQD
     KTSLSPKSVT AKKNSAQEAK PYIPFQRQTL NEQVNYTPQQ RQYLESFIEK YVDKTKGSKQ
     YTDETRFAHA NNRNLSSFRS YWKEMVYPII AERSDGSRMW DIDGNEYIDI TMGFGVNLFG
     HHPSFITQTV VDSTHSALPP LGPMSNVAGE VADRIRACTG VERVAFYNSG TEAVMVALRL
     ARAATGRTKV VVFAGSYHGT FDGVLGVANT KGGAEPANPL APGIPQSFMN DLIILHYNHP
     DSLDVIRNLG NELAAVLVEP VQSRRPDLQP ESFLKELRAI TQQSGTALIM DEIITGFRIG
     LGGAQEWFDI QADLVTYGKI IGGGQPLGIV AGKAEFMNTI DGGTWQYGDD SYPTDEAKRT
     FVAGTFNTHP LTMRMSLAVL RYLQAEGETL YERLNQKTTY LVDQLNSYFE QSQVPIRMVQ
     FGSLFRFVSS VDNDLFFYHL NYKGVYVWEG RNCFLSTAHT SDDIAYIIQA VQETVKDLRR
     GGFIPEGPDS PNDGGHKEPE TYELSPEQKQ LAVVSQYGND ASAALNQSIM LKVKGAVQHT
     LLKQAVRNIV KRHDALRTVI HVDDEVQQVQ ARINVEIPII DFTGYPNEQR ESEVQKWLTE
     DAKRPFHFHE QKPLFRVHVL TSKQDEHLIV LTFHHIIADG WSIAVFVQEL ESTYAAIVQG
     SPLPSHEVVS FRQYLDWQQA QIENGHYEEG IRYWRQYLSE PIPQAILTSM SSSRYPHGYE
     GDRYTVTLDR PLSKAIKSLS IRMKNSVFAT ILGAFHLFLQ QLTKQAGLVI GIPTAGQLHM
     KQPMLVGNCV NMVPVKNTAS SESTLADYLG HMKENMDQVM RHQDVPMTLV ASQLPHDQMP
     DMRIIFNLDR PFRKLHFGQM EAELIAYPIK CISYDLFLNV TEFDQEYVLD FDFNTSVISS
     EIMNKWGTGF VNLLKKMVEG DSASLDSLKM FSKEDQHDLL ELYADHQLRI SSTLDHKGVR
     AVYEEPENET ELQIAQIWAE LLGLEKVGRS DHFLSLGGNS LKATLMLSKI QQTFNQKVSI
     GQFFSHQTVK ELANFIRGEK NVKYPPMKPV EQKAFYRTSP AQQRVYFLHQ MEPNQVSQNM
     FGQISIIGKY DEKALIASLQ QVMQRHEAFR TSFHIIDGEI VQQIAGELDF NVRVHSMDRE
     EFEAYADGYV KPFRLEQAPL VRAELIKVDN EQAELLIDMH HIISDGYSMS ILTNELFALY
     HGNPLPEIPF EYKDFAEWQN QLLIGEVMEQ QEEYWLEQFK QEVPILQLPA DGSRAMEWSS
     EGQRVTCSLQ SSLIRSLQEM AQQKGTTLYM VLLAAYNVLL HKYTGQEDIV VGTPVSGRNQ
     PNIESMIGIF IQTMGIRTKP QANKRFTDYL DEVKRQTLDA FENQDYPFDW LVEKVNVQRE
     TTGKSLFNTM FVYQNIEFQE IHQDGCTFRV KERNPGVSLY DLMLTIEDAE KQLDIHFDFN
     PNQFEQETIE QIIRHYTSLL DSLVKEPEKS LSSVPMLSDI ERHQLLMGCN DTETPFPHND
     TVCQWFETQA EQRPDDEAVI FGNERCTYGQ LNERVNQLAR TLRTKGVQAD QFVAIICPHR
     IELIVGILAV LKAGGAYVPI DPEYPEDRIQ YMLKDSEAKI VLAQLDLHKH LTFDADVVLL
     DEESSYHEDR SNLEPTCGAN DLAYMIYTSG STGNPKGVLI EHRGLANYIE WAKEVYVNDE
     KTNFPLYSSI SFDLTVTSIF TPLVTGNTII VFDGEDKSAV LSTIMQDPRI DIIKLTPAHL
     HVLKEMKIAD GTTIRKMIVG GENLSTRLAQ SVSEQFKGQL DIFNEYGPTE AVVGCMIYRY
     DTKRDRREFV PIGSPAANTS IYVLDASMNL VPVGVPGEMY IGGAGVARGY WNRPDLTAEK
     FVHNPFAPGT IMYKTGDLAK RLRDGNLIYL GRIDEQVKIR GHRIELGEVE AAMHKVEAVQ
     KAVVLAREEE DGLQQLCAYY VSNKPITIAE IREQLSLELP DYMVPSHYIQ LEQLPLTSNG
     KINRKALPAP EVSLEQIAEY VPPGNEVESK LAVLWQEMLG IHRVGIKHNF FDLGGNSIRA
     TALAARIHKE LDVNLSVKDI FKFPTIEQLA NMALRMEKIR YVSIPSAQKI SYYPVSSAQK
     RMYLLSHTEG GELTYNMTGA MSVEGAIDLE RLTAAFQKLI ERHEVLRTSF ELYEGEPAQR
     IHPSIEFTIE QIQAREEEVE DHVLDFIKSF DLAKPPLMRV GLIELTPEKH VLLVDMHHII
     SDGVSMNILM KDLNQFYKGI EPDPLPIQYK DYAVWQQTEA QRQNIKKQEA YWLNRFHDEI
     PVLDMPTDYE RPAIRDYEGE SFEFLIPIEL KQRLSQMEEA TGTTLYMILM AAYTILLSKY
     SGQEDIVVGT PVSGRSHMDV ESVVGMFVNT LVIRNHPAGR KIFEDYLNEV KENMLNAYQN
     QDYPLEELIQ HVHLLKDSSR NPLFDTMFVL QNLDQVELNL DSLRFTPYKL HHTVAKFDLT
     LSIQTDQDKH HGLFEYSKKL FKKSRIEALS KDYLHILSVI SQQPSIQIEH IELSGSTAED
     DNLIHSIELN F
//