(data stored in ACNUC7421 zone)

SWISSPROT: SRFAA_BACSU

ID   SRFAA_BACSU             Reviewed;        3587 AA.
AC   P27206;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 4.
DT   11-DEC-2019, entry version 149.
DE   RecName: Full=Surfactin synthase subunit 1;
GN   Name=srfAA; Synonyms=srfA, srfA1; OrderedLocusNames=BSU03480;
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;
RX   PubMed=8441623; DOI=10.1093/nar/21.1.93;
RA   Fuma S., Fujishima Y., Corbell N., D'Souza C., Nakano M.M., Zuber P.,
RA   Yamane K.;
RT   "Nucleotide sequence of 5' portion of srfA that contains the region
RT   required for competence establishment in Bacillus subtilis.";
RL   Nucleic Acids Res. 21:93-97(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
RA   Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M., Venema G.,
RA   van Sinderen D.;
RT   "Sequence and analysis of the genetic locus responsible for surfactin
RT   synthesis in Bacillus subtilis.";
RL   Mol. Microbiol. 8:821-831(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [4]
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   [5]
RP   SEQUENCE REVISION.
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-460.
RX   PubMed=1847909; DOI=10.1128/jb.173.5.1770-1778.1991;
RA   Nakano M.M., Magnuson R., Myers A.M., Curry J., Grossman A.D., Zuber P.;
RT   "srfA is an operon required for surfactin production, competence
RT   development, and efficient sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 173:1770-1778(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC   STRAIN=168;
RX   PubMed=7704255; DOI=10.1099/13500872-141-2-277;
RA   Fujishima Y., Yamane K.;
RT   "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT   srfAA of the Bacillus subtilis chromosome.";
RL   Microbiology 141:277-279(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX   PubMed=1715856; DOI=10.1128/jb.173.17.5487-5493.1991;
RA   Nakano M.M., Xia L., Zuber P.;
RT   "Transcription initiation region of the srfA operon, which is controlled by
RT   the comP-comA signal transduction system in Bacillus subtilis.";
RL   J. Bacteriol. 173:5487-5493(1991).
RN   [9]
RP   PHOSPHOPANTETHEINYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
CC   -!- FUNCTION: This protein is a multifunctional enzyme able to activate and
CC       polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for
CC       these AA consist of individual domains.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC       Note=Binds 3 phosphopantetheines covalently.;
CC   -!- PATHWAY: Antibiotic biosynthesis; surfactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The phosphoserine observed at Ser-1006 in PubMed:17218307
CC       undoubtedly results from the secondary neutral loss of pantetheine from
CC       the phosphodiester linked cofactor. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA08982.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA49816.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; D13262; BAA02522.1; -; Genomic_DNA.
DR   EMBL; X70356; CAA49816.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; D50453; BAA08982.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB12142.2; -; Genomic_DNA.
DR   EMBL; M59939; AAA22815.1; -; Genomic_DNA.
DR   EMBL; D30762; BAA21034.1; -; Genomic_DNA.
DR   EMBL; M64702; AAA22816.1; -; Genomic_DNA.
DR   PIR; I40485; I40485.
DR   RefSeq; NP_388230.2; NC_000964.3.
DR   RefSeq; WP_010886402.1; NZ_CP019663.1.
DR   SMR; P27206; -.
DR   IntAct; P27206; 4.
DR   MINT; P27206; -.
DR   STRING; 224308.BSU03480; -.
DR   jPOST; P27206; -.
DR   PaxDb; P27206; -.
DR   PRIDE; P27206; -.
DR   EnsemblBacteria; CAB12142; CAB12142; BSU03480.
DR   GeneID; 938306; -.
DR   KEGG; bsu:BSU03480; -.
DR   PATRIC; fig|224308.179.peg.366; -.
DR   eggNOG; ENOG4105CEY; Bacteria.
DR   eggNOG; COG0318; LUCA.
DR   HOGENOM; HOG000229991; -.
DR   InParanoid; P27206; -.
DR   KO; K15654; -.
DR   OMA; NRQHWNQ; -.
DR   PhylomeDB; P27206; -.
DR   BioCyc; BSUB:BSU03480-MONOMER; -.
DR   UniPathway; UPA00181; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.30.559.10; -; 4.
DR   Gene3D; 3.40.50.12780; -; 3.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 3.
DR   Pfam; PF13193; AMP-binding_C; 3.
DR   Pfam; PF00668; Condensation; 4.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR   PROSITE; PS00455; AMP_BINDING; 3.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   1: Evidence at protein level;
DR   PRODOM; P27206.
DR   SWISS-2DPAGE; P27206.
KW   Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Sporulation.
FT   CHAIN           1..3587
FT                   /note="Surfactin synthase subunit 1"
FT                   /id="PRO_0000193099"
FT   DOMAIN          971..1046
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2010..2085
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3038..3112
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          ?..1047
FT                   /note="Domain 1 (glutamate-activating)"
FT   REGION          ?..2086
FT                   /note="Domain 2 (leucine-activating)"
FT   REGION          ?..3114
FT                   /note="Domain 3 (D-leucine-activating)"
FT   MOD_RES         1006
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:17218307"
FT   MOD_RES         2045
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3073
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   CONFLICT        146
FT                   /note="I -> M (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="L -> V (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="G -> A (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="T -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="D -> T (in Ref. 6; AAA22815)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="P -> A (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="I -> Y (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639..640
FT                   /note="GS -> PT (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        644
FT                   /note="R -> P (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647..649
FT                   /note="LLA -> FLP (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1026
FT                   /note="L -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1132..1133
FT                   /note="DS -> VC (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1164
FT                   /note="A -> R (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1458
FT                   /note="L -> V (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1850
FT                   /note="S -> T (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1894
FT                   /note="D -> T (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1911
FT                   /note="R -> A (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1973..1980
FT                   /note="PAVFIQMD -> LRCLSKWT (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2052
FT                   /note="L -> P (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2218
FT                   /note="H -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2265..2266
FT                   /note="QQ -> HR (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2291
FT                   /note="L -> V (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2349
FT                   /note="S -> C (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2428
FT                   /note="R -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2611..2612
FT                   /note="AV -> RC (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2685
FT                   /note="E -> ENPE (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2755
FT                   /note="T -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2896..2897
FT                   /note="TA -> SP (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3025
FT                   /note="P -> N (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3096
FT                   /note="F -> N (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3271
FT                   /note="A -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3316
FT                   /note="R -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3451
FT                   /note="Y -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3483..3495
FT                   /note="DEMSDAGLFTRSE -> HQMSHPPFFTTSH (in Ref. 2; CAA49816
FT                   and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3499..3500
FT                   /note="GQ -> PH (in Ref. 2; CAA49816 and 3; BAA08982)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3507
FT                   /note="E -> R (in Ref. 1; BAA02522)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3587 AA;  402146 MW;  5CA8D98D71FD0A84 CRC64;
     MEITFYPLTD AQKRIWYTEK FYPHTSISNL AGIGKLVSAD AIDYVLVEQA IQEFIRRNDA
     MRLRLRLDEN GEPVQYISEY RPVDIKHTDT TEDPNAIEFI SQWSREETKK PLPLYDCDLF
     RFSLFTIKEN EVWFYANVHH VISDGISMNI LGNAIMHIYL ELASGSETKE GISHSFIDHV
     LSEQEYAQSK RFEKDKAFWN KQFESVPELV SLKRNASAGG SLDAERFSKD VPEALHQQIL
     SFCEANKVSV LSVFQSLLAA YLYRVSGQND VVTGTFMGNR TNAKEKQMLG MFVSTVPLRT
     NIDGGQAFSE FVKDRMKDLM KTLRHQKYPY NLLINDLRET KSSLTKLFTV SLEYQVMQWQ
     KEEDLAFLTE PIFSGSGLND VSIHVKDRWD TGKLTIDFDY RTDLFSREEI NMICERMITM
     LENALTHPEH TIDELTLISD AEKEKLLARA GGKSVSYRKD MTIPELFQEK AELLSDHPAV
     VFEDRTLSYR TLHEQSARIA NVLKQKGVGP DSPVAVLIER SERMITAIMG ILKAGGAYVP
     IDPGFPAERI QYILEDCGAD FILTESKVAA PEADAELIDL DQAIEEGAEE SLNADVNARN
     LAYIIYTSGT TGRPKGVMIE HRQVHHLVES LQQTIYQSGS QTLRMALLAP FHFDASVKQI
     FASLLLGQTL YIVPKKTVTN GAALTAYYRK NSIEATDGTP AHLQMLAAAG DFEGLKLKHM
     LIGGEGLSSV VADKLLKLFK EAGTAPRLTN VYGPTETCVD ASVHPVIPEN AVQSAYVPIG
     KALGNNRLYI LDQKGRLQPE GVAGELYIAG DGVGRGYLHL PELTEEKFLQ DPFVPGDRMY
     RTGDVVRWLP DGTIEYLGRE DDQVKVRGYR IELGEIEAVI QQAPDVAKAV VLARPDEQGN
     LEVCAYVVQK PGSEFAPAGL REHAARQLPD YMVPAYFTEV TEIPLTPSGK VDRRKLFALE
     VKAVSGTAYT APRNETEKAI AAIWQDVLNV EKAGIFDNFF ETGGHSLKAM TLLTKIHKET
     GIEIPLQFLF EHPTITALAE EADHRESKAF AVIEPAEKQE HYPLSLAQQR TYIVSQFEDA
     GVGYNMPAAA ILEGPLDIQK LERAFQGLIR RHESLRTSFV LENSTPRQKI HDSVDFNIEM
     IERGGRSDEA IMASFVRTFD LAKAPLFRIG LLGLEENRHM LLFDMHHLIS DGVSIGIMLE
     ELARIYKGEQ LPDLRLQYKD YAVWQSRQAA EGYKKDQAYW KEVFAGELPV LQLLSDYPRP
     PVQSFEGDRV SIKLDAGVKD RLNRLAEQNG ATLYMVMLSA YYTLLSKYTG QDDIIVGTPS
     AGRNHSDTEG IIGMFVNTLA IRSEVKQNET FTQLISRVRK RVLDAFSHQD YPFEWLVEDL
     NIPRDVSRHP LFDTMFSLQN ATEGIPAVGD LSLSVQETNF KIAKFDLTVQ ARETDEGIEI
     DVDYSTKLFK QSTADRLLTH FARLLEDAAA DPEKPISEYK LLSEEEAASQ IQQFNPGRTP
     YPKDKTIVQL FEEQAANTPD HTALQYEGES LTYRELNERA NRLARGILSL GAGEGRTAAV
     LCERSMDMIV SILAVLKSGS AYVPIDPEHP IQRMQHFFRD SGAKVLLTQR KLKALAEEAE
     FKGVIVLADE EESYHADARN LALPLDSAAM ANLTYTSGTT GTPKGNIVTH ANILRTVKET
     NYLSITEQDT ILGLSNYVFD AFMFDMFGSL LNGAKLVLIP KETVLDMARL SRVIERENIS
     ILMITTALFH LLVDLNPACL STLRKIMFGG ERASVEHVRK ALQTVGKGKL LHMYGPSEST
     VFATYHPVDE LEEHTLSVPI GKPVSNTEVY ILDRTGHVQP AGIAGELCVS GEGLVKGYYN
     RPELTEEKFV PHPFTSGERM YKTGDLARWL PNGDIEFIGR IDHQVKIRGQ RIELGEIEHQ
     LQTHDRVQES VVLAVDQGAG DKLLCAYYVG EGDISSQEMR EHAAKDLPAY MVPAVFIQMD
     ELPLTGNGKI DRRALPIPDA NVSRGVSYVA PRNGTEQKVA DIWAQVLQAE QVGAYDHFFD
     IGGHSLAGMK MLALVHQELG VELSLKDLFQ SPTVEGLAQV IASAEKGTAA SISPAEKQDT
     YPVSSPQKRM YVLQQLEDAQ TSYNMPAVLR LTGELDVERL NSVMQQLMQR HEALRTTFEI
     KDGETVQRIW EEAECEIAYF EAPEEETERI VSEFIKPFKI DQLPLFRIGL IKHSDTEHVL
     LFDMHHIISD GASVGVLIEE LSKLYDGETL EPLRIQYKDY AVWQQQFIQS ELYKKQEEHW
     LKELDGELPV LTLPTDYSRP AVQTFEGDRI AFSLEAGKAD ALRRLAKETD STLYMVLLAS
     YSAFLSKISG QDDIIVGSPV AGRSQADVSR VIGMFVNTLA LRTYPKGEKT FADYLNEVKE
     TALSAFDAQD YPLEDLIGNV QVQRDTSRNP LFDAVFSMQN ANIKDLTMKG IQLEPHPFER
     KTAKFDLTLT ADETDGGLTF VLEYNTALFK QETIERWKQY WMELLDAVTG NPNQPLSSLS
     LVTETEKQAL LEAWKGKALP VPTDKTVHQL FEETAQRHKD RPAVTYNGQS WTYGELNAKA
     NRLARILMDC GISPDDRVGV LTKPSLEMSA AVLGVLKAGA AFVPIDPDYP DQRIEYILQD
     SGAKLLLKQE GISVPDSYTG DVILLDGSRT ILSLPLDEND EENPETAVTA ENLAYMIYTS
     GTTGQPKGVM VEHHALVNLC FWHHDAFSMT AEDRSAKYAG FGFDASIWEM FPTWTIGAEL
     HVIEEAIRLD IVRLNDYFET NGVTITFLPT QLAEQFMELE NTSLRVLLTG GDKLKRAVKK
     PYTLVNNYGP TENTVVATSA EIHPEEGSLS IGRAIANTRV YILGEGNQVQ PEGVAGELCV
     AGRGLARGYL NREDETAKRF VADPFVPGER MYRTGDLVKW TGGGIEYIGR IDQQVKVRGY
     RIELSEIEVQ LAQLSEVQDA AVTAVKDKGG NTAIAAYVTP ESADIEALKS ALKETLPDYM
     IPAFWVTLNE LPVTANGKVD RKALPEPDIE AGSGEYKAPT TDMEELLAGI WQDVLGMSEV
     GVTDNFFSLG GDSIKGIQMA SRLNQHGWKL EMKDLFQHPT IEELTQYVER AEGKQADQGP
     VEGEVILTPI QRWFFEKNFT NKHHWNQSVM LHAKKGFDPE RVEKTLQALI EHHDALRMVY
     REGQEDVIQY NRGLEAASAQ LEVIQIEGQA ADYEDRIERE AERLQSSIDL QEGGLLKAGL
     FQAEDGDHLL LAIHHLVVDG VSWRILLEDF AAVYTQLEQG NEPVLPQKTH SFAEYAERLQ
     DFANSKAFLK EKEYWRQLEE QAVAAKLPKD RESGDQRMKH TKTIEFSLTA EETEQLTTKV
     HEAYHTEMND ILLTAFGLAM KEWTGQDRVS VHLEGHGREE IIEDLTISRT VGWFTSMYPM
     VLDMKHADDL GYQLKQMKED IRHVPNKGVG YGILRYLTAP EHKEDVAFSI QPDVSFNYLG
     QFDEMSDAGL FTRSELPSGQ SLSPETEKPN ALDVVGYIEN GKLTMSLAYH SLEFHEKTVQ
     TFSDSFKAHL LRIIEHCLSQ DGTELTPSDL GDDDLTLDEL DKLMEIF
//

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