(data stored in SCRATCH zone)

SWISSPROT: SRFAC_BACSU

ID   SRFAC_BACSU             Reviewed;        1275 AA.
AC   Q08787;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 164.
DE   RecName: Full=Surfactin synthase subunit 3;
GN   Name=srfAC; Synonyms=srfA3; OrderedLocusNames=BSU03510;
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 / 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   [2]
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   [3]
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   [4]
RP   SEQUENCE REVISION TO 26; 33 AND 1010-1015.
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   PHOSPHOPANTETHEINYLATION [LARGE SCALE ANALYSIS] AT SER-1003, 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).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1042-1271.
RX   PubMed=12005429; DOI=10.1016/s0969-2126(02)00716-5;
RA   Bruner S.D., Weber T., Kohli R.M., Schwarzer D., Marahiel M.A., Walsh C.T.,
RA   Stubbs M.T.;
RT   "Structural basis for the cyclization of the lipopeptide antibiotic
RT   surfactin by the thioesterase domain SrfTE.";
RL   Structure 10:301-310(2002).
CC   -!- FUNCTION: Probably activates a leucine.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC       Note=Binds 1 phosphopantetheine 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-1003 in PubMed:17218307 may
CC       result from the secondary neutral loss of pantetheine from the
CC       phosphodiester linked cofactor. {ECO:0000305}.
DR   EMBL; X70356; CAA49818.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08985.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12145.2; -; Genomic_DNA.
DR   PIR; I40487; I40487.
DR   RefSeq; NP_388233.2; NC_000964.3.
DR   RefSeq; WP_003234570.1; NZ_JNCM01000031.1.
DR   PDB; 1JMK; X-ray; 1.71 A; C/O=1042-1271.
DR   PDB; 2VSQ; X-ray; 2.60 A; A=1-1275.
DR   PDBsum; 1JMK; -.
DR   PDBsum; 2VSQ; -.
DR   SMR; Q08787; -.
DR   IntAct; Q08787; 2.
DR   MINT; Q08787; -.
DR   STRING; 224308.BSU03510; -.
DR   ESTHER; bacsu-srfac; Thioesterase.
DR   jPOST; Q08787; -.
DR   PaxDb; Q08787; -.
DR   PRIDE; Q08787; -.
DR   EnsemblBacteria; CAB12145; CAB12145; BSU03510.
DR   GeneID; 938308; -.
DR   KEGG; bsu:BSU03510; -.
DR   PATRIC; fig|224308.179.peg.368; -.
DR   eggNOG; COG3319; LUCA.
DR   HOGENOM; HOG000229993; -.
DR   InParanoid; Q08787; -.
DR   KO; K15656; -.
DR   OMA; IISPQAF; -.
DR   PhylomeDB; Q08787; -.
DR   BioCyc; BSUB:BSU03510-MONOMER; -.
DR   SABIO-RK; Q08787; -.
DR   UniPathway; UPA00181; -.
DR   EvolutionaryTrace; Q08787; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR   GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q08787.
DR   SWISS-2DPAGE; Q08787.
KW   3D-structure; Antibiotic biosynthesis; Ligase; Phosphopantetheine;
KW   Phosphoprotein; Reference proteome; Sporulation.
FT   CHAIN           1..1275
FT                   /note="Surfactin synthase subunit 3"
FT                   /id="PRO_0000193101"
FT   DOMAIN          968..1043
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1059..1271
FT                   /note="Thioesterase"
FT   ACT_SITE        1120
FT   ACT_SITE        1147
FT   ACT_SITE        1247
FT   MOD_RES         1003
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:17218307"
FT   CONFLICT        26
FT                   /note="A -> P (in Ref. 1; CAA49818 and 2; BAA08985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="S -> T (in Ref. 1; CAA49818 and 2; BAA08985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1010..1015
FT                   /note="ASRIKK -> VPHQQ (in Ref. 1; CAA49818 and 2;
FT                   BAA08985)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..8
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          9..14
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           17..28
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          36..45
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           49..62
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           64..67
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          68..71
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          79..84
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          90..94
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           100..117
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            121..123
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          126..135
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          138..146
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           147..149
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           152..170
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           184..191
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           195..206
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            214..218
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          228..233
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           237..249
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           254..270
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          273..281
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           291..293
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          300..307
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           314..328
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           329..331
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           336..341
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          342..344
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          346..348
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          352..355
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           360..363
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           368..371
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          372..380
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          386..393
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          395..397
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          399..405
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            406..408
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           411..430
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           436..438
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           444..451
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            452..454
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           466..476
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          480..487
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          489..491
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           492..508
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          516..519
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           525..536
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          540..543
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           550..560
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          564..567
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          582..588
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           590..594
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          608..615
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          618..621
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          623..628
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           629..636
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          649..652
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           660..669
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            670..672
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          674..677
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           680..682
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           686..696
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          700..704
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           705..714
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           717..720
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          723..730
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           734..744
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          749..753
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           756..758
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          762..766
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          780..782
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          786..791
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          804..810
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           821..827
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          828..830
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          838..848
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          854..859
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           860..862
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          863..866
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          869..872
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           873..882
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          883..885
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          888..894
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          897..899
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          902..908
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          910..913
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           915..925
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           928..930
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          933..939
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           959..962
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           972..985
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            996..1000
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           1003..1012
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          1013..1015
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            1026..1028
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           1032..1041
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          1044..1046
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   TURN            1047..1049
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   STRAND          1050..1054
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1058..1064
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1071..1074
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1075..1080
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1084..1089
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1097..1108
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1114..1119
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1121..1135
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1140..1147
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1166..1172
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   TURN            1173..1175
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1178..1180
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1182..1201
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1208..1216
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1225..1228
FT                   /evidence="ECO:0000244|PDB:2VSQ"
FT   HELIX           1231..1233
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1234..1236
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   STRAND          1238..1242
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1247..1249
FT                   /evidence="ECO:0000244|PDB:1JMK"
FT   HELIX           1253..1267
FT                   /evidence="ECO:0000244|PDB:1JMK"
SQ   SEQUENCE   1275 AA;  143872 MW;  C17C1685127BAF56 CRC64;
     MSQFSKDQVQ DMYYLSPMQE GMLFHAILNP GQSFYLEQIT MKVKGSLNIK CLEESMNVIM
     DRYDVFRTVF IHEKVKRPVQ VVLKKRQFHI EEIDLTHLTG SEQTAKINEY KEQDKIRGFD
     LTRDIPMRAA IFKKAEESFE WVWSYHHIIL DGWCFGIVVQ DLFKVYNALR EQKPYSLPPV
     KPYKDYIKWL EKQDKQASLR YWREYLEGFE GQTTFAEQRK KQKDGYEPKE LLFSLSEAET
     KAFTELAKSQ HTTLSTALQA VWSVLISRYQ QSGDLAFGTV VSGRPAEIKG VEHMVGLFIN
     VVPRRVKLSE GITFNGLLKR LQEQSLQSEP HQYVPLYDIQ SQADQPKLID HIIVFENYPL
     QDAKNEESSE NGFDMVDVHV FEKSNYDLNL MASPGDEMLI KLAYNENVFD EAFILRLKSQ
     LLTAIQQLIQ NPDQPVSTIN LVDDREREFL LTGLNPPAQA HETKPLTYWF KEAVNANPDA
     PALTYSGQTL SYRELDEEAN RIARRLQKHG AGKGSVVALY TKRSLELVIG ILGVLKAGAA
     YLPVDPKLPE DRISYMLADS AAACLLTHQE MKEQAAELPY TGTTLFIDDQ TRFEEQASDP
     ATAIDPNDPA YIMYTSGTTG KPKGNITTHA NIQGLVKHVD YMAFSDQDTF LSVSNYAFDA
     FTFDFYASML NAARLIIADE HTLLDTERLT DLILQENVNV MFATTALFNL LTDAGEDWMK
     GLRCILFGGE RASVPHVRKA LRIMGPGKLI NCYGPTEGTV FATAHVVHDL PDSISSLPIG
     KPISNASVYI LNEQSQLQPF GAVGELCISG MGVSKGYVNR ADLTKEKFIE NPFKPGETLY
     RTGDLARWLP DGTIEYAGRI DDQVKIRGHR IELEEIEKQL QEYPGVKDAV VVADRHESGD
     ASINAYLVNR TQLSAEDVKA HLKKQLPAYM VPQTFTFLDE LPLTTNGKVN KRLLPKPDQD
     QLAEEWIGPR NEMEETIAQI WSEVLGRKQI GIHDDFFALG GHSLKAMTAA SRIKKELGID
     LPVKLLFEAP TIAGISAYLK NGGSDGLQDV TIMNQDQEQI IFAFPPVLGY GLMYQNLSSR
     LPSYKLCAFD FIEEEDRLDR YADLIQKLQP EGPLTLFGYS AGCSLAFEAA KKLEEQGRIV
     QRIIMVDSYK KQGVSDLDGR TVESDVEALM NVNRDNEALN SEAVKHGLKQ KTHAFYSYYV
     NLISTGQVKA DIDLLTSGAD FDMPEWLASW EEATTGVYRV KRGFGTHAEM LQGETLDRNA
     EILLEFLNTQ TVTVS
//

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