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 03-AUG-2022, entry version 173.
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}.
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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 AlphaFoldDB; Q08787; -.
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; BSU_03510.
DR GeneID; 938308; -.
DR KEGG; bsu:BSU03510; -.
DR PATRIC; fig|224308.179.peg.368; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; Q08787; -.
DR OMA; IISPQAF; -.
DR PhylomeDB; Q08787; -.
DR BioCyc; BSUB:BSU03510-MON; -.
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: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; 3.30.300.30; -; 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; IPR045851; AMP-bd_C_sf.
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;
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:0007829|PDB:2VSQ"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 152..170
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 214..218
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 411..430
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 466..476
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 492..508
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 525..536
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 629..636
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 660..669
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 700..704
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 723..730
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 734..744
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 762..766
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 786..791
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 804..810
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 821..827
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 838..848
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 854..859
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 860..862
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 869..872
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 873..882
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 883..885
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 888..894
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 902..908
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 915..925
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 928..930
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 933..939
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 959..962
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 972..985
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 996..1000
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 1003..1012
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 1026..1028
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 1032..1041
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 1044..1046
FT /evidence="ECO:0007829|PDB:2VSQ"
FT TURN 1047..1049
FT /evidence="ECO:0007829|PDB:2VSQ"
FT STRAND 1050..1054
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1058..1064
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1071..1074
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1075..1080
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1084..1089
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1097..1108
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1114..1119
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1121..1135
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1140..1147
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1166..1172
FT /evidence="ECO:0007829|PDB:1JMK"
FT TURN 1173..1175
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1178..1180
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1182..1201
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1208..1216
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1225..1228
FT /evidence="ECO:0007829|PDB:2VSQ"
FT HELIX 1231..1233
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1234..1236
FT /evidence="ECO:0007829|PDB:1JMK"
FT STRAND 1238..1242
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1247..1249
FT /evidence="ECO:0007829|PDB:1JMK"
FT HELIX 1253..1267
FT /evidence="ECO:0007829|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
