SIDC_ASPFU
ID SIDC_ASPFU Reviewed; 4763 AA.
AC Q4WR82;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 23-FEB-2022, entry version 111.
DE RecName: Full=Nonribosomal peptide synthetase sidC {ECO:0000303|PubMed:15953695};
DE Short=NPRS sidC {ECO:0000303|PubMed:15953695};
DE EC=6.3.2.- {ECO:0000305|PubMed:17845073};
DE AltName: Full=Siderophore peptide synthetase C {ECO:0000303|PubMed:17845073};
GN Name=NRPS2 {ECO:0000303|PubMed:16962256};
GN Synonyms=sidC {ECO:0000303|PubMed:15953695}; ORFNames=AFUA_1G17200;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
RX PubMed=15504822; DOI=10.1084/jem.20041242;
RA Schrettl M., Bignell E., Kragl C., Joechl C., Rogers T., Arst H.N. Jr.,
RA Haynes K., Haas H.;
RT "Siderophore biosynthesis but not reductive iron assimilation is essential
RT for Aspergillus fumigatus virulence.";
RL J. Exp. Med. 200:1213-1219(2004).
RN [3]
RP FUNCTION.
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=16113265; DOI=10.1128/iai.73.9.5493-5503.2005;
RA Hissen A.H., Wan A.N., Warwas M.L., Pinto L.J., Moore M.M.;
RT "The Aspergillus fumigatus siderophore biosynthetic gene sidA, encoding L-
RT ornithine N(5)-oxygenase, is required for virulence.";
RL Infect. Immun. 73:5493-5503(2005).
RN [4]
RP DOMAIN, INDUCTION, AND FUNCTION.
RX PubMed=15953695; DOI=10.1016/j.femsle.2005.05.028;
RA Reiber K., Reeves E.P., Neville C.M., Winkler R., Gebhardt P., Kavanagh K.,
RA Doyle S.;
RT "The expression of selected non-ribosomal peptide synthetases in
RT Aspergillus fumigatus is controlled by the availability of free iron.";
RL FEMS Microbiol. Lett. 248:83-91(2005).
RN [5]
RP NOMENCLATURE.
RX PubMed=16962256; DOI=10.1016/j.gene.2006.07.008;
RA Cramer R.A. Jr., Stajich J.E., Yamanaka Y., Dietrich F.S., Steinbach W.J.,
RA Perfect J.R.;
RT "Phylogenomic analysis of non-ribosomal peptide synthetases in the genus
RT Aspergillus.";
RL Gene 383:24-32(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=17845073; DOI=10.1371/journal.ppat.0030128;
RA Schrettl M., Bignell E., Kragl C., Sabiha Y., Loss O., Eisendle M.,
RA Wallner A., Arst H.N. Jr., Haynes K., Haas H.;
RT "Distinct roles for intra- and extracellular siderophores during
RT Aspergillus fumigatus infection.";
RL PLoS Pathog. 3:1195-1207(2007).
RN [7]
RP REVIEW ON FUNCTION, AND DOMAIN.
RX PubMed=17464044; DOI=10.1099/mic.0.2006/006908-0;
RA Stack D., Neville C., Doyle S.;
RT "Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi.";
RL Microbiology 153:1297-1306(2007).
RN [8]
RP INDUCTION.
RX PubMed=18721228; DOI=10.1111/j.1365-2958.2008.06376.x;
RA Schrettl M., Kim H.S., Eisendle M., Kragl C., Nierman W.C., Heinekamp T.,
RA Werner E.R., Jacobsen I., Illmer P., Yi H., Brakhage A.A., Haas H.;
RT "SreA-mediated iron regulation in Aspergillus fumigatus.";
RL Mol. Microbiol. 70:27-43(2008).
RN [9]
RP FUNCTION.
RX PubMed=21622789; DOI=10.1128/aem.00182-11;
RA Blatzer M., Schrettl M., Sarg B., Lindner H.H., Pfaller K., Haas H.;
RT "SidL, an Aspergillus fumigatus transacetylase involved in biosynthesis of
RT the siderophores ferricrocin and hydroxyferricrocin.";
RL Appl. Environ. Microbiol. 77:4959-4966(2011).
RN [10]
RP FUNCTION.
RX PubMed=22106303; DOI=10.1073/pnas.1106399108;
RA Yasmin S., Alcazar-Fuoli L., Gruendlinger M., Puempel T., Cairns T.,
RA Blatzer M., Lopez J.F., Grimalt J.O., Bignell E., Haas H.;
RT "Mevalonate governs interdependency of ergosterol and siderophore
RT biosyntheses in the fungal pathogen Aspergillus fumigatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E497-E504(2012).
CC -!- FUNCTION: Nonribosomal peptide synthase; part of the siderophore
CC biosynthetic pathway (PubMed:17845073). Aspergillus fumigatus produces
CC four types of siderophores, low-molecular-mass iron chelators,
CC including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC)
CC for iron uptake; and intacellular ferricrocin (FC) for hyphal and
CC hydroxyferricrocin (HFC) for conidial iron distribution and storage.
CC TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-
CC hydroxyornithine residues cyclically linked by ester bonds; FC is a
CC cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-
CC hydroxyornithine)x3. The biosynthesis of all four siderophores depends
CC on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA
CC (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for
CC biosynthesis of extra- and intracellular siderophores split
CC (PubMed:17845073). For biosynthesis of extracellular siderophores, the
CC transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine
CC (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived
CC from mevalonate by CoA ligation and dehydration catalyzed by sidI and
CC sidH respectively (PubMed:22106303). The acetylation of N(5)-
CC hydroxyornithine for FC biosynthesis involves the constitutively
CC expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as
CC yet uncharacterized enzyme during conidiation (PubMed:17845073).
CC Assembly of fusarinine C (FsC) and FC is catalyzed by two different
CC nonribosomal peptide synthetases (NRPS), sidD and sidC respectively
CC (PubMed:15953695, PubMed:17845073, PubMed:17464044). Subsequently, sidG
CC catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073).
CC Both extra- and intracellular siderophores are crucial for growth
CC during iron limitation and virulence (PubMed:16113265).
CC {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:15953695,
CC ECO:0000269|PubMed:16113265, ECO:0000269|PubMed:17464044,
CC ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:21622789,
CC ECO:0000269|PubMed:22106303}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17845073}.
CC -!- INDUCTION: Expression is induced during iron starvation
CC (PubMed:15953695, PubMed:17845073). {ECO:0000269|PubMed:15953695,
CC ECO:0000269|PubMed:17845073}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D- amino acid conversion)
CC are present within the NRP synthetase. NRPS2 has the following
CC architecture: A-T-C-A-T-C-A-T-C-T-C-T-C. {ECO:0000269|PubMed:15953695,
CC ECO:0000269|PubMed:17464044}.
CC -!- DISRUPTION PHENOTYPE: Leads to a delay in both conidial swelling and
CC germ tube production during iron-depleted conditions (PubMed:17845073).
CC {ECO:0000269|PubMed:17845073}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AAHF01000004; EAL91050.1; -; Genomic_DNA.
DR RefSeq; XP_753088.1; XM_747995.1.
DR SMR; Q4WR82; -.
DR STRING; 746128.CADAFUBP00001627; -.
DR PRIDE; Q4WR82; -.
DR EnsemblFungi; EAL91050; EAL91050; AFUA_1G17200.
DR GeneID; 3510120; -.
DR KEGG; afm:AFUA_1G17200; -.
DR VEuPathDB; FungiDB:Afu1g17200; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000092_1_0_1; -.
DR InParanoid; Q4WR82; -.
DR OMA; ITMIGEK; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; 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:0006879; P:cellular iron ion homeostasis; IMP:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:AspGD.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IBA:GO_Central.
DR GO; GO:0031171; P:ferricrocin biosynthetic process; IMP:AspGD.
DR GO; GO:0019184; P:nonribosomal peptide biosynthetic process; ISM:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:AspGD.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:AspGD.
DR Gene3D; 1.10.1200.10; -; 5.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 5.
DR Gene3D; 3.40.50.12780; -; 3.
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; IPR042099; ANL_N_sf.
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 Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 5.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 5.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Virulence.
FT CHAIN 1..4763
FT /note="Nonribosomal peptide synthetase sidC"
FT /id="PRO_0000416543"
FT DOMAIN 853..930
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17464044"
FT DOMAIN 1979..2055
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17464044"
FT DOMAIN 3099..3175
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17464044"
FT DOMAIN 3647..3720
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17464044"
FT DOMAIN 4204..4277
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:17464044"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..815
FT /note="Adenylation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 1003..1396
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 1398..1951
FT /note="Adenylation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 2092..2423
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 2556..3070
FT /note="Adenylation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 3217..3626
FT /note="Condensation 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 3761..4093
FT /note="Condensation 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT REGION 4344..4593
FT /note="Condensation 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17464044"
FT MOD_RES 890
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2016
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3136
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3681
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4238
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4763 AA; 522418 MW; 7C5F60213B253FC8 CRC64;
MAGTANPADE GLTGPTETTN HINSARSDVA LGSSLSGIVP MTKIPALNTI DQFVAEGSPD
DLIGQSPWRR IGQGDVSGEL ATGLIEGYAR FVSALTGVED VAFAVLCQAS TRPSQALICA
SVTLTDQGRE VPSAWQCAVR ELDFSYYNRS EVQFALDLGL TGGPENRKAG LSTLAENDCL
SLYVRGSTDG LCISFTYPRR LIPEAAVSQL LKTITFHITQ TTGCLQSTGA WPDDPTPDLS
ILNFPPLMIP PSRDHDSATM PRHSKSFLLH SAFEGWAQKS PTSIALDFVH SLPSASTVAE
HSTLTYAALN AAATYLAIHI RSLLSDNTRN AGSRIIPVYM STSPELYISY LGILKAGYAF
CPIPTDAPPQ RVREIFQDID SSVILGDGEE PSSVSWFLSA AGEATSKPTW VNVAEVSRWK
HLSREDTEIA TEDRLFEPPD IDHNEIAYLL FTSGSTGKPK GVQVSHLAVT CSIESHATAI
PLPGTSAGDF RWFQFASPTF DPSLMEIFVT LSSGGTLCSA SRSLTLTDLE GTINEARATV
MMATPSLAAL LRPAQLTTLQ YLWTMGEKLN RTVIENFTQK AHSNDLNGDS VPALRLLVNA
YGPTEAAINC TFFAPVEYHT RGSIIGEPLP TCSIFVLDPA SHTPKPIPAG LAGELAIGGP
QVSQGYLNRP EETANSFVHS PEYGYLYRTG DLARIVWDEK GAQVIEFLGR ITSDQVKISG
RRVELGEIES VLATLTGVRE VVAVVPKRDA SVQGSEQIVA CIVADSLSED AAPEFVRLAD
ECAHRHLAAY MCPSSYVFFD SIPRTSSGKV DRNSISSMLQ QGKDSGMKFY MPSNDVPEAR
GMARAEWDPL EDEKALELRT LVLDLVAQTT GQDISVIKPN TSLYTLGLDS LGSMQFLQKL
RDKSLHNLSV GDVLQSNTVN GLLTLILNGK TNLRGLTNGQ LADDSRMSLA EHLQAFNDTN
LSRCAKRLSI SPERIQTVLP TTETQSGMLT SFLRTSTDSS FATRSYIYHS VISLEPHVDI
ERLKKAWESV IASYDSFRTR FCWIDDDMAP FAQCILKEDA ASAPMWAINH TFGDSMHEDS
LTRALREAEN TISLDSPWKL SLLESSGDKV IILSMFHGIF DGGSLQLLLE NVSSVYDGQL
PAPRTSLEHV VVNHFQANQT ATSNFWKEYL NKYSPIAFPS LTAYRPPAVN ATGCVEITPR
TTHDILKQQS RTIGSTPLSV LQAAWASLLL AYTGTQDHDV VMGSVISGRF DPDSEICIGP
TFTTIPTRLA LGQIPKAGGF WTNKSVVNHL ASLNAKALSH LQPRLGSLVT ADSKLPYDTV
LAYQDFSAGS STSSIWKSID HPPMANDYAV MIEVWPARDS SLTLRASFAL SQMDRDGAKV
MLHQLDDIIA FILQNPDGDF ENALLYTRPD LKASYNPMPK EADEVSDGDL IHTKFENHAN
SHPDDMALLF KYDLEDDGNL QNISWTYGEL NARADNLAAY LCETYDKLTN KVVPICIEKS
PAMYIAILGI LKAGGAWCPI DTFSPAQRRH DLIKRTGAGV LLVSSEDGEQ PKDAIPIGID
VVDVKKYADP LVSWPSVGRW SSKKLSSPAG LAYLIWTSGT TGAPKGVPIT HSAAVSCFRS
LKKDIPSDVS GGVVRCLQFS QYTFDVSIQD LFYTWSLGGV LISATREIML GSFAKLANTT
RATHAHLTPA FAAGVPRNSC ETLEVITMIG EKLTQHVADD WGTDMRAYNT YGPAEVTIVS
TVREFGNDCL NIKSANVGWP MESVSVFVTR NKQIVMKNAV GELALGGPQL SPGYLDQEDV
TKAKYVWSEE AGQILYYTGD LVRMLADGSL EFMNRVDDLV KIGGIRIELS EISFALGGCH
PLVENIETLY IDRPDRPSKV LVAFLSASNA TGADAGDDLL LLNDSALQIA LSTREKAHTA
LPAYMVPSVY LVMKRIPRTQ SAKTDRRALQ AAYASVDIED WENRMNPENN ATGHPTDDLV
ASDAMEKIVH MIASLINISP SIVAKASRLR SLGIDSIHAI RLASRLKEAG YRLSFIEVIN
CVTVQDLARL CTSSSEVDAL PAAEFDINLF NDQWHDIVAS KVDGEFFTVR ATPIQESLLS
ETMGTYNLYW SNHLFSLDKS VDVKRLKQAW LALCQKNEAL RTGFIPVAEV NNSSRKDDLD
FSILQVLHDH PTLDWEYVMC EDHEWDRLLH SRIEDVMKAH QKTYFKQPPW AVTVLDNGVE
RFMVLTMHHS IHDGPSLDLI ERDLRSAYID KPPSRYQLRS ALSKILPTDE MAAETRRFWS
SELQKYSELD APAWPDLTGK RKPETAVQEH NLISEQMRMT EPLEKLQSIS AELGVSSIAS
LIRAAWGFVS LSYLGVPAAV FAETVSDRIL HADLDNGIGP LISVVPVPFD PKGTAREVLA
EQQRISTQSR KYRHIHAREV RRMLNRPRGE PLYPAVFAFH PAGAEADGTT NPGLWHELED
RIGLHVEHPM AFNVLQNADS SLVLEVFSDA SLMSHEHLSI FVRQVDSLVS AMLANPDKEL
RELINHLPPS LRSKSSQHVS EAVRNSVTLS PTHWLELNAR EHPEWTAVEV ASSISASGIE
KQSMSYGTLN AAANCVAAFI ASVGYKNRMI AVCAGRNLPS YPVIVGVFKS GNTYLPIDNN
LPNDRKTFLI EDGNCPLVFT ETAFAATFSD VPETCRVLCI DHPSFVDSLA GMPTDNRAYA
SDPQDNAYLL YTSGSTGKPK GVMVSRANLS AFIESFSEFV CRVAPSTLEL GGRGRYLAQA
SRAFDVHLLE MFFAWRHGMA SVTAERTMLL DDLQLTITKW GITHASMVPS LVDQTNLRPE
LCPELKYLSV GGEKISKRVL DTWAGLPHVA LANAYGPTEV TIGCTFALVG KETTIRNIGP
PLSACTCHVL IPGTMDYALR GQTGELCFTG DIVGNGYLNR PDATGFVQGP DGEKMYRTGD
IGRLMSDDSV EYVGRGDDQT KIRGQRLELG EVSEVIRSSS PVQIGVVTTV TKHPGLARPQ
LISFIARSGD KSRQRSGDAT IIHSDLATLG KELRDACQRK LPAYMVPEII LPITFIPLAP
MSGKANIKEL HSMFSSLPLA SILQGNNPGT SDTAAFTDRP LSSDEEAVVS EICAVIKVER
ENINPLTNIF EIGLDSLSAI SLSVKLRRIG YDATVALVMG NPVVEQLAQL PRKSTEAVAD
PHSSDLTKRL AELETEYHKG YTRPANSGQV AVRPCLPLQE GLVARSINSE EDQLYVNHIA
LSFGPGLDSG RLRFAWQDTA DNSEILRTCF APLEKEIVQV VLTPGGAISW TEDEYDSLED
CIKEQRARQQ EISRGIIKNM TDVPPVRFHL ATLSSKRPLV LFIAIHHALY DGESFSMLLE
DVAARYVGEP VTRRGSPAAF IDHVYGQNLE KAQQHWVNAL SDCQPTIFRV DTGVVEETTF
INRKLHAGLA KLERHSADLH TTVPSLMQAL FALLLADRVN SSDVTYGLVL SGRAVAVPDA
ESVLLPCITT IPARLNTSGL KTVSDVVRSV HQSTARSLEY QHTSLRHIQR WLKSEKPLFD
CLFSYIRSTP APKNTLWGQL ESTMPSEYPL AVEIEANSEK DEMYVHCGFS PSFGSADRGQ
EFLEKLDALL SAFLFEDDIA LDSFSLANSG NPGSRATEVK WDATTWSATE TKIRDLTATF
CGLDVVNVSK GTSFISLGID SVTAIQFARK LRELQFEIVP SDIMRFPCVG ALAEHVDERS
SEGRQSARVG DKKPRVSLAA HRDNVPLLDD GDSVAAIFES TPLQAGMITR TLGSDTQVYV
HPHIVRLTEG VDIDRLSKAI SEVVAKNDIL RTSFHPIAEN GVTWVGAVHT NPPLQWKEIT
LPSNADVIAE LTSLYSFREV ADFETPPVRF VLVHRKNEKL FVVIMHHALY DGVSLPLLFE
ELAATYHGQT TVGRPQFSEI AHYIVEGQND SCDFWTKKLA GYEPVEIPAL SSSEATERML
LSERKIGLDV EKVVESCKSM EVTVQSVALL AYAKVLACLG GKRDVVFGQV LAGRSLPVPG
ADQTIGPLFN TVAQRVLFEP KFLSNREMAQ RVQQLTSESQ AFQHAPLKDV QRALRQEHGM
NAASLFDTLF VFQKSADLTT DTPHEQQIWT PFETEGYAAQ AEHKLNVEID HGREAIIVSG
SGDGRYICQQ ALDEFMADFC TAFQDIIEHP SRCATAAPER LGGLPLRLSN AEEPERGHSE
SDAPAHESII RDVLAEVSGV SVDSITPSTS IYNIGLDSLS AIRIASICRS RGLKAGVADV
LQGNTLRGIS ARIISPVEAP IQAREPLIKD HEAIEKAVLQ RLGLNKDEVE TILPCLSGQL
YHLVSWLKSG RTLFEPAWSY YSIERIDSGK LEEAWNQLRQ RHHILRTCFV ATSPSMAVQA
VLKDAPQNAE IFKVIESPAC IEEAAKAQAR EEGLNPSSLF VPPVRLRLLK ASDKDGIQIF
INHAAYDAWT MPMFVSELAH LYREQPVEST PDFPSFVEYA TRSLREVDEQ TYWSSQVGSS
LPTLIKPTNQ GLPKQFFVGV WEKVQNLSQL ERACRSACLS LQSVVLLAVS RSLARTTGVQ
SPTIGLYQTG RSASFSNIEN LSGPCLNVTP FTFPSPGAKA ESNALDEVQA IQNSLAERVL
YEQSCLRDIL TNWASTKGKG PLFNTWVNLL WMHQPSTRGD SKSHTDLDLF QPLRIGVPTD
FIPATPLPDP SGETTSISAL DTSYLPDENL YIDIGPDYST DTIGFGVRVE GGLLTEKEVR
GMVDDVSGEI EGIMAAIQQG KSR
