PFSYN_ROSSX
ID PFSYN_ROSSX Reviewed; 3210 AA.
AC P9WEP7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=PF 1022-synthetase {ECO:0000303|PubMed:10751395};
DE Short=PFSYN {ECO:0000303|PubMed:10751395};
DE EC=2.1.1.- {ECO:0000269|PubMed:10751395, ECO:0000269|PubMed:19072825};
DE EC=6.3.2.- {ECO:0000269|PubMed:10751395, ECO:0000269|PubMed:19072825};
DE AltName: Full=Cyclooctadepsipeptide synthetase PFSYN {ECO:0000303|PubMed:19072825};
DE AltName: Full=Nonribosomal peptide synthetase PFSYN {ECO:0000303|PubMed:10751395};
OS Rosellinia sp. (Mycelia sterilia).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia;
OC unclassified Rosellinia.
OX NCBI_TaxID=1769365;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mido N., Okakura K., Miyamoto K., Watanabe M., Yanai K., Yasutake T.,
RA Aihara S., Futamura T., Kleinkauf H., Murakami T.;
RT "Cyclic depsipeptide synthetase and its gene and mass production system of
RT cyclic depsipeptide.";
RL Patent number WO2001018179, 15-MAR-2001.
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=7592027; DOI=10.7164/antibiotics.48.820;
RA Conder G.A., Johnson S.S., Nowakowski D.S., Blake T.E., Dutton F.E.,
RA Nelson S.J., Thomas E.M., Davis J.P., Thompson D.P.;
RT "Anthelmintic profile of the cyclodepsipeptide PF1022A in in vitro and in
RT vivo models.";
RL J. Antibiot. 48:820-823(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10751395; DOI=10.1074/jbc.m001084200;
RA Weckwerth W., Miyamoto K., Iinuma K., Krause M., Glinski M., Storm T.,
RA Bonse G., Kleinkauf H., Zocher R.;
RT "Biosynthesis of PF1022A and related cyclooctadepsipeptides.";
RL J. Biol. Chem. 275:17909-17915(2000).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=11344131; DOI=10.1096/fj.00-0664fje;
RA Saeger B., Schmitt-Wrede H.P., Dehnhardt M., Benten W.P., Kruecken J.,
RA Harder A., Von Samson-Himmelstjerna G., Wiegand H., Wunderlich F.;
RT "Latrophilin-like receptor from the parasitic nematode Haemonchus contortus
RT as target for the anthelmintic depsipeptide PF1022A.";
RL FASEB J. 15:1332-1334(2001).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=16228266; DOI=10.1007/s00436-005-1439-y;
RA Jeschke R., Iinuma K., Harder A., Schindler M., Murakami T.;
RT "Influence of the cyclooctadepsipeptides PF1022A and PF1022E as natural
RT products on the design of semi-synthetic anthelmintics such as
RT emodepside.";
RL Parasitol. Res. 97:S11-S16(2005).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19072825; DOI=10.1002/cbic.200800539;
RA Mueller J., Feifel S.C., Schmiederer T., Zocher R., Suessmuth R.D.;
RT "In vitro synthesis of new cyclodepsipeptides of the PF1022-type: probing
RT the alpha-D-hydroxy acid tolerance of PF1022 synthetase.";
RL ChemBioChem 10:323-328(2009).
CC -!- FUNCTION: Nonribosomal peptide synthetase that synthesizes
CC cyclooctadepsipeptides (CODPs) PF 1022 that show powerful broad-
CC spectrum anthelmintic activity with low toxicity in animals
CC (PubMed:10751395, PubMed:19072825). Couples 4 N-methyl-L-leucines and a
CC varying content of alpha-D-hydroxy acids (D-lactates or D-
CC phenyllactates) in an alternative fashion (PubMed:10751395,
CC PubMed:19072825). The enzyme is capable of synthesizing all known
CC natural cyclooctadepsipeptides of the PF1022 type differing in the
CC content of D-lactate and D-phenyllactate, using from 4 D-lactates (PF
CC 1022F) to 4 D-phenyllactates (PF 1022B), respectively
CC (PubMed:10751395). The formation of different PF-related compounds is
CC mainly controlled by the molar ratio of the hydroxy acids
CC (PubMed:10751395). N-methylation of the substrate L-leucine takes place
CC after covalent binding prior to peptide bond formation
CC (PubMed:10751395). {ECO:0000269|PubMed:10751395,
CC ECO:0000269|PubMed:19072825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (R)-3-phenyllactate + 2 (R)-lactate + 8 ATP + 4 L-leucine +
CC 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022A
CC + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68744,
CC ChEBI:CHEBI:11009, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:180461,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10751395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68745;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 (R)-3-phenyllactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-
CC methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022B + 4 S-adenosyl-
CC L-homocysteine; Xref=Rhea:RHEA:68756, ChEBI:CHEBI:11009,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:180462, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10751395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68757;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 (R)-3-phenyllactate + (R)-lactate + 8 ATP + 4 L-leucine + 4
CC S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022C +
CC 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68760, ChEBI:CHEBI:11009,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:180463, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10751395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68761;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-phenyllactate + 3 (R)-lactate + 8 ATP + 4 L-leucine + 4
CC S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022D +
CC 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68764, ChEBI:CHEBI:11009,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:180464, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10751395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68765;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 (R)-lactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-
CC methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022F + 4 S-adenosyl-
CC L-homocysteine; Xref=Rhea:RHEA:68768, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:180465, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:10751395};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68769;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000269|PubMed:10751395};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.77 uM for D-lactate {ECO:0000269|PubMed:10751395};
CC KM=0.45 uM for D-phenyllactate {ECO:0000269|PubMed:10751395};
CC KM=20 uM for L-leucine {ECO:0000269|PubMed:10751395};
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product. Thus, an NRP synthetase is generally composed
CC of one or more modules and can terminate in a thioesterase domain (TE)
CC that releases the newly synthesized peptide from the enzyme (By
CC similarity). Occasionally, additional domains required for further
CC modifications are also present (By similarity). PF 1022 synthetase has
CC the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (By similarity).
CC The precursors D-hydroxycarboxylic acids and L-Leucine become activated
CC at the A1 and the A2 domains (By similarity). N-methylation of the
CC amino acid takes place at the MT-domain. The building blocks are
CC transferred from one module to another by means of T-domains and are
CC ultimately stored at the waiting position T2b (By similarity).
CC Condensation of the building blocks and final cyclization and release
CC from the enzyme is catalyzed by the C-domains (By similarity).
CC {ECO:0000250|UniProtKB:Q00869}.
CC -!- BIOTECHNOLOGY: The cyclooctadepsipeptides (CODP) of the PF 1022 type
CC such as PF 1022A are described as powerful broad-spectrum anthelmintic
CC neurotoxins that have low toxicity in animals (PubMed:7592027). PF
CC 1022A has been shown to bind to the aminoterminus of a the latrophilin-
CC like transmembrane receptor (HC-110R) from Haemonchus contortus
CC (Rudolphi) and thereby induces an influx of external Ca(2+) into cells
CC (PubMed:11344131). Both PF 1022A and PF 1022E can serve as valuable
CC starting materials for the synthesis of semi-synthetic CODP derivatives
CC with improved intrinsic anthelmintic potency and broad-spectrum
CC activity (PubMed:16228266). {ECO:0000269|PubMed:11344131,
CC ECO:0000269|PubMed:16228266, ECO:0000269|PubMed:7592027}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; BD013055.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 3.
DR Gene3D; 3.40.50.12780; -; 3.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 1: Evidence at protein level;
KW Ligase; Methyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..3210
FT /note="PF 1022-synthetase"
FT /id="PRO_0000454455"
FT DOMAIN 1010..1086
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2570..2644
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2668..2742
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 68..454
FT /note="Condensation 1"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 483..876
FT /note="Adenylation 1"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 1104..1534
FT /note="Condensation 2"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 1563..2023
FT /note="Adenylation 2"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 2081..2236
FT /note="S-adenosyl-L-methionine-dependent N-
FT methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 2788..3203
FT /note="Condensation 3"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1EA36, ECO:0000255"
FT REGION 2976..3002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1047
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2604
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2702
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3210 AA; 354313 MW; 4CA6D199DCE9FEFF CRC64;
MSNMAPLPTM GVEQQALSLS CPLLPHDDEK HSDNLYEQAT RHFGLSRDKI ENVLPCTSFQ
CDVIDCAVDD RRHAIGHVVY DIPNTVDIQR LAAAWKEVVR QTPILRTGIF TSETGDSFQI
VLKEGCLPWM YATCLGMKGA VIQDEAVAAM TGPRCNRYVV LEDPSTKQRL LIWTFSHALV
DYTVQERILQ RVLTVYDGRD VECPRIKDTE HVSRFWQQHF EGLDASVFPL LPSHLTVCNP
NARAEHHISY TGPVQRKWSH TSICRAALAV LLSRFTHSSE ALFGVVTEQS HNSEDQRRSI
DGPARTVVPI RVLCAPDQYV SDVIGAITAH EHAMRGFEHA GLRNIRRTGD DGSAACGFQT
VLLVTDGDAP KTPGSVLHRS VEESDRFMPC ANRALLLDCQ MAGNSASLVA RYDHNVIDPR
QMSRFLRQLG YLIQQFHHHV DLPLVKELDV VTAEDCAEIE KWNSERLTMQ DALIHDTISK
WAAGDPNKAA VFAWDGEWTY AELDNISSRL AVYIQSLDLR PGQAILPLCF EKSKWVVATI
LAVLKVGRAF TLIDPCDPSA RMAQVCQQTS ATVALTSKLH NTTLRSVVSR CIVVDDDLLR
SLPHADGRLK ATVKPQDLAY VIFTSGSTGE PKGIMIEHRG FVSCAMKFGP ALGMDEHTRA
LQFASYAFGA CLVEVVTALM HGGCVCIPSD DDRLNNVPEF IKRAQVNWVI LTPSYIGTFQ
PEDVPGLQTL VLVGEPISAS IRDTWASQVR LLNAYGQSES STMCSVTEVS PLSLEPNNIG
RAVGARSWII DPDEPDRLAP IGCIGELVIE SPGIARDYII APPPDKSPFL LAPPAWYPAG
KLSNAFKFYK TGDLVRYGPD GTIVCLGRKD SQVKIRGQRV EISAVEASLR RQLPSDIMPV
AEAIKRSDSS GSTVLTAFLI GSSKSGDGNG HALSAADAVI LDHGATNEIN AKLQQILPQH
SVPSYYIHME NLPRTATGKA DRKMLRSIAS KLLGELSQNV TSQPIEKHDA PATGIEVKLK
ELWFLSLNLN PNSQDVGASF FDLGGNSIIA IKMVNMARSA GIALKVSDIF QNPTLAGLVD
VIGRDPAPYN LIPTTAYSGP VEQSFAQGRL WFLDQIELDA LWYLLPYAVR MRGPLHIDAL
TIALLAIQQR HETLRTTFEE QDGVGVQVVH ASPISDLRII DVSGDRNSDY LQLLHQEQTT
PFILACQAGW RVSLIRLGED DHILSIVMHH IISDGWSIDI LRRELSNFYS AALRGSDPLS
VVSPLPLHYR DFSVWQKQVE QETEHERQLE YWVKQLADSS AAEFLTDFPR PNILSGEAGS
VPVTIEGELY ERLQEFCKVE QMTPFAVLLG AFRATHYRLT GAEDSIIGTP IANRNRQELE
NMIGFFVNTQ CMRITVDGDD TFESLVRQVR TTATAAFEHQ DVPFERVVTA LLPRSRDLSR
NPLAQLTFAL HSQQDLGKFE LEGLVAEPVS NKVYTRFDVE FHLFQEAGRL SGNVAFAADL
FKPETISNVV AIFFQILRQG IRQPRTPIAV LPLTDGLADL RAMGLLEIEK AEYPRESSVV
DVFRKQVAAH PHAFAVVDSA SRLTYADLDR QSDQLATWLG RRNMTAETLV GVLAPRSCQT
VVAILGILKA NLAYLPLDVN CPTARLQTIL STLNRHKLVL LGSNATTPDV QIPDVELVRI
SDILDRPING QAKLNGHTKS NGYSKPNGYT HLKGYSNLNG YSKQNGYAQL NGHRERNNYL
DLNGHSLLNG NSDITTSGPS ATSLAYVIFT SGSTGKPKGV MVEHRSIIRL AKKNRIISRF
PSVAKVAHLS NIAFDAATWE MFAALLNGGT LVCIDYMTTL DSKTLEAAFA REQINAALLT
PALLKQCLAN IPTTLGRLSA LVIGGDRLDG QDAIAAHALV GAGVYNAYGP TENGVISTIY
NITKNDSFIN GVPIGCAISN SGAYITDPDQ QLVPPGVMGE LVVTGDGLAR GYTDPALDAG
RFVQIMINDK AVRAYRTGDR ARYRVGDGQI EFFGRMDQQV KIRGHRIEPA EVERAILDQD
SARDAVVVIR HQEGEEPEMV GFVATHGDHS AEQEEADDQV EGWKDFFESN TYADMDTIGQ
SAIGNDFTGW TSMYDGSEIN KAEMQEWLDD TMRTLLDGQA PGHVLEIGTG SGMVLFNLGA
GLQSYVGLEP SRSAATFVTK AINSTPALAG KAEVHVGTAT DINRLRGLRP DLVVLNSVVQ
YFPTPEYLLE VVESLVRIPG VKRVVFGDIR SHATNRHFLA ARALHSLGSK ATKDAIRQKM
TEMEEREEEL LVDPAFFTAL LQGQLADRIK HVEILPKNMR ATNELSAYRY TAVIHVRGPE
EQSRPVYPIQ VNDWIDFQAS RIDRRALLRL LQRSADAATV AVSNIPYSKT IVERHVVESL
DNNNRENTHR APDGAAWISA VRSKAERCTS LSVTDLVQLG EEAGFRVEVS AARQWSQSGA
LDAVFHRYNL PTQSNSRVLI QFPTEDGQTR RSATLTNRPL QRLQSRRFAS QIREQLKAVL
PSYMIPSRIV VIDQMPLNAN GKVDRKELTR RAQIAPKSQA APAKPVKQVD PFVNLEAILC
EEFAEVLGME VGVNDHFFQL GGHSLLATKL VARLSRRLNG RVSVRDVFDQ PVISDLAVTL
RQGLTLENAI PATPDSGYWE QTMSAPTTPS DDMEAVLCKE FADVLGVEVS ATDSFFDLGG
HSLMATKLAA RISRRLDVPV SIKDIFDHSV PLNLARKIRL TQAKGHEATN GVQIANDAPF
QLISVEDPEI FVQREIAPQL QCSPETILDV YPATQMQRVF LLNPVTGKPR SPTPFHIDFP
PDADCASLMR ACASLAKHFD IFRTVFLEAR GELYQVVLKH VDVPIEMLQT EENINSATRS
FLDVDAEKPI RLGQPLIRIA ILEKPGSTLR VILRLSHALY DGLSLEHILH SLHILFFGGS
LPPPPKFAGY MQHVASSRRE GYDFWRSVLR DSSMTVIKGN NNTTPPPPPQ QQSTPSGAHH
ASKVVTIPTQ ANTDSRITRA TIFTTACALM LAKEDNSSDV VFGRTVSGRQ GLPLAHQNVI
GPCLNQVPVR ARGLNRGTTH HRELLREMQE QYLNSLAFET LGYDEIKAHC TDWPDVPATA
SFGCCIVYQN FDSHPDSRVE EQRLQIGVLS RNYEAINEGL VHDLVIAGES EPDGDDLRVT
VVANRRLCDE ERLKRMLEEL CGNIRALALV
