CCTN_TALIS
ID CCTN_TALIS Reviewed; 5641 AA.
AC A0A0U1LQE6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Cyclochlorotine synthetase {ECO:0000303|PubMed:26954535};
DE EC=6.3.2.- {ECO:0000305|PubMed:26954535};
DE AltName: Full=Cyclochlorotine biosynthesis protein N {ECO:0000303|PubMed:26954535};
DE AltName: Full=Nonribosomal peptide synthetase cctN {ECO:0000303|PubMed:26954535};
DE Short=NRPS cctN {ECO:0000303|PubMed:26954535};
GN Name=cctN {ECO:0000303|PubMed:26954535}; ORFNames=PISL3812_02619;
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26535 / WF-38-12;
RX PubMed=26197417; DOI=10.1016/j.jbiotec.2015.07.004;
RA Schafhauser T., Wibberg D., Rueckert C., Winkler A., Flor L., van Pee K.H.,
RA Fewer D.P., Sivonen K., Jahn L., Ludwig-Mueller J., Caradec T., Jacques P.,
RA Huijbers M.M., van Berkel W.J., Weber T., Wohlleben W., Kalinowski J.;
RT "Draft genome sequence of Talaromyces islandicus ('Penicillium islandicum')
RT WF-38-12, a neglected mold with significant biotechnological potential.";
RL J. Biotechnol. 211:101-102(2015).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND PATHWAY.
RX PubMed=26954535; DOI=10.1111/1462-2920.13294;
RA Schafhauser T., Kirchner N., Kulik A., Huijbers M.M., Flor L., Caradec T.,
RA Fewer D.P., Gross H., Jacques P., Jahn L., Jokela J., Leclere V.,
RA Ludwig-Mueller J., Sivonen K., van Berkel W.J., Weber T., Wohlleben W.,
RA van Pee K.H.;
RT "The cyclochlorotine mycotoxin is produced by the nonribosomal peptide
RT synthetase CctN in Talaromyces islandicus ('Penicillium islandicum').";
RL Environ. Microbiol. 18:3728-3741(2016).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of the mycotoxin cyclochlorotine, a
CC hepatotoxic and carcinogenic cyclic chlorinated pentapeptide
CC (PubMed:26954535). Cyclochlorotine is formed by the nonproteinogenic
CC amino acids L-2-aminobutyrate (2Abu), L-beta-phenylalanine (beta-Phe),
CC the unique L-cis-3,4-dichloroproline Pro(Cl(2)) and two L-serines (Ser)
CC (PubMed:26954535). The condensation of the 5 building blocks is
CC performed by the cyclochlorotine synthetase cctN, a nonribosomal
CC peptide synthetase (PubMed:26954535). The assembled linear pentapeptide
CC is then assumed to be released through cyclization by the terminal
CC condensation-like domain of cctN (PubMed:26954535). Incorporation of
CC the alternative substrates allo-threonine or alanine by the domains A3
CC or A1 respectively may lead to the production of the variants hydroxy-
CC cyclochlorotine and deoxy-cyclochlorotine, respectively
CC (PubMed:26954535). CctP probably acts as a phenylalanine aminomutase
CC and provides the uncommon building block beta-Phe (PubMed:26954535).
CC Furthermore, 2Abu can be synthesized from threonine by one of the
CC threonine dehydratases and transaminases localized outside of the
CC cluster (PubMed:26954535). The biosynthesis of the unusual
CC dichloroproline moiety remains elusive since the actual halogenase
CC still awaits to be detected, with the possibility that proline
CC halogenation is accomplished by a so far unknown type of halogenase
CC (PubMed:26954535). Finally, the cluster encoded transporters cctQ and
CC cctS are most likely responsible for cyclochlorotine secretion and
CC thereby may contribute to intrinsic resistance (PubMed:26954535). The
CC functions of the remaining proteins encoded by the cluster (cctM, cctO,
CC cctR and cctG) have not been identified yet (PubMed:26954535).
CC {ECO:0000269|PubMed:26954535}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26954535}.
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 (PubMed:26954535). Each module is responsible for the
CC recognition (via the A domain) and incorporation of a single amino acid
CC into the growing peptide product. Thus, an NRP synthetase is generally
CC composed of one or more modules and can terminate in a thioesterase
CC domain (TE) that releases the newly synthesized peptide from the
CC enzyme. Occasionally, epimerase (E) domains (responsible for L- to D-
CC amino acid conversion) are present within the NRP synthetase. VlmS has
CC the following 7 module architecture: A-T-C-A-T-C-A-T-C-A-T-C-A-T-C
CC (PubMed:26954535). The assembled linear pentapeptide, tethered to
CC domain T5 of module 5, is then assumed to be released through
CC cyclization by the terminal condensation-like domain which shows the
CC characteristic variations in the first histidine residue of the highly
CC conserved HHxxxDGxS motif of C domains (PubMed:26954535).
CC {ECO:0000269|PubMed:26954535}.
CC -!- DISRUPTION PHENOTYPE: Leads to complete loss of production of
CC cyclochlorotine and its variants such as hydroxy-cyclochlorotine and
CC deoxy-cyclochlorotine (PubMed:26954535). {ECO:0000269|PubMed:26954535}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; CVMT01000002; CRG85572.1; -; Genomic_DNA.
DR SMR; A0A0U1LQE6; -.
DR STRING; 28573.A0A0U1LQE6; -.
DR EnsemblFungi; CRG85572; CRG85572; PISL3812_02619.
DR OMA; HERFEDR; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 5.
DR Gene3D; 3.30.300.30; -; 5.
DR Gene3D; 3.30.559.10; -; 5.
DR Gene3D; 3.40.50.12780; -; 4.
DR InterPro; IPR010071; AA_adenyl_domain.
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 Pfam; PF00501; AMP-binding; 6.
DR Pfam; PF00668; Condensation; 5.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 5.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR PROSITE; PS00455; AMP_BINDING; 4.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Repeat; Virulence.
FT CHAIN 1..5641
FT /note="Cyclochlorotine synthetase"
FT /id="PRO_0000438669"
FT DOMAIN 816..892
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1902..1978
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2976..3052
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4005..4081
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 5118..5194
FT /note="Carrier 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 95..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..622
FT /note="Adenylation (A) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 821..889
FT /note="Thiolation (T) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 926..1333
FT /note="Condensation (C) domain 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 1390..1768
FT /note="Adenylation (A) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 1907..1975
FT /note="Thiolation (T) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 2022..2438
FT /note="Condensation (C) domain 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 2459..2859
FT /note="Adenylation (A) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 2977..3049
FT /note="Thiolation (T) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 3089..3482
FT /note="Condensation (C) domain 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 3523..3873
FT /note="Adenylation (A) domain 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 4010..4078
FT /note="Thiolation (T) domain 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 4123..4549
FT /note="Condensation (C) domain 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 4574..4982
FT /note="Adenylation (A) domain 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 5123..5191
FT /note="Thiolation (T) domain 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT REGION 5260..5556
FT /note="Condensation (C) domain 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26954535"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 853
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1939
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3013
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4042
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 5155
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5641 AA; 626721 MW; 28E6C5FB385ACA56 CRC64;
MYTDKFRFKT GVSSFQILLA WTVLLKDYIG SSGVSFSFSD STQCHKGTGK IDLELDEHDT
IGLLSRRIKE QLLVKSDSNE YLSFKTHLDI SSGEPENLNG HLIGSTNGHK KQWENDSADD
KRGQHPREIV DWTIKCVLSE DGRGMKTTAI PKLSTASSRQ GLRLMYQLEH VLRHIHLSTE
GTLVYKIDTA TKSDLNDIWK WNFNNPPLSE RTVLEIFTEN VQRYPTATAV NAWDGDLSYQ
ELDRLSTEFS FHLAYAGVKR GNIVPLFFEK SMWTPVAIWA VIKTGAAFVL LDEVLPESRL
QQLGQVIRQE IIVALASSSQ ESRAKLLGTQ VIIIDSYYLE TAASVPSEFK TQPQIQPSDL
IYIVFTSGTT GVPKAVMIQH SNVSAFARSL RTISDVGPNS RIVALSSYAF DVSLGNLFLS
LLSGCCLCIP SSWECRNTVP RVLQDYQITH AQMTPSISKM LRPCQLSTLE VLELSGEQCT
EDVLARWQET PIRVMNTYSP AECTITTVGN GNVLTSSKSS IIGKGLGNCC WVLDPIDHDR
LSPVGGIGEL VLEGPSVGMG YLHDPRATAL KFFEDPEWLL KGLPGVSPGR KGRLYRTGDL
VRYTEDGSID FVGRRDTQVK IRGQRVELGE ISAHLQQLVH PSIWCSPEVV KVSSGTELLV
VFLVVTEDEV GNGTASILRS TLRVTVDLVD SELRSRLPPA MVPGAYACIK DIPLTLTGKT
DHRKLREIGL SLAADMLIFP SNKQESYATN GDRQNRGLHT TLNGNGYQEQ NGHAHTHAHT
NGDTNGHTNG YVNGSHSHTN SRNKTQKYGH VTYDGTEEEY KIQTLKEIWS DEFHVDIESI
TLSDSFFAHG GESLTAIKMV GVAFEKGIQL DVPTIFRHPQ LSDLVSNCKM SATASPDHPK
PFSLLEGEII PVEAVEACGT CLDNIEDVYP CTPLQEGLIT ASISKSTAYV GQKAFLLPDG
INFERLALAW QRVVQTHQIL RTRIFDTESH GLLQAVLTDG KVFLGIQKRD LKSYLEDDND
RKMGLGTELC RCAIVRESGC SYFVLTMHHA IYDGWTLPRI GSEVFKAYQG VRVEPNMGFN
AFIKHIKSLP SQTANKFWAH QLANPGESAV FPIVPLYIQE PKSDSTVSKR FPVPQNANSG
VSMPSLLRSA WALLVSKLSD SNDVTFGATV SGRNVPIYGI KDLLSPTIST VPVRVKIDKD
SNIETFIATV QDDSLSAIPF ENFGLQNIRK INTDTREGSK FQTLFVVHPP NSTTPDQTLN
LSLADHELKD ILENLDISSV LSNFNEYGLM VIVTQEQDSL IVQASYDSRV LETDQVILLL
DQFAHVAEQI GQPANLACKV QELQFASGKD VETIWTWNST RVPGLKECIH DVICRTIAVQ
PHGQAISAWD GNLTFEELNV LSLRLAHILR SKGVGRGSLV PICMEKSKWA TIAMLGILRI
GAGFIAMDVR HQPRQRLQTI ADAVNSKWIV TAGPATELVP DVSEGVIVCD QDLQIETSDF
PVPLEPVCSA SSDTAFVVFT SGTTGVPKGI VITHENFCST IQHHAHQLKI SKESRIYDYA
SYSFDIAVHN SLMAMCLGAC LCIPSEDERE NDIEGSFERL QANWTDITPS VARLVDPTGV
PGLKTLVLSG EAVRKDLVER WATKVNLINA YGPAECQICT IQENIIDPQQ AAHIGRAVGC
TAWIIDPEND SLCPIGAVGE LVIEGPIVSP GYLNATRDAF IQDPKWLIEG SASIPGRRGS
VYRTGDLCRF RPDGTIIYIS RATTQIKING QRIELEDVEF YVQQAMATPG QVIASVVNFD
GVNHLTAFLA PVPTLKTNDK FHGLGKDVEP TVELIPPPIG LQNKLKDALP AYMIPTVFLK
ISHIPLTTTR KIDRRQLNDC ASRISRDDLI ALDQEGTGPV KIELSEKQEN MARLWAQVLK
LNSSKIGLHS DFFRLGGESI SAMRLVKYAR KEGLVLTVAD IFRHSRFDQL VMIATELTSR
ENTAEYFNGK LQPFALVPMN HRDSLISTAA MACNLPSDDI IDIYACTPFQ EGVFALTASN
SSAYVQHTEL RFSDELNLDQ VLDAWVSVIA ANPILRTRFI QSEDAKLMQV VVRPQKQAWK
WYYSPQEYLS EAENIPFGLG DPLFCFGLVR HGSTSSPGHT LIWTLHHAVY DAWTMDLILR
QVSSCYYGEK QAESGPDYSV FVDFLRHQES ESANWWKSYL SGSSDASIFP KMPISAAESQ
IDNTIRKEFA MPNIVPPGYS PAVILRAAWA AAVARYTGDE SVLFGETRLG RNVPVSGIDK
LLGPTIASVP LLVHIDREQT IGSLLYAIRE DGLQMQPFEH LGLQNISHIS EDTKAACKFQ
TLLVFLENAE DVDSSSIFKI DETIDDIRNF NSYYLLVYFT LNQKGLVAQA VFKDSAISSG
QVEFLLEQVQ SIFSKLCESP LDTPLRSLDL ASEQDLAKIW NWNATSAEAV DKFVHELIAE
KARQHPNKLA VFAHDGQITY KELDDYSTNL ASQLIGRGIG LGCFVPLCFE KSAMVPVCML
AVIKTGAAFY VMDVSYPEGR LKLITETLKA SLMLASPSQQ WLAKRLAGNI LVVDSVCCTD
NTYRSSHPVI EDPSRNTNRL MYVCFTSGST GLPKGVMVTH KNISSAAVAQ TQDLDFDPED
RVYDFSSHAF DANIWHFYLG FIVGACVCIP SQEDRIGNLA GSITFFQSTA LFLTPSVART
LDPKELPTVK RLYLGGEAVT PLDVSKWVEH LDLWGAYGPT ETTPLCIFTR LHSPEFASNI
GKGVGVRSWI CNPNNNEELM AIGAVGEMVN EGPLVTQGYY EQPEKTAKVF IENPEFLLRG
YKEIPGRRGR LYRTGDLVRY AFDGSIEYLG RADTQVKLRG QRVEFGEIEY HLNNALPGTS
SICEVIIHPS SRMPMLAAFC TLSSSMDTLN ETGARAYLCK RVPPYMVPEF FFTIPEIPKN
PSGKVDRLKL RSFGPQVLLE RSTSHEEGSV TERVHGPLTE METTLAELWA TAVDHDVTWL
GMESEFADVG GDSIAAMKLS NLARRHELSL TVKDIINSSN LAGMAIKIQP IHESFASPQP
FSLLPPSRID QTVARAAMTC GVSIDSITDI YPCTPLQVEL FSLTMKQPQA YIKRSVFEVP
TSVNFEKLIE SWDSVFDINA ILRTRFVEVD DLGLLQVVIK GHQRKKYGSL DSFIQACSQE
RLDFGSPLSH LAVVEDSVAL KIAWTIHHAL YDEWSTLIIE EQLRQAYRSR CIPRPPDYSE
FVRYIRTNNH EEARGFWRNS LAGCISAKIY PELPVGNYQV RPRKAFKRSL QYSARPGVNI
QATIHAAWAL IVSRLSASDD VVFSTTLAGR NAPVAGIEQM VGPTITPVPI RVKLGNQKQS
VQSMLDMIEK DIAKMAPYQH IGTKNIERIN DDTRAACKFR TLIVVTPTSY STTHELQDIK
TETYGVNSEE GQAFHTIPLV LFFFPGESGL DLEIVFDPVI LHEREIERLT GRLETVLSAF
STANSVSDIQ CIGREDLEDV WKWNAILPSS SKKLLHEDIL ECVQRAPDKV AIEAWDCKIT
YSQLDQLSEN HAVHLNNYNV RKGTVVPILS LKSGLVPVAA LAVLRAGGTL LPLDITQPVQ
RLKMIIDQVK PNVVMAGLSS IGIASQLCEN VIVIKSCVDI TPCAHGDAVY FETPSPDDVA
CILFTSGSTG IPKGVKQTHR GLSSAIKHQA RESGFNENTR AFEFASYGFD VSWNMIFKVL
AVGGTLCVPE EEERQNDLAR ALNRTAATLT ELTPSVARLI NPQQLTSLTT LILSGESVDP
REFAHWKPQN HHQLMPVGAI GEIIIEGPIV GSGYYNNENL TSASYVHDVP WLRNDHDGND
ARTSRVFKSG DLARFDSKGN IHFIARKDLQ VKLNGQRIEL EEVQHHVRNL MHDFVGPVIS
CVLGDSKQRS DQKLATFLVN KHGNTQGTCL AVPEEKAVEQ LETLDERLRE MLPKYMVPSI
YYFVTAVPRT NNGKIDMKRL VEVAAMARPD QIYRGRTDRQ RVRRIPSTPT EMKMQQLWAA
ALEVPIAEIG ADDTFFNLNG DSISAMKLVA GARSEGFDLR VSDVFETPRL SELATKIAPR
ITKKQLAVST IRPFELLGES ANIVAIRSEV AAKCGMQDPG AVKDVYPCTP LQESMLAATI
RDPRAFISMR VYRIRQGVDL VRLENAWATV VAQHPILRTR LVDLEHHGLT QAIFEESHII
WQTYVDMDSF LRHYEEQKMG PTTTLTRWAL IDEADDWKLV WTIHHAIYDG WVLPIVEEEV
RKTYFGSEQD KQYLDMKPLV KYILQEEKAK SIDFWARLLA GSEESIVYPP LPSHKYESSP
ATYLERTISA DLSSSRGINL SALLYGSWSV LVSHMTGIPK VSFGAILTGR NAPVDGIDRM
IGPAVTTVPI LVDANPSFSV RKFMDRLQDM TVQRMPHEHL GVHAIRRIND ACEAGCRFQT
VLVIQPPGGN GHDTSNIQDS FLMEEVDETT IEGFPDQHSV LNQYGLMIEI LPRGKEIKVR
ASFDSNLIST SQLSKTISRW ERIINQISQT LSQGVHTTIQ SLDSLSQQDI EEIWTWNKEL
PDVVDDRFVF EIIQEIAGRH PDALAIDAWD GQLTYRDLES LSTRVSELLV SFGVGPGSFV
PLLFHKSMWT NVSMLGVLKV GAAFVPLDFS HPEGHLRAVM QPLNADIILC ADNTRDRAAR
LSRRAIIVDE RSLNADHGNN LATDIPNASV SHTGNAALHI DDLAYAVFTS GSTGAAKGVK
VSHKNLVTAI HHHCKPERFQ IGLNTRSLDS SSYSFDACIF NFFYTVTQGG CLCVPNDEAL
KGDIGAFMRQ YKVNWAQLVP SVARTLNPKV LPDLKDLILT GEPLTRTDIE TWCHNVRLFN
VYGPTECTIL CSISSPIKGS SHFGYIGRGQ GANIWLTEIG NPDKLVPIGV PGEILIEGPI
IGAGYLGPYQ YPLVEDPPWL LAGTGHISGR QGKLFRTGDQ ALYTDDGTLV FIGRIGTDIK
LRGQRVDIVA VEDIIRRHVP SGLEIAVGIA RITVGGKVLA REMLLCFASQ NQTFRDNGAS
PQNKLNDILR ALVADIIPEL DAAMPKYLHP EAFVALSSMP KTSSGKTDRR CLKEAEKQLR
LHDLIWISTE MAESTNTPPS TQEEKVIAAL WAEVIGIEHE SISREDDFFK LGGDSLGVMR
LTTKAHRLGL VLKSNDVFRN SKLASLAEKI SWESIGPSEI APYKPYSLVP EISDIDAFTA
NHIVPSLNIE ANQVEDILPA NGFQVDYIHN KEEPLGLRYA YLDIGPDVQW QRLIQACRTM
LQGYECFRAR FILYKGRYYQ IILRDAPFII EEISATQQIA IFSQQLCRAD LHAASLSDVF
SKMTLVNVGI NRRRVILRLS HMQHDGWCTT QLLNAVAAAF NSLEIEKTPK WTSVLHYRHL
MVEESCRYWR TKLQGATQIT PSLVYKPGGS KVRTLRSYAL SNFHASDDNR RTRPTVVVNV
AWALILEQLA GHQDVVFGNV TTGRNGNMPG LDSVVGPCVN MLPMRLQLQS HSTTNREHKL
RDLVEASAQQ VDDGAFHNGL DWDELIDKCT TCVSGSRYKS AVHFRNMEFE PELSLGGDRV
VVQWYELVET PRWTTVLVYP EENVLRLWLL ADPAQIGDDG ADEILHMLAG YCEEIVQSLQ
T
