CGHG_CHAGB
ID CGHG_CHAGB Reviewed; 4017 AA.
AC Q2HBN0; Q2HBM6; Q2HBM7; Q2HBM8; Q2HBM9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Hybrid PKS-NRPS synthetase cghG {ECO:0000303|PubMed:26360642};
DE Short=PKS-NRPS cghG {ECO:0000303|PubMed:26360642};
DE EC=2.3.1.- {ECO:0000269|PubMed:26360642};
DE EC=6.3.2.- {ECO:0000269|PubMed:26360642};
DE AltName: Full=Sch210972 biosynthesis cluster protein G {ECO:0000303|PubMed:26360642};
GN Name=cghG {ECO:0000303|PubMed:26360642};
GN ORFNames=CHGG_02374, CHGG_02375, CHGG_02376, CHGG_02377, CHGG_02378;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX PubMed=26360642; DOI=10.1002/cbic.201500386;
RA Sato M., Yagishita F., Mino T., Uchiyama N., Patel A., Chooi Y.H., Goda Y.,
RA Xu W., Noguchi H., Yamamoto T., Hotta K., Houk K.N., Tang Y., Watanabe K.;
RT "Involvement of lipocalin-like CghA in decalin-forming stereoselective
RT intramolecular [4+2] cycloaddition.";
RL ChemBioChem 16:2294-2298(2015).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of the tetramic acid Sch210972, a potential
CC anti-HIV fungal natural product that contains a decalin core
CC (PubMed:26360642). The PKS module of cghG together with the
CC enoylreductase cghC catalyze the formation of the polyketide unit which
CC is then conjugated to 4-hydroxyl-4-methyl glutamate (HMG) by the
CC condensation domain of the cghG NRPS module (PubMed:26360642). One
CC unique structural feature of Sch210972 is the tetramic acid motif
CC proposed to be derived from the non-proteinogenic amino acid HMG, by a
CC Dieckmann-type condensation catalyzed by the reductase domain of cghG
CC (PubMed:26360642). The aldolase cghB catalyzes the aldol condensation
CC of 2 molecules of pyruvic acid to yield the intermediate 4-hydroxyl-4-
CC methyl-2-oxoglutarate (HMOG), which can then be stereoselectively
CC transaminated by an unidentified enzyme to form HMG (PubMed:26360642).
CC The Diels-Alderase cghA then uses the Dieckmann product released by
CC cghG as substrate and catalyzes the Diels-Alder cycloaddition to form
CC the decalin ring of Sch210972 (PubMed:26360642). CghA also suppresses
CC the nonenzymatic formation of the alternative stereoisomer
CC (PubMed:26360642). {ECO:0000269|PubMed:26360642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,4S)-4-hydroxy-4-methylglutamate + ATP + 11 H(+) + 8
CC malonyl-CoA + 8 NADPH + 3 S-adenosyl-L-methionine = (2S)-3-[(2S)-3,5-
CC dioxo-4-[(2E,4R,6R,8E,10E,12E)-4,6,12-trimethyltetradeca-2,8,10,12-
CC tetraenoyl]pyrrolidin-2-yl]-2-hydroxy-2-methylpropanoate + AMP + 8
CC CO2 + 8 CoA + diphosphate + 6 H2O + 8 NADP(+) + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67264, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57856, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167901, ChEBI:CHEBI:167907,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26360642};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67265;
CC Evidence={ECO:0000269|PubMed:26360642};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26360642}.
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. CcsA contains also a polyketide
CC synthase module (PKS) consisting of several catalytic domains including
CC a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a
CC dehydratase domain (DH), a methyltransferase domain (MT), and a
CC ketoreductase domain (KR). Instead of a thioesterase domain (TE), cghG
CC finishes with a reductase-like domain (R) for peptide release. CghG has
CC the following architecture: KS-MAT-DH-MT-KR-PCP-C-A-T-R.
CC {ECO:0000305|PubMed:26360642}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ90439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAQ90440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAQ90441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAQ90442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAQ90443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH408030; EAQ90439.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH408030; EAQ90440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH408030; EAQ90441.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH408030; EAQ90442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH408030; EAQ90443.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001228890.1; XM_001228889.1.
DR RefSeq; XP_001228891.1; XM_001228890.1.
DR RefSeq; XP_001228892.1; XM_001228891.1.
DR RefSeq; XP_001228893.1; XM_001228892.1.
DR RefSeq; XP_001228894.1; XM_001228893.1.
DR STRING; 38033.XP_001228890.1; -.
DR EnsemblFungi; EAQ90439; EAQ90439; CHGG_02374.
DR EnsemblFungi; EAQ90440; EAQ90440; CHGG_02375.
DR EnsemblFungi; EAQ90441; EAQ90441; CHGG_02376.
DR EnsemblFungi; EAQ90442; EAQ90442; CHGG_02377.
DR EnsemblFungi; EAQ90443; EAQ90443; CHGG_02378.
DR GeneID; 4389928; -.
DR GeneID; 4389929; -.
DR GeneID; 4389930; -.
DR GeneID; 4389931; -.
DR GeneID; 4389932; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_35_7_1; -.
DR InParanoid; Q2HBN0; -.
DR OMA; TYAFDAR; -.
DR OrthoDB; 167817at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
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 InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Ligase; Methyltransferase; Multifunctional enzyme; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..4017
FT /note="Hybrid PKS-NRPS synthetase cghG"
FT /id="PRO_0000453331"
FT DOMAIN 2423..2499
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3583..3661
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 9..443
FT /note="Ketoacyl synthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..869
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 937..1240
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 1398..1585
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 2127..2300
FT /note="Ketoreductase (KR)domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 2514..2536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2548..2628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2626..3020
FT /note="Condensation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 3053..3453
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 3567..3588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3588..3658
FT /note="Thiolation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT REGION 3696..3920
FT /note="Reductase-like"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26360642"
FT COMPBIAS 2548..2580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2458
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3621
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4017 AA; 434809 MW; 4AC70F77DDC1889F CRC64;
MSAADQEPIA VIGMACRFPG GSNSPSKLWE LLKAPHDIAK PIPDDRFDST GFFHKNGSHH
GATDCREAYF LDEDVTRFDN AFFNVQPGEA EALDPQQRFL METIYDSLCS AGQTIEGLRG
SRAAVYVGLM CDDWSQMNGR DWDLVPTYAA TGTSRAVVSN RVSYFFDWHG PSMTIDTACS
SSLVAVHEGV NALRRGESPI VVAAGANMIL SPGMMIAESN LHMLSPTGRS KMWDASADGY
ARGEGIAAVV LKPLSAALRD GDPINCVIRG TGVNQDGRTP GLTMPNNVAQ ADLIRDTYER
AGLNIQDPKD RPQFFHAHGT GTPAGDPQEA EAISRAFYEG GSVKDPLFVG SIKTVIGHTE
GTAGLASLIG TALAMQNNTI PPNLHFNTLS PRVAEFCDNL RIPTKALPWP TPVAGQPRRA
SVNSFGFGGT NAHAIIESYE AAPTEQRTVS TKVPAFTPLT ISAASASALR TTLSDLSAYV
LSHPDTDLRD LAYTFQHRRS TLAFRKAIAT DNRDALVGTI DALLNEGGAG DGGLTARYFD
SPDPKILGVF TGQGAQWPRM GALLLEQSPY VGELLTQLDQ ALATLPEGDR PDWTLREQIL
AEAAQSRLSE AAISQPLCTA VQIALVDLLG LAGIRLRGVV GHSSGEIAAA YASGYLSATD
AIRVAYYRGL YAKLAGSPAG RGSMLAVGTS FEDAVEFCEL EEFEGRIKVA ARNSSNSVTL
SGDEDAIEEA LEIYKDEGRF ARQLRVDTAY HSHHMEPCAV PYRDALTRCE IKVGEGNGIP
WYSSVIEGHV MAPTDVSPQY WVDNMTSAVL FSPAVAHAVA EGGPFDLGVE VGPHPALKGP
CLDTVEEAAG HRIPYTGLLG RNKNDVVELS SALGFIWTQL GAASVDFDRL ERAISGNPYP
KKVVDDLPTY PFDHSRSFYT LTRFSGAHRN MHAPPNPILG RRCVETETAD EVSWRNILKS
GEISWLQGHQ LQGQTVFPAM GYIAMCVEAA AVLAGPERPL GLVTLEDVII GRALAFQNES
VGMESKVTVK IDHTSDDELR GHIACHSGLP FDSAAPLALN FSATLHVRFH EPRADTLPAV
RADEISLVKT DPGRLYSQFT QLGYNYSPPF TGVKAIQRKR GFATGDIEDI SGEGWEDQLI
VHPGWLDSAL QTAFAAYSYP HDNRLWALHV PTEIRTVSIN PYFTERGAGG RTRQLQYQST
AREGLGAPVA ADIDVFAAGE EDGHAFIQLE AVQVKPFAAA TARDDALLFA RFDYRLANPD
AIAAVEGDDL LPPKTEAVVE TIERVGFYYL RRVHETVTPA ERRPTLPHFR HLIDLCGRVV
PLVAAGEHPH VPREAINDSA SYIRSLIARY HDRADIQLLE AVGENLVGEI RRNGIMLEHM
MKDGILDRFY EELAGLDVAN VWIARMVAQV AHRHPHLRIL EIGAGTGGTT RTVLPMLGDA
FQSYTFTDIS AGFFGSAQER FRTYADRMVF ATYNMELTPE EQGFEEGTYD VVLASNVLHA
TGRLDDMMAN TRRLLRPGGY LMMLEFVSND RTGITACMGG LPGWWGNGIV DPARGDGPCL
TPAQWDELVR RHGFSGVDTH CPVEKHLQWY TVHLCQAVDD RVLALRNPLE SLESAATLAP
PPAELVIVGG TTATVSKLID EASTLLAPRY NTISRVATLE ELDQRGLPLG SSVLSLTELD
HQFFEHRTAA KLEALKALWR AGGSIIWATR GVRDASPYSA MILGLARVVR FEYPNINLQI
LDFDRAPDAA TLAADLVRLE MGRHWKEEGA NILYSVEPEA HYENGALFIP RMYPDRDANA
RYNTQRRTVA REVDPRETSV VLEPAGPVGG ALELCAPSPL RVAPAARPGA EKTVEVIVEQ
SVLHAVKVPD AGFFSLCAGT DAETGRPLLA LVDSPVESRL RVPVEWTVSL REPLSRTGAF
SLGDVASHLV ASAILAGAPA FGSLLIHEAD ESLKEAFGRQ AAGHGAHVVF TTADKAKARA
GADWVLVHEK LPGRLVQRLL PHDISSFTDL SHSEGSASAQ LIVHSLPVYS PITTVKDVIR
AQAGAFPDAA PQDVGAALKA AWQAASRKRK GSGNKSQTSA IPVLPLQDVS RAGARHAPLT
VVDWNTNSVS VALRPIDAGT IFRSDGTYFL VGLSGEVGQS LCQWMVAHGA RHIVLSSRRP
KVHPRYIEDL AALGATVRVM ALDITNREAL RACYDTXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXAVVQDSLT ENLIRILMMP ATETVDPMMS LVELGIDSIM
AVDLRTWFLK ELDVDVPVLK ILSPGETVKS LAEEAMAKIP AEIVDLSKLA EGSADVSGAP
APAAVQPVQP APVPVPVPVT KKAIDQVSEA SGVSATTPST RAETDASSSP ALVSTPGTSL
ERPDQEEDKQ LFQPPPRPKP TTLQHRLPRQ AYWAGSASTT SPKPSRRAAQ RHETLRTRFF
WSTDDSRTPM QGILSQTLVR LETATIETEA QASEELEAMR KYEWNLGDWV PLRIKLLTLS
ETSHYLILGS HHISMDGHSF SVFLLDIHQA YNNPARPLPP MPSTSQARAF GAHQIAAYES
GQMRPAIEHY KTTLPAADLA RPIELFPFAR TKVRPPLDRY GTHVARAHLG PDTTAKLKTL
ARGRRATSFH AYLGALQALL FRLLPADTTE RVYIGIADAN RLDSRFAASV GNFLNVLPLR
FDRDAATFGQ AIETARDKAR DALKHSALPF DLLLDEVGVP RSPTLLIRCI VFMNYRLVVK
EHADKQWIGC RIGEERWHTA RTGYDVALEI VEDHDGATLA MHVQQSLYDA DAAELLVRSF
ANAVKEFAAK GDAMETEKLQ KWDKVDVEKA LEIGTGPALN LKWPATVAHR IDEVIAQNPT
AVALKDGLGN VLTYAQMDAR VESIANALNV RLPNNADGKA PVVGVFQAPS ADWICSLVAI
HRVGAVYLPL DLRNSIPRLK SNVAVARPAA LLVDAETASR VGELEIKDAV PAIDVSRLAA
DTKGKKPTNT AAARADQPAY IIFTSGSTGE PKGIVVTHAG LRNNLEGYHN AWNIPSLAGV
VLQQVSFGFD ALSASDLCLR XXXXXXXXXX LMVDHGVTMT QATPSEYEMW LRFAPDQLRR
CTSWKAAWFG GERAAPGLVR SFRDLCVALP NLNVYTSYGP TESTISAMKG VADVRNDPTL
TVPVPGRLLP NYTAYLVDDE MRPLPIGVPG EILLGGAGVG KNEYLGRPDL TTQAFLSSPF
PVPGDGGKPA RLYRTGDYGR LDKSGFLAIE GRIAGDTQVK LRGFRIELAE IERVMLRESD
GQLAQVVVTA RGVDDGEAEG FLAAHVVLES QSTDAAATAQ VINRLRSRLP LSLPQYMCPA
IIVPLAKLPL TSNDKVDRRA VQALSLPKTT TASTTADGTQ PAQPLTPTES RLATLWAGVL
PQRGGGVLQP RSDFFTAGGN SLLLVKLQAA IKREFGDAPR LSKLMSATEL GSMAALLDQA
GATALDWERE TALDLPQGVT APAKARENGA GLRVLVTGAS GSLGKRIVRR LVGDNRVATV
VCLVRPTEGR DPSTLFFAAG QADNAKIRTI LADLPTIPTT HPDLDPAIID AVIHCAADRS
FWDGYSAVSL STSTRSRPRC SLLTAGAHLH ALSSGALGAF EDPNTYNTKS TLPRPSPTDG
YLASKWVAER YLARAVREAG LRATAHRPSG AVPASEREGK EVLAAMAGDM LRLSASLGVR
PDYARLSGSF DVGRLEDVAA AVVGEVTGGL GGQGGEEGMG VVEYPGMASV QIRELAEYAE
MLLKNGGAEA EAVKGLPMVP ALHWVGLAKR AGLFEWLLTA QHLVVDDEEG RKIVSRR
