GenomeNet

Database: UniProt
Entry: Q9ZGI4
LinkDB: Q9ZGI4
Original site: Q9ZGI4 
ID   PIKA2_STRVZ             Reviewed;        3739 AA.
AC   Q9ZGI4;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-JUN-2016, entry version 101.
DE   RecName: Full=Narbonolide/10-deoxymethynolide synthase PikA2, modules 3 and 4 {ECO:0000305};
DE            EC=2.3.1.239 {ECO:0000269|PubMed:10421766, ECO:0000305|PubMed:21570406};
DE            EC=2.3.1.240 {ECO:0000269|PubMed:10421766, ECO:0000305|PubMed:21570406};
DE   AltName: Full=Narbonolide/10-deoxymethynolide synthase PikAII {ECO:0000305};
DE   AltName: Full=Pikromycin polyketide synthase component PikAII {ECO:0000303|PubMed:10421766};
DE            Short=Pikromycin PKS component PikAII {ECO:0000303|PubMed:10421766};
DE   AltName: Full=Type I modular polyketide synthase PikAII {ECO:0000303|PubMed:10421766};
DE            Short=PKS {ECO:0000303|PubMed:10421766};
GN   Name=pikAII {ECO:0000303|PubMed:9770448};
OS   Streptomyces venezuelae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=54571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA   Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT   "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT   venezuelae: architecture of metabolic diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10421766; DOI=10.1016/S1074-5521(99)80087-8;
RA   Tang L., Fu H., Betlach M.C., McDaniel R.;
RT   "Elucidating the mechanism of chain termination switching in the
RT   picromycin/methymycin polyketide synthase.";
RL   Chem. Biol. 6:553-558(1999).
RN   [3]
RP   FUNCTION, PATHWAY, AND SUBUNIT.
RX   PubMed=19027305; DOI=10.1016/j.bmc.2008.10.082;
RA   Kittendorf J.D., Sherman D.H.;
RT   "The methymycin/pikromycin pathway: a model for metabolic diversity in
RT   natural product biosynthesis.";
RL   Bioorg. Med. Chem. 17:2137-2146(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 920-1423, FUNCTION,
RP   CATALYTIC ACTIVITY, REACTION MECHANISM, COFACTOR, ACTIVE SITE, AND
RP   SUBUNIT.
RX   PubMed=21570406; DOI=10.1016/j.jmb.2011.04.065;
RA   Zheng J., Keatinge-Clay A.T.;
RT   "Structural and functional analysis of C2-type ketoreductases from
RT   modular polyketide synthases.";
RL   J. Mol. Biol. 410:105-117(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of 12- and 14-membered ring
CC       macrolactone antibiotics such as methymycin/neomethymycin and
CC       pikromycin/narbomycin, respectively. Component of the pikromycin
CC       PKS which catalyzes the biosynthesis of both precursors 10-
CC       deoxymethynolide (12-membered ring macrolactone) and narbonolide
CC       (14-membered ring macrolactone). Chain elongation through PikAI,
CC       PikAII and PikAIII followed by thioesterase catalyzed termination
CC       results in the production of 10-deoxymethynolide, while continued
CC       elongation through PikAIV, followed by thioesterase (TE) catalyzed
CC       cyclization results in the biosynthesis of the narbonolide.
CC       {ECO:0000269|PubMed:10421766, ECO:0000269|PubMed:21570406,
CC       ECO:0000305|PubMed:19027305}.
CC   -!- CATALYTIC ACTIVITY: Malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5
CC       NADPH = 10-deoxymethynolide + 6 CoA + 6 CO(2) + 5 NADP(+) + 2
CC       H(2)O. {ECO:0000269|PubMed:10421766, ECO:0000305|PubMed:21570406}.
CC   -!- CATALYTIC ACTIVITY: Malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5
CC       NADPH = narbonolide + 7 CoA + 7 CO(2) + 5 NADP(+) + 2 H(2)O.
CC       {ECO:0000269|PubMed:10421766, ECO:0000305|PubMed:21570406}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305|PubMed:21570406};
CC       Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:19027305,
CC       ECO:0000305|PubMed:9770448}.
CC   -!- SUBUNIT: Homodimer (PubMed:21570406). Pikromycin PKS consists of a
CC       combination of multimodular (PikAI and PikAII) and monomodular
CC       (PikAIII and PikAIV) polypeptides each coding for a functional
CC       synthase subunit which participates in 1 (monomodular) or 2
CC       (multimodular) of the six FAS-like elongation steps required for
CC       formation of the polyketide. Module 1, 2, 3, 4, 5, and 6
CC       participating in biosynthesis steps 1, 2, 3, 4, 5, and 6,
CC       respectively. {ECO:0000269|PubMed:21570406,
CC       ECO:0000305|PubMed:19027305}.
CC   -!- MISCELLANEOUS: Type I modular polyketide synthases (PKSs) catalyze
CC       the step-wise condensation of simple carboxylic acid derivatives.
CC       Organizationally, type I PKSs are arranged into modules, wherein
CC       each module is comprised of a set of catalytic activities that is
CC       responsible for a single elongation of the polyketide chain and
CC       the appropriate reductive processing of the beta-keto
CC       functionality. A minimal elongation module contains an acyl
CC       transferase (AT) domain, an acyl-carrier protein (ACP) domain, and
CC       a ketosynthase (KS) domain. The AT domain is responsible for
CC       loading the methylmalonyl-CoA extender unit onto the
CC       phosphopantetheinylated ACP domain. Subsequently, the KS domain
CC       decarboxylates and then condenses the ACP-bound extender unit with
CC       the growing polyketide chain obtained from the preceding module to
CC       yield an ACP-bound beta-ketoacyl intermediate. In addition to the
CC       three core domains, each elongation module may contain up to three
CC       additional domains: a ketoreductase (KR), dehydratase (DH), and an
CC       enoyl reductase (ER) that are responsible for the reductive
CC       processing of the beta-keto functionality prior to the next
CC       extension step. The presence of a KR domain alone gives rise to a
CC       beta-hydroxyl functionality, the presence of both a KR and a DH
CC       domain generates an alkene, while the combination of KR, DH, and
CC       ER results in complete reduction to the alkane. Finally, a
CC       thioesterase (TE) domain, typically found at the terminus of the
CC       last elongation module, catalyzes the termination of polyketide
CC       biosynthesis. The activity of this domain results in cleavage of
CC       the acyl chain from the adjacent ACP and formation of the
CC       macrocyclic ring. {ECO:0000305|PubMed:19027305,
CC       ECO:0000305|PubMed:21570406}.
CC   -!- MISCELLANEOUS: C2-type beta-ketoacyl reductase 1 is unable to bind
CC       NADP and seems to act as a racemase.
CC       {ECO:0000269|PubMed:21570406}.
CC   -!- SIMILARITY: Contains 2 acyl carrier domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258}.
DR   EMBL; AF079138; AAC69330.1; -; Genomic_DNA.
DR   PIR; T17410; T17410.
DR   PDB; 3QP9; X-ray; 1.88 A; A/B/C/D=920-1423.
DR   PDBsum; 3QP9; -.
DR   ProteinModelPortal; Q9ZGI4; -.
DR   SMR; Q9ZGI4; 6-913, 1435-1518, 1538-2409, 3555-3645.
DR   KEGG; ag:AAC69330; -.
DR   KO; K16001; -.
DR   BioCyc; MetaCyc:MONOMER-18412; -.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; TAS:UniProtKB.
DR   GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.40.366.10; -; 4.
DR   Gene3D; 3.40.47.10; -; 4.
DR   Gene3D; 3.40.50.720; -; 4.
DR   Gene3D; 3.90.180.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR032821; KAsynt_C_assoc.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 2.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 5.
DR   SUPFAM; SSF52151; SSF52151; 4.
DR   SUPFAM; SSF53901; SSF53901; 4.
DR   SUPFAM; SSF55048; SSF55048; 2.
DR   PROSITE; PS50075; ACP_DOMAIN; 2.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Antibiotic biosynthesis;
KW   Multifunctional enzyme; NADP; Phosphopantetheine; Phosphoprotein;
KW   Repeat; Transferase.
FT   CHAIN         1   3739       Narbonolide/10-deoxymethynolide synthase
FT                                PikA2, modules 3 and 4.
FT                                /FTId=PRO_0000436358.
FT   DOMAIN     1443   1517       Acyl carrier 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   DOMAIN     3572   3642       Acyl carrier 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   NP_BIND    3092   3109       NADP (Enoyl reductase).
FT                                {ECO:0000250|UniProtKB:Q03132}.
FT   NP_BIND    3285   3288       NADP (Beta-ketoacyl reductase 2).
FT                                {ECO:0000305}.
FT   NP_BIND    3309   3312       NADP (Beta-ketoacyl reductase 2).
FT                                {ECO:0000305}.
FT   NP_BIND    3338   3339       NADP (Beta-ketoacyl reductase 2).
FT                                {ECO:0000305}.
FT   NP_BIND    3412   3413       NADP (Beta-ketoacyl reductase 2).
FT                                {ECO:0000305}.
FT   REGION       38   1517       Module 3. {ECO:0000305}.
FT   REGION       38    466       Beta-ketoacyl synthase 1. {ECO:0000305}.
FT   REGION      572    877       Acyltransferase 1. {ECO:0000305}.
FT   REGION     1150   1343       C2-type beta-ketoacyl reductase 1.
FT                                {ECO:0000305|PubMed:21570406}.
FT   REGION     1542   3642       Module 4. {ECO:0000305}.
FT   REGION     1542   1970       Beta-ketoacyl synthase 2. {ECO:0000305}.
FT   REGION     2069   2374       Acyltransferase 2. {ECO:0000305}.
FT   REGION     2428   2703       Dehydratase. {ECO:0000305}.
FT   REGION     2959   3267       Enoyl reductase. {ECO:0000305}.
FT   REGION     3277   3458       Beta-ketoacyl reductase 2. {ECO:0000305}.
FT   ACT_SITE    208    208       Acyl-thioester intermediate; for beta-
FT                                ketoacyl synthase 1 activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE    662    662       Acyl-ester intermediate; for
FT                                acyltransferase 1 activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE   1313   1313       For C2-type beta-ketoacyl reductase 1
FT                                (with a probable racemase activity).
FT                                {ECO:0000250|UniProtKB:Q03132,
FT                                ECO:0000305|PubMed:21570406}.
FT   ACT_SITE   1712   1712       Acyl-thioester intermediate; for beta-
FT                                ketoacyl synthase 2 activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE   2159   2159       Acyl-ester intermediate; for
FT                                acyltransferase 2 activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE   2460   2460       Proton acceptor; for dehydratase
FT                                activity. {ECO:0000250|UniProtKB:Q03132}.
FT   ACT_SITE   2629   2629       Proton donor; for dehydratase activity.
FT                                {ECO:0000250|UniProtKB:Q03132}.
FT   ACT_SITE   3005   3005       For enoyl reductase activity.
FT                                {ECO:0000250|UniProtKB:Q03132}.
FT   ACT_SITE   3427   3427       For beta-ketoacyl reductase 2 activity.
FT                                {ECO:0000305}.
FT   BINDING    3388   3388       NADP (Beta-ketoacyl reductase 2).
FT                                {ECO:0000250|UniProtKB:Q03131}.
FT   MOD_RES    1480   1480       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    3605   3605       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   3739 AA;  387178 MW;  3D3910824DA5B080 CRC64;
     MSTVNEEKYL DYLRRATADL HEARGRLREL EAKAGEPVAI VGMACRLPGG VASPEDLWRL
     VAGGEDAISE FPQDRGWDVE GLYDPNPEAT GKSYAREAGF LYEAGEFDAD FFGISPREAL
     AMDPQQRLLL EASWEAFEHA GIPAATARGT SVGVFTGVMY HDYATRLTDV PEGIEGYLGT
     GNSGSVASGR VAYTLGLEGP AVTVDTACSS SLVALHLAVQ ALRKGEVDMA LAGGVTVMST
     PSTFVEFSRQ RGLAPDGRSK SFSSTADGTS WSEGVGVLLV ERLSDARRKG HRILAVVRGT
     AVNQDGASSG LTAPNGPSQQ RVIRRALADA RLTTSDVDVV EAHGTGTRLG DPIEAQAVIA
     TYGQGRDGEQ PLRLGSLKSN IGHTQAAAGV SGVIKMVQAM RHGVLPKTLH VEKPTDQVDW
     SAGAVELLTE AMDWPDKGDG GLRRAAVSSF GVSGTNAHVV LEEAPAAEET PASEATPAVE
     PSVGAGLVPW LVSAKTPAAL DAQIGRLAAF ASQGRTDAAD PGAVARVLAG GRAEFEHRAV
     VLGTGQDDFA QALTAPEGLI RGTPSDVGRV AFVFPGQGTQ WAGMGAELLD VSKEFAAAMA
     ECESALSRYV DWSLEAVVRQ APGAPTLERV DVVQPVTFAV MVSLAKVWQH HGVTPQAVVG
     HSQGEIAAAY VAGALTLDDA ARVVTLRSKS IAAHLAGKGG MISLALSEEA TRQRIENLHG
     LSIAAVNGPT ATVVSGDPTQ IQELAQACEA DGVRARIIPV DYASHSAHVE TIESELAEVL
     AGLSPRTPEV PFFSTLEGAW ITEPVLDGTY WYRNLRHRVG FAPAVETLAT DEGFTHFIEV
     SAHPVLTMTL PETVTGLGTL RREQGGQERL VTSLAEAWTN GLTIDWAPVL PTATGHHPEL
     PTYAFQRRHY WLHDSPAVQG SVQDSWRYRI DWKRLAVADA SERAGLSGRW LVVVPEDRSA
     EAAPVLAALS GAGADPVQLD VSPLGDRQRL AATLGEALAA AGGAVDGVLS LLAWDESAHP
     GHPAPFTRGT GATLTLVQAL EDAGVAAPLW CVTHGAVSVG RADHVTSPAQ AMVWGMGRVA
     ALEHPERWGG LIDLPSDADR AALDRMTTVL AGGTGEDQVA VRASGLLARR LVRASLPAHG
     TASPWWQADG TVLVTGAEEP AAAEAARRLA RDGAGHLLLH TTPSGSEGAE GTSGAAEDSG
     LAGLVAELAD LGATATVVTC DLTDAEAAAR LLAGVSDAHP LSAVLHLPPT VDSEPLAATD
     ADALARVVTA KATAALHLDR LLREAAAAGG RPPVLVLFSS VAAIWGGAGQ GAYAAGTAFL
     DALAGQHRAD GPTVTSVAWS PWEGSRVTEG ATGERLRRLG LRPLAPATAL TALDTALGHG
     DTAVTIADVD WSSFAPGFTT ARPGTLLADL PEARRALDEQ QSTTAADDTV LSRELGALTG
     AEQQRRMQEL VREHLAVVLN HPSPEAVDTG RAFRDLGFDS LTAVELRNRL KNATGLALPA
     TLVFDYPTPR TLAEFLLAEI LGEQAGAGEQ LPVDGGVDDE PVAIVGMACR LPGGVASPED
     LWRLVAGGED AISGFPQDRG WDVEGLYDPD PDASGRTYCR AGGFLDEAGE FDADFFGISP
     REALAMDPQQ RLLLETSWEA VEDAGIDPTS LQGQQVGVFA GTNGPHYEPL LRNTAEDLEG
     YVGTGNAASI MSGRVSYTLG LEGPAVTVDT ACSSSLVALH LAVQALRKGE CGLALAGGVT
     VMSTPTTFVE FSRQRGLAED GRSKAFAASA DGFGPAEGVG MLLVERLSDA RRNGHRVLAV
     VRGSAVNQDG ASNGLTAPNG PSQQRVIRRA LADARLTTAD VDVVEAHGTG TRLGDPIEAQ
     ALIATYGQGR DTEQPLRLGS LKSNIGHTQA AAGVSGIIKM VQAMRHGVLP KTLHVDRPSD
     QIDWSAGTVE LLTEAMDWPR KQEGGLRRAA VSSFGISGTN AHIVLEEAPV DEDAPADEPS
     VGGVVPWLVS AKTPAALDAQ IGRLAAFASQ GRTDAADPGA VARVLAGGRA QFEHRAVALG
     TGQDDLAAAL AAPEGLVRGV ASGVGRVAFV FPGQGTQWAG MGAELLDVSK EFAAAMAECE
     AALAPYVDWS LEAVVRQAPG APTLERVDVV QPVTFAVMVS LAKVWQHHGV TPQAVVGHSQ
     GEIAAAYVAG ALSLDDAARV VTLRSKSIGA HLAGQGGMLS LALSEAAVVE RLAGFDGLSV
     AAVNGPTATV VSGDPTQIQE LAQACEADGV RARIIPVDYA SHSAHVETIE SELADVLAGL
     SPQTPQVPFF STLEGAWITE PALDGGYWYR NLRHRVGFAP AVETLATDEG FTHFVEVSAH
     PVLTMALPET VTGLGTLRRD NGGQHRLTTS LAEAWANGLT VDWASLLPTT TTHPDLPTYA
     FQTERYWPQP DLSAAGDITS AGLGAAEHPL LGAAVALADS DGCLLTGSLS LRTHPWLADH
     AVAGTVLLPG TAFVELAFRA GDQVGCDLVE ELTLDAPLVL PRRGAVRVQL SVGASDESGR
     RTFGLYAHPE DAPGEAEWTR HATGVLAARA DRTAPVADPE AWPPPGAEPV DVDGLYERFA
     ANGYGYGPLF QGVRGVWRRG DEVFADVALP AEVAGAEGAR FGLHPALLDA AVQAAGAGRG
     VRRGHAAAVR LERDLLYAVG ATALRVRLAP AGPDTVSVSA ADSSGQPVFA ADSLTVLPVD
     PAQLAAFSDP TLDALHLLEW TAWDGAAQAL PGAVVLGGDA DGLAAALRAG GTEVLSFPDL
     TDLVEAVDRG ETPAPATVLV ACPAAGPDGP EHVREALHGS LALMQAWLAD ERFTDGRLVL
     VTRDAVAARS GDGLRSTGQA AVWGLGRSAQ TESPGRFVLL DLAGEARTAG DATAGDGLTT
     GDATVGGTSG DAALGSALAT ALGSGEPQLA LRDGALLVPR LARAAAPAAA DGLAAADGLA
     ALPLPAAPAL WRLEPGTDGS LESLTAAPGD AETLAPEPLG PGQVRIAIRA TGLNFRDVLI
     ALGMYPDPAL MGTEGAGVVT ATGPGVTHLA PGDRVMGLLS GAYAPVVVAD ARTVARMPEG
     WTFAQGASVP VVFLTAVYAL RDLADVKPGE RLLVHSAAGG VGMAAVQLAR HWGVEVHGTA
     SHGKWDALRA LGLDDAHIAS SRTLDFESAF RAASGGAGMD VVLNSLAREF VDASLRLLGP
     GGRFVEMGKT DVRDAERVAA DHPGVGYRAF DLGEAGPERI GEMLAEVIAL FEDGVLRHLP
     VTTWDVRRAR DAFRHVSQAR HTGKVVLTMP SGLDPEGTVL LTGGTGALGG IVARHVVGEW
     GVRRLLLVSR RGTDAPGAGE LVHELEALGA DVSVAACDVA DREALTAVLD SIPAEHPLTA
     VVHTAGVLSD GTLPSMTAED VEHVLRPKVD AAFLLDELTS TPGYDLAAFV MFSSAAAVFG
     GAGQGAYAAA NATLDALAWR RRTAGLPALS LGWGLWAETS GMTGGLSDTD RSRLARSGAT
     PMDSELTLSL LDAAMRRDDP ALVPIALDVA ALRAQQRDGM LAPLLSGLTR GSRVGGAPVN
     QRRAAAGGAG EADTDLGGRL AAMTPDDRVA HLRDLVRTHV ATVLGHGTPS RVDLERAFRD
     TGFDSLTAVE LRNRLNAATG LRLPATLVFD HPTPGELAGH LLDELATAAG GSWAEGTGSG
     DTASATDRQT TAALAELDRL EGVLASLAPA AGGRPELAAR LRALAAALGD DGDDATDLDE
     ASDDDLFSFI DKELGDSDF
//
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