ID   BACC_BACLI              Reviewed;        6359 AA.
AC   O68008;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Bacitracin synthase 3;
DE            Short=BA3;
DE   Includes:
DE     RecName: Full=ATP-dependent isoleucine adenylase;
DE              Short=IleA;
DE     AltName: Full=Isoleucine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent D-phenylalanine adenylase;
DE              Short=D-PheA;
DE     AltName: Full=D-phenylalanine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent histidine adenylase;
DE              Short=HisA;
DE     AltName: Full=Histidine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent D-aspartate adenylase;
DE              Short=D-AspA;
DE     AltName: Full=D-aspartate activase;
DE   Includes:
DE     RecName: Full=ATP-dependent asparagine adenylase;
DE              Short=AsnA;
DE     AltName: Full=Asparagine activase;
DE   Includes:
DE     RecName: Full=Aspartate racemase;
DE              EC=5.1.1.13;
DE   Includes:
DE     RecName: Full=Phenylalanine racemase [ATP hydrolyzing];
DE              EC=5.1.1.11;
GN   Name=bacC;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10716 / DSM 603 / NBRC 12199 / NCIMB 8874 / Tracy I;
RX   PubMed=9427658; DOI=10.1016/s1074-5521(97)90301-x;
RA   Konz D., Klens A., Schoergendorfer K., Marahiel M.A.;
RT   "The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716:
RT   molecular characterization of three multi-modular peptide synthetases.";
RL   Chem. Biol. 4:927-937(1997).
CC   -!- FUNCTION: Induces peptide synthesis, activates and incorporates five
CC       amino acids, forms a thiazoline ring between the first two amino acids
CC       and incorporates a D-glutamine in the fourth position.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate = D-aspartate; Xref=Rhea:RHEA:14973,
CC         ChEBI:CHEBI:29990, ChEBI:CHEBI:29991; EC=5.1.1.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-phenylalanine = AMP + D-phenylalanine +
CC         diphosphate + H(+); Xref=Rhea:RHEA:20201, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57981, ChEBI:CHEBI:58095, ChEBI:CHEBI:456215;
CC         EC=5.1.1.11;
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 5 phosphopantetheines covalently. {ECO:0000305};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacitracin biosynthesis.
CC   -!- SUBUNIT: Large multienzyme complex of BA1, BA2 and BA3.
CC   -!- DOMAIN: Consists of five modules with two epimerization domains in the
CC       second and fourth modules, and a putative C-terminal thioesterase
CC       domain. Each module incorporates one amino acid into the peptide
CC       product and can be further subdivided into domains responsible for
CC       substrate adenylation, thiolation, condensation (not for the initiation
CC       module), and epimerization (optional), and N methylation (optional).
CC   -!- MISCELLANEOUS: Bacitracin is a mixture of at least ten cyclic
CC       dodecapeptides, that differ by one or two amino acids. The most
CC       abundant is bacitracin A, a branched cyclic dodecapeptide. It contains
CC       an N-terminal linear pentapeptide moiety (Ile-Cys-Leu-D-Glu-Ile) with
CC       an isoleucine-cysteine thiazoline condensation product and a C-terminal
CC       heptapeptide ring (Lys-D-Orn-Ile-D-Phe-His-D-Asp-Asn), in which the
CC       free alpha-carboxy group of the C-terminal Asn is bound to the epsilon-
CC       amino group of Lys.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF007865; AAC06348.1; -; Genomic_DNA.
DR   PIR; T31679; T31679.
DR   SMR; O68008; -.
DR   ESTHER; bacli-bacc; Thioesterase.
DR   PRIDE; O68008; -.
DR   UniPathway; UPA00179; -.
DR   GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 5.
DR   Gene3D; 3.30.300.30; -; 5.
DR   Gene3D; 3.30.559.10; -; 7.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 5.
DR   Pfam; PF13193; AMP-binding_C; 5.
DR   Pfam; PF00668; Condensation; 7.
DR   Pfam; PF00550; PP-binding; 5.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 5.
DR   SUPFAM; SSF47336; SSF47336; 5.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 5.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 2.
DR   PROSITE; PS00455; AMP_BINDING; 5.
DR   PROSITE; PS50075; CARRIER; 5.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 4.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; Hydrolase; Isomerase; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW   Phosphoprotein; Repeat.
FT   CHAIN           1..6359
FT                   /note="Bacitracin synthase 3"
FT                   /id="PRO_0000193084"
FT   DOMAIN          961..1036
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1993..2067
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3497..3572
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4539..4613
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          6047..6122
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          461..1034
FT                   /note="Domain 1 (isoleucine-activating)"
FT   REGION          941..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1517..2064
FT                   /note="Domain 2 (D-phenylalanine-activating)"
FT   REGION          2999..3570
FT                   /note="Domain 3 (histidine-activating)"
FT   REGION          4047..4612
FT                   /note="Domain 4 (D-aspartic acid-activating)"
FT   REGION          4521..4544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          5549..6129
FT                   /note="Domain 5 (asparagine-activating)"
FT   MOD_RES         996
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2028
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3532
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4574
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         6082
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   6359 AA;  722943 MW;  82A273C546253074 CRC64;
     MKTKVEKIYP LSNMQKGMLF HAMKDEASHA YFEQFIIELK GDVDERMFEE SLNEVMKRHE
     ILRASFHHRL DEPLHVIIKD RHMKFDYLDI RGRHDQDGVL ERYLAEDRQK GFDLAKDTLM
     RACLIRMSDD SYQFVWTYHH ILLDGWCLGI ILDELLTIYE MKRKGQNHQL EDPRPYSDYI
     KWLEDQDKEE AQSYWESYLS GYDQKNSLPK LRTPSETGFK RREKTIECSK ELTNRLIKLA
     NRNHVTINTV LQSIWGVILA KYNNSEDVVF GTVVSGRDAE VEGIETMVGV FINTIPTRIR
     LDKDKLFKDV LRQTQADALE SSRYNYMNLA EVQALSELKN DLIDHVMVFE NYAVDQKAFE
     EKNDVGFEMV NVSGEEQTNY HFSISAALDD QLKLLFIYDE NVYDTTIIET LEKHIITVAE
     QVAEDETQTL RDINLVSKEE QHRILDTFND TKTGYPKDKP LHELFEEQAM KTPDHTALVF
     GAQRMTYREL NEKANQTARL LREKGIGRGS IAAIIADRSF EMIIGIIGIL KAGGAYLPID
     PETPKHRIAF MLSDTKAGVL LAQGKAADGI DCEADIIHLD KGVADGFSKK RLSSVNDSGD
     TAYIIYTSGS TGMPKGVVTP HYSAARVVKN TNYIDITEDD AILQLSNYSF DGSVFDIFGA
     LLNGASLVLI EKETVLNTHE LAEVIKKEQV SVMFITTALF NTLADINIGC LAKLRKIFLG
     GERASIPHVR KVLNHVGRDK LIHVYGPTES TVYATYYFIN EIDDEAETIP IGSPLANTSV
     LIMDEAGKLL PIGVPGELCI AGDGLSKGYL NREELTAEKF IPHPFIPGER LYKTGDLAKW
     LPDGNIEFIG RIDHQVKIRG FRIELGEIES RLEMHEDINE TIVTVREDEE SRPYICAYIT
     ANREISLDEL KGFLGEKLPE YMIPAYFVKM DKLPLTKNGK VDRKALPEPD RTAGAENEYE
     APRNETEEKL AAIWRDILKV EKSGINDHFF EMGGHSLKAA AMAARIRKEL KAEIPLGQIF
     KTPTIKGLGE YIRSTKDSVY SSIQKVEEKE YYRLSSAQKR LYILDQIEGS GLSYNIPFTM
     KVKGRFDIRR FENALKTIIQ RHEALRTSFL MADGEPVQKI EKEVDFSIKC SKIQSLSIQE
     IIKQFVRPFD LKKAPLFRTE VVKVDDEEHI ILFDMHHIIS DGASMGVLTK EICDLYGGKE
     LKPLSLQYKD YSEWQRDFYQ KDEMKRQKEY WLNIFKGEIP VLNMPTDYPR PQMHSVEGDR
     IGFAIDGELT KKLKRIAKDN GATMYMLLLA AYTVLLRTYS GQEDVIIGTP IQGRKHHELK
     HVIGMFVNTL AMRNHPKGDK TFAEYLQDVK ETALKAYENQ DYQFDDLVEQ LDLERDMSRN
     PLFDTMFVLQ NLEKADAEIE GLTFEPFESD IHISKFDLTL SAIEKDSKIE FDLEYCTKLF
     KRETVERMAA HFVRVLEDIS KRTDKRLDQI EAMSEDEKNT LLYRFNDTKT DAPTDKTICQ
     LFAERAETSP DKTAVVFEDQ TLTYRQLHER SNQLARFLRE KGVQPDTAVG IMVDRSPEMI
     IGLLGILKAG GAYLPLDPAY PEDRIKYILG DSQTKFLLSE EALIKKRAFI KEADMINIDI
     HDKQIAAQDA AQLEPVSRSG DLAYIIYTSG STGKPKGVLI EQKGLSNLVS AVVKLMHLNT
     GSRVIQFASL SFDASAFEIF PALAAGSALV LGRQEEMMPG QPLTSFLRQY NITHATLPPT
     VLDVLNESGL ENLKVIVSAG SACSEELAKR WSGNRLFINA YGPTETTVCA TAGIYEGSGR
     PHIGSPIANT NVYVLDQNQK PVPTGVVGEL CVGGMSLARG YLNRPELTAE KFISHPFASG
     ERLYRTGDLA RWLPDGHLEF LGRIDHQVKI RGYRIELGEI ENQLLKLDKI DEAAVIARKD
     DDHSDYLCAY IVSKEDWTST EISEWLEKEL PHYMIPAYFV RLDKLPLTSN DKVDRKALPA
     PDRHVATGAV YEAPRNDTEA KLVDIWRDVL GAGDIGISHH FFAAGGDSIK ALQIVSRLSR
     LGLKLEMKDL FANPRIKDLA KYVKKQSQRK NANTIVTGHA ELTPIQKWYF ANNKEELDHF
     NQSFVLFRKG GFDESCVKKA FNKIMEQHDA LRMIYEEKGG DFIQYNRSFR EDLFDLDVYD
     VRGLDRQAEK VYELATSIQK LSSIRKGKLV HLGIFRADEG DHLLIVIHHL VVDGVSWRIL
     FEDFETLYSQ ALKGQTLEIG YKTDSYQEFA RRLKAYAHSR TLSKEAEYWR NIAKARVRFI
     PPKNVLKEDV YENSTTLSIK LGKEATADLL RNTNRAYNTE INDILLTALL TGARDITGEN
     KLKVMMEGHG REDILEGVDI TRTIGWFTTM YPVLLDAGEE KALSQQIKMV KETLRKIPNK
     GIGYGLLKYM AEDPDFTNEE KARISFNYLG DIDADMNRGE FSGSSFSEGE SIGGKIARSH
     SIEINAIVMN HELVIHTTFN QMEYEKDTIS RLNHQLKERL EQIIKHCTQQ TESERTPSDY
     GDTNISLAEL EEIKGKYRSA IEKIYPLANM QKGMLFHAIE DHTSDAYFQQ TVMDIEGYVD
     PAILEASFND IMKRHEILRA SYEYEIVEEP RQIIIENRSI DFTYFNIAKS SAQQQEMFIE
     RLLNEDRKKG FDLSKDVLMR AYLLKTAERS YRLVWSHHHI LLDGWCLGII MRELFVIYEN
     RMNGKASPLK ETKPYSDYIK WLERQDQEEA RQYWREYLKG YEEQAQLPTL TKRKKSSRYD
     RREKVIHLSK QLTKQLKELA AKNSVTLHTV IQTIWGLMLT RYTKIDDVVF GTVVSGREAN
     VDGIEDMIGL FINTIPTRIR FNEQARFNDC LQKVQEDAIQ SNRYNYMNLA EVQALSSLKK
     DLIDHILVFE NYEADEQDFE ESQMKTGFKV NEISAAEQSI TAFSMSVTPG EELTLVLTYD
     GNVYDRDIIN NIEGHIKRVA EQVTANENRK IAEIDMLAEE ERKTLLYEFN RTNADYPRNK
     TIHQLFEEQA ERTPGHTAVV FEKEELSYKA LNERSNQLAG LLREKGVKPD MIVGVMAERS
     VEMIVGMLAV LKAGGAYLPI DPEYPEDRIR YMIEDSGISI LLKKADKQID VDFTCIDMNE
     KGLAKDMAAE NLGHTSGSSD MAYVIYTSGS TGKPKGVMVN HQSIVNTLYW RKQSYGYSTA
     DATLQVPSFS FDSSVEDIFT TLISGAKLVL IRDLRMNPRE IIGVLRTHKA TNLLAVPSFY
     LNLLDTIEQP LDDLRFVTVA GEGFNESLIR QHFEKLPNVK LFNEYGPTEN SVCSTRGELR
     KDDEKVVIGR PISNHKVYIL NHNQQLLPLG TPGELCLSGE GLARGYLNRP DLTLEKFVPN
     PFAPGESMYR TGDLARFLPD GQIEYLGRID HQVKIRGFRI ELGEIENQLL KIEGIDAAAV
     MAREDQAGGK YLCAYIVADK AAGVADVRKC LLKELPDYMV PSYFVKLDQL PLTANGKIDR
     KALPEPSSTI SEATYEAPRN RTEEKLVSIW EDVLGIENIG ISHNFFELGG HSLKAAALTA
     KLHKEMKIEV PLRQLFETPT IKDIGDFIES MKESPYASIT QAEEKEYYAL SSAQRRLYIL
     NQIEPGGLSY NMPFAMKIAG DFDVDRFEDA FRQLIERHEA LRTAFVMVDG EPVQKIEKEV
     DFKVKYGRLG QDPLEEKIKA FIKPFALEKA PLLRAEVLKA SGDEHVLMLD MHHIISDGVS
     MAIFTRELAE LYEGKTLPPL TIQYKDFSEW QKLFYQKDEV KRQEDYWLNV FQGEVPVLNL
     PADEKRPQKR SIEGDIVQFE IDGETSAMLN KLAKENGATM YMLLLAGYTT LLAKYTGQED
     IVVGSPIAGR HHSDLKHVIG LFINTLAMRN HPKGDMPFAD YLKEVKETAL KAYENQDYPF
     DELVEKLDVK RDMSRHPLFD TMLVLQNFDG DEADIDGLTF QPLQTEVNIS KFDLTLTAAE
     TNEGIQCVFN YSTKLFKRST IERMAGHLIN ILKEAANDPH MPLSDVNMLS DEEMNALLDQ
     NQGKQADYPQ DQTVHQLFEQ QADKTPEQTA VVYADEKLTY RELNERANQL ARLLRDKGAD
     ADQPVAIMIE PSLEMIISML AVLKAGAAYV PIEPEQLAKR TNEILSDSRA AILLVKGSVK
     ENVAFAGEIV NVADGLIDAK VASNLSASGS ADQNAYIIYT SGSTGKPKGV FVRHGNVVNY
     TTWFMKEAGL TENDKAMLVS SYAFDLGYTS IFSALLSGSE LHIARKECYT NAHRALKYIK
     ENGITYIKLT PSLFNIFVND PGFSAEKPCA TLRLVVLGGE MINTRDVETF YNQYPDHVVM
     NHYGPTETTI GSVFKVIDPE HLDSFKECPV IGTPIHNTNA YVLDENMKLL PEGVYGELCI
     AGAGVTGGYV NRPDETKEKF IENPFAPHTK MYRTGDLARR LSDGNIELAG RIDTQVKVRG
     YRIEPEEIKN RLLAHDDIKE AFIAAREDHK GAKQLCAYFT ADAELPFEDI RTYLMHELPE
     YMIPSSFVQI EKMPLSANGK IDTAALPEPQ PGKETEYEPP RNETEEKLVQ IWEEVLGIDK
     IGITHHFFAA GGDSIKALQM ISRLSREGLS LEMKDLFANP QIKSLSRYVK AESDKSASYE
     TVEGEVLLTP IQQEYFSLNK TDRNHYNHAV MLYRKNGFDE SIVKRVFKEI IKHHDALRTV
     FTEEDGKIIQ YNRGPDKQLF DLFVYDVSSE NDQPQKVYQL ATELQQSIDI ETGPLVKLAV
     FKTNNGDHLL IIIHHLVVDG ISWRILFEDL AIGYSQLANG EKVEFYPKTA SYQAYARHIA
     EYAKSVKLLS EKQYWLKAIA EGVEFLDMNE NAGAFKVEDS RTFSTELEKE ETKRLLRETN
     RAYHTEINDI LITALLVAAR DMNGQNQLRI TLEGHGREQV ADGIDISRTV GWFTSKYPVF
     IDLGQETDMS RTIKMVKEHL RNVPNKGIGY GILKYLTRDS EIAKGAASPI LFNYLGQLDE
     DINSGEFSSS HLSPGEAAGK GITREHPLEI NAVVFRGKLA IQTTYNTRAY SEDVVRAFAQ
     NYKEALKAVI RHCAEREETE KTPSDYGDKG ISLDQLEEIK LKYKGMEIEK IYPLANMQRG
     MLFHALEDKE SQAYFEQMAI NMKGLIDERL FAETFNDIME RHEILRASIE YEITDEPRNV
     IIKDRKINLD YHDLRKQSPA EREQVIQAYR KADREKGFRL NSEPLIRAAL MRTEDDSYTF
     IWTNHHILLD GWSRGIIMGE LFHMYHMKEA RQKHRLEEAR PYSDYIGWLQ QQDKEAAKAY
     WRNYLSGFTE KSPISVLAGS SGHAKYKRKE AVIEFPEQLT GRITELASRN NVTFHTVLQC
     IWGMLLARYN QTDDVVFGTV ISGRDAQVTG IEKMVGLFIN TVPTRIRLDK SQSFKELIKS
     VQEQALEGRT YHDMNLSEVQ SLSELKRELL DHILIFENYA VDQSAFETSG KRGAGFVFEE
     IHAEEQTNYG FNIVAVPGER LVIKLTYDGN IYHDHIIAGI KGHLQQVMEQ VVQHEDQSLN
     DITVLSEAER NRLLYEWNDT KAEYPNQTIH RLFEEQAEKT PELAAVVSGN DKLTYRELNE
     KSNQLARYLR DKGVKADTIV AIMAERSPEM VVGIMGILKA GGAYLPIDPD YPEERIKYML
     EDSGAAIILA DHKQDLGTLH QEAVELTGDF SSYPADNLEP AGNADSLAYI IYTSGSTGKP
     KGVMIRQRGL VNYITWADRV YVQGEQLDFA LYSSIAFDLT VTSIFTPLIS GNRVIVYRHS
     EDGEPLIRKV FRDQKAGIVK LTPSHLSLVK DMDASGSSIK RLIVGGEDLK TELAKEITER
     FHHNIEIYNE YGPTETVVGC MIYQYDAGWD RQVSVPIGKP ASNVQLYILD ERQEVQPVGI
     AGELYISGDG VAKGYLNKPE LTSEKFLPNP FLPGERMYRT GDLAKMRPDG HIEYLGRIDH
     QVKIRGYRIE LGEIEHQLLR HSDIKEAAVA AKTDQNNDQV LCAYVVSERD ITQKDIKTFL
     AKELPEYMVP SYLLKLDELP LTPNGKVDLK ALPEPDRSAG ALLEYEPPRH ELEEKMAAIW
     EDILNIEQIG INANIFDIGA NSLNVMSFVS RLYAELGFRV PFKDIFSKPT IKELSDFLKH
     AQDLLKDYTD DCMQLTRAEE GGKNLFCFPP AASMGIAYMG LAKHLKQHSV YSFNFIPSAN
     RIRKYADIIK NIQGEGPYTL IGYSSGGILA FDVAKELNRQ GYEVEDLIII DSKYRTKAEK
     HQFTEEEYRE EISKTFELEK YRDVEKLLSD YLVDLVMKSY VYIQNTVTTG AIDGHISYIK
     SSDNQRGENM MMWEKATSKT FTVVQGAGTH MQMISKSHPD ILERNARLIH DIINKTVKI