ID GRSB_ANEMI Reviewed; 4451 AA.
AC P0C063; P14688; Q44928;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-NOV-2024, entry version 81.
DE RecName: Full=Gramicidin S synthase 2;
DE AltName: Full=Gramicidin S synthase II;
DE Includes:
DE RecName: Full=ATP-dependent proline adenylase;
DE Short=ProA;
DE AltName: Full=Proline activase;
DE Includes:
DE RecName: Full=ATP-dependent valine adenylase;
DE Short=ValA;
DE AltName: Full=Valine activase;
DE Includes:
DE RecName: Full=ATP-dependent ornithine adenylase;
DE Short=OrnA;
DE AltName: Full=Ornithine activase;
DE Includes:
DE RecName: Full=ATP-dependent leucine adenylase;
DE Short=LeuA;
DE AltName: Full=Leucine activase;
GN Name=grsB; Synonyms=grs2;
OS Aneurinibacillus migulanus (Bacillus migulanus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=47500;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCIMB 7096 / NCTC
RC 7096;
RX PubMed=1560782; DOI=10.1111/j.1365-2958.1992.tb01498.x;
RA Turgay K., Krause M., Marahiel M.A.;
RT "Four homologous domains in the primary structure of GrsB are related to
RT domains in a superfamily of adenylate-forming enzymes.";
RL Mol. Microbiol. 6:529-546(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
RC STRAIN=ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCIMB 7096 / NCTC
RC 7096;
RX PubMed=2477357; DOI=10.1128/jb.171.10.5422-5429.1989;
RA Kraetzschmar J., Krause M., Marahiel M.A.;
RT "Gramicidin S biosynthesis operon containing the structural genes grsA and
RT grsB has an open reading frame encoding a protein homologous to fatty acid
RT thioesterases.";
RL J. Bacteriol. 171:5422-5429(1989).
CC -!- FUNCTION: This protein is a multifunctional enzyme, able to activate
CC and polymerize the amino acids Pro, Val, Orn and Leu. Activation sites
CC for these AA consist of individual domains.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Note=Binds 4 phosphopantetheines covalently.;
CC -!- PATHWAY: Antibiotic biosynthesis; gramicidin S biosynthesis.
CC -!- SUBUNIT: Large multienzyme complex of GrsA and GrsB.
CC -!- DOMAIN: Consists of four modules, and harbors a putative thioesterase
CC domain at its C-terminal end. Each module incorporates one amino acid
CC into the peptide product and can be further subdivided into domains
CC responsible for substrate adenylation, thiolation, condensation (not
CC for the initiation module), and epimerization (optional), and N
CC methylation (optional).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61658; CAA43838.1; -; Genomic_DNA.
DR EMBL; M29703; AAA58719.1; -; Genomic_DNA.
DR EMBL; X15577; CAA33604.1; -; Genomic_DNA.
DR PIR; S20542; YGBSG2.
DR PDB; 8P5O; X-ray; 2.60 A; A/B/C/D=460-862.
DR PDBsum; 8P5O; -.
DR SMR; P0C063; -.
DR STRING; 47500.AF333_17645; -.
DR KEGG; ag:CAA43838; -.
DR BioCyc; MetaCyc:MONOMER-14129; -.
DR UniPathway; UPA00102; -.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd17650; A_NRPS_PpsD_like; 1.
DR CDD; cd17656; A_NRPS_ProA; 1.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd19543; DCL_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 3.
DR FunFam; 3.30.300.30:FF:000010; Enterobactin synthetase component F; 3.
DR FunFam; 3.30.559.10:FF:000012; Non-ribosomal peptide synthetase; 1.
DR FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 4.
DR FunFam; 3.40.50.980:FF:000001; Non-ribosomal peptide synthetase; 4.
DR FunFam; 2.30.38.10:FF:000001; Non-ribosomal peptide synthetase PvdI; 4.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 4.
DR Gene3D; 3.30.300.30; -; 4.
DR Gene3D; 3.40.50.980; -; 8.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 4.
DR Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 4.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase_fold.
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_com.
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; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 4.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 4.
DR Pfam; PF13193; AMP-binding_C; 4.
DR Pfam; PF00668; Condensation; 4.
DR Pfam; PF00550; PP-binding; 4.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 4.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 8.
DR PROSITE; PS00455; AMP_BINDING; 4.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Hydrolase; Ligase;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..4451
FT /note="Gramicidin S synthase 2"
FT /id="PRO_0000193087"
FT DOMAIN 971..1046
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2006..2081
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3052..3127
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4090..4165
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 467..1044
FT /note="Domain 1 (proline-activating)"
FT /evidence="ECO:0000250"
FT REGION 1521..2080
FT /note="Domain 2 (valine-activating)"
FT /evidence="ECO:0000250"
FT REGION 2538..3135
FT /note="Domain 3 (ornithine-activating)"
FT /evidence="ECO:0000250"
FT REGION 3591..4173
FT /note="Domain 4 (leucine-activating)"
FT MOD_RES 1006
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2041
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3087
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4125
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 655..665
FT /note="TCSFDVCYQEI -> NAVLTCVTKKF (in Ref. 1; CAA43838)"
FT /evidence="ECO:0000305"
FT CONFLICT 942..947
FT /note="QLPLTP -> HVRLHL (in Ref. 1; CAA43838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240..1304
FT /note="YWLNVFTEEIPVLNLPTDYPRPTIQSFDGKRFTFSTGKQLMDDLYKVATETG
FT TTLYMVLLAAYNV -> SLAERICRRDSSIESTDRLPKYQPFKALMVKDLHSVQESSLW
FT MIYTRWQQKQEQHYIWFYLLRIMF (in Ref. 1; CAA43838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504..1520
FT /note="HMQTIQGLFEEQVEKTP -> LCKQFKDYLRNRWRRRA (in Ref. 1;
FT CAA43838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2842..2849
FT /note="CIDSSYYE -> ALILAIMN (in Ref. 1; CAA43838)"
FT /evidence="ECO:0000305"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 496..512
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 529..541
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 554..560
FT /evidence="ECO:0007829|PDB:8P5O"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 628..641
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 648..651
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 660..669
FT /evidence="ECO:0007829|PDB:8P5O"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 680..683
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 700..704
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 705..711
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 715..720
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 739..748
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 751..756
FT /evidence="ECO:0007829|PDB:8P5O"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 788..793
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 806..812
FT /evidence="ECO:0007829|PDB:8P5O"
FT HELIX 823..829
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 830..832
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 839..850
FT /evidence="ECO:0007829|PDB:8P5O"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:8P5O"
SQ SEQUENCE 4451 AA; 509254 MW; 1C6DBA8B27636121 CRC64;
MSTFKKEHVQ DMYRLSPMQE GMLFHALLDK DKNAHLVQMS IAIEGIVDVE LLSESLNILI
DRYDVFRTTF LHEKIKQPLQ VVLKERPVQL QFKDISSLDE EKREQAIEQY KYQDGETVFD
LTRDPLMRVA IFQTGKVNYQ MIWSFHHILM DGWCFNIIFN DLFNIYLSLK EKKPLQLEAV
QPYKQFIKWL EKQDKQEALR YWKEHLMNYD QSVTLPKKKA AINNTTYEPA QFRFAFDKVL
TQQLLRIANQ SQVTLNIVFQ TIWGIVLQKY NSTNHVVYGS VVSGRPSEIS GIEKMVGLFI
NTLPLRIQTQ KDQSFIELVK TVHQNVLFSQ QHEYFPLYEI QNHTELKQNL IDHIMVIENY
PLVEELQKNS IMQKVGFTVR DVKMFEPTNY DMTVMVLPRD EISVRLDYNA AVYDIDFIKK
IEGHMKEVAL CVANNPHVLV QDVPLLTKQE KQHLLVELHD SITEYPDKTI HQLFTEQVEK
TPEHVAVVFE DEKVTYRELH ERSNQLARFL REKGVKKESI IGIMMERSVE MIVGILGILK
AGGAFVPIDP EYPKERIGYM LDSVRLVLTQ RHLKDKFAFT KETIVIEDPS ISHELTEEID
YINESEDLFY IIYTSGTTGK PKGVMLEHKN IVNLLHFTFE KTNINFSDKV LQYTTCSFDV
CYQEIFSTLL SGGQLYLIRK ETQRDVEQLF DLVKRENIEV LSFPVAFLKF IFNEREFINR
FPTCVKHIIT AGEQLVVNNE FKRYLHEHNV HLHNHYGPSE THVVTTYTIN PEAEIPELPP
IGKPISNTWI YILDQEQQLQ PQGIVGELYI SGANVGRGYL NNQELTAEKF FADPFRPNER
MYRTGDLARW LPDGNIEFLG RADHQVKIRG HRIELGEIEA QLLNCKGVKE AVVIDKADDK
GGKYLCAYVV MEVEVNDSEL REYLGKALPD YMIPSFFVPL DQLPLTPNGK IDRKSLPNLE
GIVNTNAKYV VPTNELEEKL AKIWEEVLGI SQIGIQDNFF SLGGHSLKAI TLISRMNKEC
NVDIPLRLLF EAPTIQEISN YINGAKKESY VAIQPVPEQE YYPVSSVQKR MFILNEFDRS
GTAYNLPGVM FLDGKLNYRQ LEAAVKKLVE RHEALRTSFH SINGEPVQRV HQNVELQIAY
SESTEDQVER IIAEFMQPFA LEVRPLLRVG LVKLEAERHL FIMDMHHIIS DGVSMQIMIQ
EIADLYKEKE LPTLGIQYKD FTVWHNRLLQ SDVIEKQEAY WLNVFTEEIP VLNLPTDYPR
PTIQSFDGKR FTFSTGKQLM DDLYKVATET GTTLYMVLLA AYNVFLSKYS GQDDIVVGTP
IAGRSHADVE NMLGMFVNTL AIRSRLNNED TFKDFLANVK QTALHAYENP DYPFDTLVEK
LGIQRDLSRN PLFDTMFVLQ NTDRKSFEVE QITITPYVPN SRHSKFDLTL EVSEEQNEIL
LCLEYCTKLF TDKTVERMAG HFLQILHAIV GNPTIIISEI EILSEEEKQH ILFEFNDTKT
TYPHMQTIQG LFEEQVEKTP DHVAVGWKDQ TLTYRELNER ANQVARVLRQ KGVQPDNIVG
LLVERSPEML VGIMGILKAG GAYLPLDPEY PADRISYMIQ DCGVRIMLTQ QHLLSLVHDE
FDCVILDEDS LYKGDSSNLA PVNQAGDLAY IMYTSGSTGK PKGVMVEHRN VIRLVKNTNY
VQVREDDRII QTGAIGFDAL TFEVFGSLLH GAELYPVTKD VLLDAEKLHK FLQANQITIM
WLTSPLFNQL SQGTEEMFAG LRSLIVGGDA LSPKHINNVK RKCPNLTMWN GYGPTENTTF
STCFLIDKEY DDNIPIGKAI SNSTVYIMDR YGQLQPVGVP GELCVGGDGV ARGYMNQPAL
TEEKFVPNPF APGERMYRTG DLARWLPDGT IEYLGRIDQQ VKIRGYRIEP GEIETLLVKH
KKVKESVIMV VEDNNGQKAL CAYYVPEEEV TVSELREYIA KELPVYMVPA YFVQIEQMPL
TQNGKVNRSA LPKPDGEFGT ATEYVAPSSD IEMKLAEIWH NVLGVNKIGV LDNFFELGGH
SLRAMTMISQ VHKEFDVELP LKVLFETPTI SALAQYIADG QKGMYLAIQP VTPTDYYPVS
SAQKRMYILY EFEGAGITYN VPNVMFIEGK LDYQRFEYAI KSLVNRHEAL RTSFYSLNGE
PVQRVHQNVE LQIAYSEAKE DEIEQIVESF VQPFDLEIAP LLRVGLVKLA SDRYLFLMDM
HHIISDGVSM QIITKEIADL YKGKELAELH IQYKDFAVWQ NEWFQSDALE KQKTYWLNTF
AEDIPVLNLS TDYPRPTIQS FEGDIVTFSA GKQLAEELKR LAAETGTTLY MLLLAAYNVL
LHKYSGQEEI VVGTPIAGRS HADVENIVGM FVNTLALKNT PIAVRTFHEF LLEVKQNALE
AFENQDYPFE NLIEKLQVRR DLSRNPLFDT MFSLSNIDEQ VEIGIEGLNF SPYEMQYWIA
KFDISFDILE KQDDIQFYFN YCTNLFKKET IERLATHFMH ILQEIVINPE IKLCEINMLS
EEEQQRVLYD FNGTDATYAT NKIFHELFEE QVEKTPDHIA VIDEREKLSY QELNAKANQL
ARVLRQKGVQ PNSMVGIMVD RSLDMIVGML GVLKAGGAYV PIDIDYPQER ISYMMEDSGA
ALLLTQQKLT QQIAFSGDIL YLDQEEWLHE EASNLEPIAR PHYIAYIIYT SGTTGKPKGV
MIEHQSYVNV AMAWKDAYRL DTFPVRLLQM ASFAFAFDVS AGDFARALLT GGQLIVCPNE
VKMDPASLYA IIKKYDITIF EATPALVIPL MEYIYEQKLD ISQLQILIVG SDSCSMEDFK
TLVSRFGSTI RIVNSYGVTE ACIDSSYYEQ PLSSLHVTGT VPIGKPYANM KMYIMNQYLQ
IQPVGVIGEL CIGGAGVARG YLNRPDLTAE KFVPNPFVPG EKLYRTGDLA RWMPDGNVEF
LGRNDHQVKI RGIRIELGEI EAQLRKHDSI KEATVIARED HMKEKYLCAY MVTEGEVNVA
ELRAYLANDR AAMIPSYFVS LEAMPLTANG KIDKRSLPEP DGSISIGTEY DRPRTMLEGK
LEEIWKDVLG LQRVGIHDDF FTIGGHSLKA MAVISQVHKE CQTEVPLRVL FETPTIQGLA
KYIEETDTEQ YMAIQPVSGQ DYYPVSSAQK RMFIVNQFVG VGISYNMPSI MLIEGKLERT
RLESAFKRLI ERHESLRTSF EIINGKPVQK IHEEVDFNMS YQVASNEQVE KMIDEFIQPF
DLSVAPLLRV ELLKLEEDRH VLIFDMHHII SDGISSNILM KELGELYQGN ALPELRIQYK
DFAVWQNEWF QSEAFKKQEE YWVNVFADER PILDIPTDYP RPMQQSFDGA QLTFGTGKQL
MDGLYRVATE TGTTLYMVLL AAYNVLLSKY SGQEDIIVGT PIVGRSHTDL ENIVGMFVNT
LAMRNKPEGE KTFKAFVSEI KQNALAAFEN QDYPFEELIE KLEIQRDLSR NPLFDTLFSL
QNIGEESFEL AELTCKPFDL VSKLEHAKFD LSLVAVVFEE EIAFGLQYCT KLYKEKTVEQ
LAQHFIQIVK AIVENPDVKL SDIDMLSEEE KKQIMLEFND TKIQYTQNQT IQELFEEQVK
KTPEHIAIVW EGQALIYHEL NIKANQLARV LREKGVTPNH PVAIMTERSL EMIVGIFSIL
KAGGAYVPID PAYPQERIQY LLEDSGAALL LTQSHVLNKL PVDIEWLDLT DEQNYVEDGT
NLPFMNQSTD LAYIIYTSGT TGKPKGVMIE HQSIINCLQW RKEEYEFGPG DTALQVFSFA
FDGFVASLFA PILAGATSVL PKEEEAKDPV ALKKLIASEE ITHYYGVPSL FSAILDVSSS
KDLQNLRCVT LGGEKLPAQI VKKIKEKNKE IEVNNEYGPT ENSVVTTIMR DIQVEQEITI
GRPLSNVDVY IVNCNHQLQP VGVVGELCIG GQGLARGYLN KPELTADKFV VNPFVPGERM
YKTGDLAKWR SDGMIEYVGR VDEQVKVRGY RIELGEIESA ILEYEKIKEA VVMVSEHTAS
EQMLCAYIVG EEDVLTLDLR SYLAKLLPSY MIPNYFIQLD SIPLTPNGKV DRKALPEPQT
IGLMAREYVA PRNEIEAQLV LIWQEVLGIE LIGITDNFFE LGGHSLKATL LVAKIYEYMQ
IEMPLNVVFK HSTIMKIAEY ITHQESENNV HQPILVNVEA DREALSLNGE KQRKNIELPI
LLNEETDRNV FLFAPIGAQG VFYKKLAEQI PTASLYGFDF IEDDDRIQQY IESMIQTQSD
GQYVLIGYSS GGNLAFEVAK EMERQGYSVS DLVLFDVYWK GKVFEQTKEE EEENIKIIME
ELRENPGMFN MTREDFELYF ANEFVKQSFT RKMRKYMSFY TQLVNYGEVE ATIHLIQAEF
EEEKIDENEK ADEEEKTYLE EKWNEKAWNK AAKRFVKYNG YGAHSNMLGG DGLERNSSIL
KQILQGTFVV K
//
