AFLP_ASPPU
ID AFLP_ASPPU Reviewed; 418 AA.
AC Q12120; A0A0F0HZ60;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Sterigmatocystin 8-O-methyltransferase {ECO:0000303|PubMed:8434913};
DE EC=2.1.1.110 {ECO:0000269|PubMed:8434913};
DE AltName: Full=Aflatoxin biosynthesis protein P {ECO:0000303|PubMed:15006741};
DE Flags: Precursor;
GN Name=aflP {ECO:0000303|PubMed:15006741}; Synonyms=omt-1, omtA;
GN ORFNames=P875_00052999-1;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=8285664; DOI=10.1128/aem.59.11.3564-3571.1993;
RA Yu J., Cary J.W., Bhatnager D., Cleveland T.E., Keller N.P., Chu F.S.;
RT "Cloning and characterization of a cDNA from Aspergillus parasiticus
RT encoding an O-methyltransferase involved in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 59:3564-3571(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=70;
RA Yu J.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=7557460; DOI=10.1016/0378-1119(95)00397-o;
RA Yu J., Chang P.-K., Payne G.A., Cary J.W., Bhatnagar D., Cleveland T.E.;
RT "Comparison of the omtA genes encoding O-methyltransferases involved in
RT aflatoxin biosynthesis from Aspergillus parasiticus and A. flavus.";
RL Gene 163:121-125(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=1339261; DOI=10.1128/aem.58.11.3527-3537.1992;
RA Skory C.D., Chang P.K., Cary J., Linz J.E.;
RT "Isolation and characterization of a gene from Aspergillus parasiticus
RT associated with the conversion of versicolorin A to sterigmatocystin in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 58:3527-3537(1992).
RN [7]
RP PROTEIN SEQUENCE OF 42-63, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56774 / SRRC 163 / avn-1;
RX PubMed=8434913; DOI=10.1128/aem.59.2.479-484.1993;
RA Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
RA Ullah A.H.J.;
RT "Purification of a 40-kilodalton methyltransferase active in the aflatoxin
RT biosynthetic pathway.";
RL Appl. Environ. Microbiol. 59:479-484(1993).
RN [8]
RP FUNCTION.
RX PubMed=8368836; DOI=10.1128/aem.59.8.2486-2492.1993;
RA Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic
RT acid to averufin.";
RL Appl. Environ. Microbiol. 59:2486-2492(1993).
RN [9]
RP FUNCTION.
RX PubMed=8368837; DOI=10.1128/aem.59.8.2493-2500.1993;
RA Yabe K., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: cyclase reaction in the
RT conversion of versiconal to versicolorin B and racemization of versiconal
RT hemiacetal acetate.";
RL Appl. Environ. Microbiol. 59:2493-2500(1993).
RN [10]
RP FUNCTION.
RX PubMed=10543813; DOI=10.1128/aem.65.11.4987-4994.1999;
RA Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
RT "Cloning and characterization of the O-methyltransferase I gene (dmtA) from
RT Aspergillus parasiticus associated with the conversions of
RT demethylsterigmatocystin to sterigmatocystin and
RT dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in aflatoxin
RT biosynthesis.";
RL Appl. Environ. Microbiol. 65:4987-4994(1999).
RN [11]
RP FUNCTION.
RX PubMed=10584035; DOI=10.1128/aem.65.12.5639-5641.1999;
RA Zhou R., Linz J.E.;
RT "Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
RT Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 65:5639-5641(1999).
RN [12]
RP FUNCTION.
RX PubMed=11055914; DOI=10.1128/aem.66.11.4715-4719.2000;
RA Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G., Bhatnagar D.,
RA Cleveland T.E.;
RT "adhA in Aspergillus parasiticus is involved in conversion of 5'-
RT hydroxyaverantin to averufin.";
RL Appl. Environ. Microbiol. 66:4715-4719(2000).
RN [13]
RP FUNCTION.
RX PubMed=16256699; DOI=10.1006/bioo.2001.1216;
RA Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
RA Townsend C.A.;
RT "Hexanoate synthase, a specialized type I fatty acid synthase in aflatoxin
RT B1 biosynthesis.";
RL Bioorg. Chem. 29:293-307(2001).
RN [14]
RP FUNCTION.
RX PubMed=11996570; DOI=10.1021/ja012185v;
RA Udwary D.W., Casillas L.K., Townsend C.A.;
RT "Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
RT cytochrome P-450 in the final step of aflatoxin biosynthesis.";
RL J. Am. Chem. Soc. 124:5294-5303(2002).
RN [15]
RP REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [16]
RP FUNCTION.
RX PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT formation.";
RL Appl. Environ. Microbiol. 70:6518-6524(2004).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=14722624; DOI=10.1007/s00203-003-0643-3;
RA Lee L.W., Chiou C.H., Klomparens K.L., Cary J.W., Linz J.E.;
RT "Subcellular localization of aflatoxin biosynthetic enzymes Nor-1, Ver-1,
RT and OmtA in time-dependent fractionated colonies of Aspergillus
RT parasiticus.";
RL Arch. Microbiol. 181:204-214(2004).
RN [18]
RP FUNCTION.
RX PubMed=15932995; DOI=10.1128/aem.71.6.2999-3006.2005;
RA Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.;
RT "Aspergillus parasiticus cyclase catalyzes two dehydration steps in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 71:2999-3006(2005).
RN [19]
RP FUNCTION.
RX PubMed=16332900; DOI=10.1128/aem.71.12.8963-8965.2005;
RA Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
RT "An aflatoxin biosynthesis cluster gene encodes a novel oxidase required
RT for conversion of versicolorin a to sterigmatocystin.";
RL Appl. Environ. Microbiol. 71:8963-8965(2005).
RN [20]
RP FUNCTION.
RX PubMed=15771506; DOI=10.1021/ja0455188;
RA Henry K.M., Townsend C.A.;
RT "Ordering the reductive and cytochrome P450 oxidative steps in
RT demethylsterigmatocystin formation yields general insights into the
RT biosynthesis of aflatoxin and related fungal metabolites.";
RL J. Am. Chem. Soc. 127:3724-3733(2005).
RN [21]
RP FUNCTION.
RX PubMed=16461654; DOI=10.1128/aem.72.2.1096-1101.2006;
RA Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
RT "The aflatoxin biosynthesis cluster gene, aflX, encodes an oxidoreductase
RT involved in conversion of versicolorin A to demethylsterigmatocystin.";
RL Appl. Environ. Microbiol. 72:1096-1101(2006).
RN [22]
RP FUNCTION.
RX PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
RA Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y., Adachi Y.,
RA Nakajima H., Yabe K.;
RT "Involvement of the nadA gene in formation of G-group aflatoxins in
RT Aspergillus parasiticus.";
RL Fungal Genet. Biol. 45:1081-1093(2008).
RN [23]
RP FUNCTION.
RX PubMed=18403714; DOI=10.1126/science.1154711;
RA Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L., Kelleher N.L.,
RA Townsend C.A.;
RT "Deconstruction of iterative multidomain polyketide synthase function.";
RL Science 320:243-246(2008).
RN [24]
RP INDUCTION.
RX PubMed=23113196;
RA Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
RT "Effect of curcumin on Aspergillus parasiticus growth and expression of
RT major genes involved in the early and late stages of aflatoxin
RT biosynthesis.";
RL Iran. J. Public Health 41:72-79(2012).
RN [25]
RP INDUCTION.
RX PubMed=24294264; DOI=10.1590/s1517-83822013000200045;
RA Yahyaraeyat R., Khosravi A.R., Shahbazzadeh D., Khalaj V.;
RT "The potential effects of Zataria multiflora Boiss essential oil on growth,
RT aflatoxin production and transcription of aflatoxin biosynthesis pathway
RT genes of toxigenic Aspergillus parasiticus.";
RL Braz. J. Microbiol. 44:643-649(2013).
CC -!- FUNCTION: Sterigmatocystin 8-O-methyltransferase; part of the gene
CC cluster that mediates the biosynthesis of aflatoxins, a group of
CC polyketide-derived furanocoumarins, and part of the most toxic and
CC carcinogenic compounds among the known mycotoxins (PubMed:15006741).
CC The four major aflatoxins produced by A.parasiticus are aflatoxin B1
CC (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2
CC (AFG2) (PubMed:15006741). The first step of the pathway is the
CC conversion of acetate to norsolorinic acid (NOR) and requires the fatty
CC acid synthase subunits aflA and aflB, as well as the PKS aflC
CC (PubMed:15006741). AflC combines a hexanoyl starter unit and 7 malonyl-
CC CoA extender units to synthesize the precursor NOR (PubMed:18403714).
CC The hexanoyl starter unit is provided to the acyl-carrier protein (ACP)
CC domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699).
CC The second step is the conversion of NOR to averantin (AVN) and
CC requires the norsolorinic acid ketoreductase aflD, which catalyzes the
CC dehydration of norsolorinic acid to form (1'S)-averantin
CC (PubMed:10584035). The norsolorinic acid reductases aflE and aflF may
CC also play a role in the conversion of NOR to AVN (PubMed:15006741). The
CC cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of
CC AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is
CC performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms
CC HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin
CC (AVF) by aflK that plays a dual role in the pathway, as a 5'-
CC oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as
CC well as a versicolorin B synthase in a later step in the pathway
CC (PubMed:15006741, PubMed:11055914, PubMed:15932995). The averufin
CC oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal
CC acetate (VHA) (PubMed:15006741). VHA is then the substrate for the
CC versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL)
CC (PubMed:15006741). Versicolorin B synthase aflK then converts VAL to
CC versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which
CC is required for DNA-binding, thus giving to aflatoxin its activity as a
CC mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the
CC activity of the versicolorin B desaturase aflL leads to versicolorin A
CC (VERA) (PubMed:15006741, PubMed:8368837). A branch point starts from
CC VERB since it can also be converted to dihydrodemethylsterigmatocystin
CC (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins
CC B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next,
CC the versicolorin reductase aflM and the cytochrome P450 monooxygenase
CC aflN are involved in conversion of VERA to demethylsterigmatocystin
CC (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and
CC aflY seem also involved in this step, through probable aflX-mediated
CC epoxide ring-opening step following versicolorin A oxidation and aflY-
CC mediated Baeyer-Villiger oxidation required for the formation of the
CC xanthone ring (PubMed:16332900, PubMed:16461654). The methyltransferase
CC aflO then leads to the modification of DMST to sterigmatocystin (ST),
CC and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both
CC ST and DHST are then substrates of the O-methyltransferase aflP to
CC yield O-methylsterigmatocystin (OMST) and dihydro-O-
CC methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). Finally
CC OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2
CC and G2, via the action of several enzymes including O-
CC methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450
CC monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase
CC nadA which is specifically required for the synthesis of AFG1
CC (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).
CC {ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:10584035,
CC ECO:0000269|PubMed:11055914, ECO:0000269|PubMed:11996570,
CC ECO:0000269|PubMed:1339261, ECO:0000269|PubMed:15528514,
CC ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
CC ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:18403714,
CC ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:8368836,
CC ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
CC ECO:0000305|PubMed:15006741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + sterigmatocystin = 8-O-
CC methylsterigmatocystin + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:15561, ChEBI:CHEBI:15378, ChEBI:CHEBI:18171,
CC ChEBI:CHEBI:18227, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.110; Evidence={ECO:0000269|PubMed:8434913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydrosterigmatocystin + S-adenosyl-L-methionine = 8-O-
CC methyldihydrosterigmatocystin + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:35767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:72677, ChEBI:CHEBI:72678;
CC EC=2.1.1.110; Evidence={ECO:0000269|PubMed:8434913};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for sterigmatocystin {ECO:0000269|PubMed:8434913};
CC KM=9.6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:8434913};
CC pH dependence:
CC Optimum pH is 7-9.4. {ECO:0000269|PubMed:8434913};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:8434913};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000305|PubMed:15006741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14722624}. Vacuole
CC {ECO:0000269|PubMed:14722624}.
CC -!- INDUCTION: Zataria multiflora essential oil reduces gene expression
CC (PubMed:24294264). Expression is repressed by curcumin
CC (PubMed:23113196). {ECO:0000269|PubMed:23113196,
CC ECO:0000269|PubMed:24294264}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60770.1; Type=Erroneous gene model prediction; Note=The predicted gene P875_00052999 has been split into 2 genes: P875_00052999-1 (aflP) and P875_00052999-2 (aflO).; Evidence={ECO:0000305};
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DR EMBL; L22091; AAA32697.1; -; mRNA.
DR EMBL; L25835; AAA32699.1; -; Genomic_DNA.
DR EMBL; AY371490; AAS66017.1; -; Genomic_DNA.
DR EMBL; JZEE01000729; KJK60770.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q12120; -.
DR SMR; Q12120; -.
DR STRING; 1403190.Q12120; -.
DR PRIDE; Q12120; -.
DR EnsemblFungi; KJK60770; KJK60770; P875_00052999.
DR KEGG; ag:AAA32697; -.
DR BioCyc; MetaCyc:MON-14043; -.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0047146; F:sterigmatocystin 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Vacuole; Zymogen.
FT PROPEP 1..41
FT /evidence="ECO:0000269|PubMed:8434913"
FT /id="PRO_0000021898"
FT CHAIN 42..418
FT /note="Sterigmatocystin 8-O-methyltransferase"
FT /id="PRO_0000021899"
FT REGION 206..225
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 170..176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 297..298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT CONFLICT 48
FT /note="S -> D (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="C -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="R -> P (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46397 MW; 2CC5F93245F91262 CRC64;
MALPSKAALV GLANTLSEQV KRYLATAGET KSPEDHKLCI ESERTPSSNE HAQAWEIVRT
CDRIGSLVHG PVPWLLSNAL SHLDSACLAA ATHLNLQDII VDGPSPTSLD TIVAATGVSE
DLLRRILRGC AQRFIFEEVA PDQYAHTDAS KMLRVTGIHA LVGFSCDEVM RSGASFSDFL
QQTKGKPPSW NVPSPFSLAF DPTKGLFDYY STVDEVRGRR FDLGMGGTEA TKPLVEEMFD
FSSLPEGSTV VDVGGGRGHL SRRVSQKHPH LRFIVQDLPA VIHGVEDTDK VTMMEHDIRR
PNPVRGADVY LLRSILHDYP DAACVEILSN IVTAMDPSKS RILLDEMIMP DLLAQDSQRF
MNQIDMTVVL TLNGKERSTK EWNSLITTVD GRLETEKIWW RKGEEGSHWG VQQLRLRK
