GLNE_ECOLI
ID GLNE_ECOLI Reviewed; 946 AA.
AC P30870; P78107; Q2M9F2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000305};
DE AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000303|PubMed:4867671};
DE AltName: Full=ATase {ECO:0000303|PubMed:9312015};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000305|PubMed:4920873};
DE EC=2.7.7.89 {ECO:0000269|PubMed:4934180, ECO:0000305|PubMed:14766310, ECO:0000305|PubMed:4893578, ECO:0000305|PubMed:4920873, ECO:0000305|PubMed:9312015};
DE AltName: Full=Adenylyl removase {ECO:0000303|PubMed:20026075};
DE Short=AR {ECO:0000303|PubMed:20026075};
DE Short=AT-N {ECO:0000303|PubMed:9312015};
DE Short=AT-N440 {ECO:0000303|PubMed:14766310};
DE Short=P-I {ECO:0000303|PubMed:4934180};
DE Includes:
DE RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000303|PubMed:4920894};
DE EC=2.7.7.42 {ECO:0000269|PubMed:4920894, ECO:0000305|PubMed:9312015};
DE AltName: Full=Adenylyl transferase {ECO:0000303|PubMed:20026075};
DE Short=AT {ECO:0000303|PubMed:20026075};
DE Short=AT-C {ECO:0000303|PubMed:9312015};
GN Name=glnE {ECO:0000303|PubMed:8412694}; OrderedLocusNames=b3053, JW3025;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / CS520;
RX PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
RA van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
RT "The genes of the glutamine synthetase adenylylation cascade are not
RT regulated by nitrogen in Escherichia coli.";
RL Mol. Microbiol. 9:443-458(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=4867671; DOI=10.1073/pnas.58.4.1703;
RA Kingdon H.S., Shapiro B.M., Stadtman E.R.;
RT "Regulation of glutamine synthetase. 8. ATP: glutamine synthetase
RT adenylyltransferase, an enzyme that catalyzes alterations in the regulatory
RT properties of glutamine synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 58:1703-1710(1967).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RX PubMed=4893578; DOI=10.1021/bi00830a030;
RA Shapiro B.M.;
RT "The glutamine synthetase deadenylylating enzyme system from Escherichia
RT coli. Resolution into two components, specific nucleotide stimulation, and
RT cofactor requirements.";
RL Biochemistry 8:659-670(1969).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4920873; DOI=10.1016/0006-291x(70)90070-7;
RA Anderson W.B., Stadtman E.R.;
RT "Glutamine synthetase deadenylation: a phosphorolytic reaction yielding ADP
RT as nucleotide product.";
RL Biochem. Biophys. Res. Commun. 41:704-709(1970).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=4920894; DOI=10.1111/j.1432-1033.1970.tb00320.x;
RA Ebner E., Wolf D., Gancedo C., Elsaesser S., Holzer H.;
RT "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B.
RT Purification and properties.";
RL Eur. J. Biochem. 14:535-544(1970).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=4934180; DOI=10.1016/0003-9861(71)90229-3;
RA Anderson W.B., Stadtman E.R.;
RT "Purification and functional roles of the P I and P II components of
RT Escherichia coli glutamine synthetase deadenylylation system.";
RL Arch. Biochem. Biophys. 143:428-443(1971).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=33597; DOI=10.1016/0003-9861(78)90398-3;
RA Engleman E.G., Francis S.H.;
RT "Cascade control of E. coli glutamine synthetase. II. Metabolite regulation
RT of the enzymes in the cascade.";
RL Arch. Biochem. Biophys. 191:602-612(1978).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=9312015; DOI=10.1093/emboj/16.18.5562;
RA Jaggi R., van Heeswijk W.C., Westerhoff H.V., Ollis D.L., Vasudevan S.G.;
RT "The two opposing activities of adenylyl transferase reside in distinct
RT homologous domains, with intramolecular signal transduction.";
RL EMBO J. 16:5562-5571(1997).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=14766310; DOI=10.1016/j.pep.2003.11.001;
RA Xu Y., Wen D., Clancy P., Carr P.D., Ollis D.L., Vasudevan S.G.;
RT "Expression, purification, crystallization, and preliminary X-ray analysis
RT of the N-terminal domain of Escherichia coli adenylyl transferase.";
RL Protein Expr. Purif. 34:142-146(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-440.
RX PubMed=15130478; DOI=10.1016/j.str.2004.02.029;
RA Xu Y., Zhang R., Joachimiak A., Carr P.D., Huber T., Vasudevan S.G.,
RA Ollis D.L.;
RT "Structure of the N-terminal domain of Escherichia coli glutamine
RT synthetase adenylyltransferase.";
RL Structure 12:861-869(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 449-946.
RX PubMed=20026075; DOI=10.1016/j.jmb.2009.12.011;
RA Xu Y., Carr P.D., Vasudevan S.G., Ollis D.L.;
RT "Structure of the adenylylation domain of E. coli glutamine synthetase
RT adenylyl transferase: evidence for gene duplication and evolution of a new
RT active site.";
RL J. Mol. Biol. 396:773-784(2010).
CC -!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA, a
CC key enzyme in the process to assimilate ammonia (PubMed:8412694). When
CC cellular nitrogen levels are high, the C-terminal adenylyl transferase
CC inactivates GlnA by covalent transfer of an adenylyl group from ATP to
CC 'Tyr-398' of GlnA, thus reducing its activity (PubMed:4920894,
CC PubMed:9312015). Conversely, when nitrogen levels are low, the N-
CC terminal adenylyl removase (AR) activates GlnA by removing the adenylyl
CC group by phosphorolysis, increasing its activity (PubMed:4893578,
CC PubMed:4920873, PubMed:4934180, PubMed:9312015, PubMed:14766310). The
CC regulatory region of GlnE binds the signal transduction protein PII
CC (GlnB) which indicates the nitrogen status of the cell
CC (PubMed:8412694). {ECO:0000269|PubMed:14766310,
CC ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578,
CC ECO:0000269|PubMed:4920873, ECO:0000269|PubMed:4920894,
CC ECO:0000269|PubMed:4934180, ECO:0000269|PubMed:8412694,
CC ECO:0000269|PubMed:9312015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine +
CC phosphate = [glutamine synthetase]-L-tyrosine + ADP;
CC Xref=Rhea:RHEA:43716, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:456216; EC=2.7.7.89;
CC Evidence={ECO:0000269|PubMed:4934180, ECO:0000305|PubMed:14766310,
CC ECO:0000305|PubMed:4893578, ECO:0000305|PubMed:4920873,
CC ECO:0000305|PubMed:9312015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutamine synthetase]-L-tyrosine + ATP = [glutamine
CC synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate;
CC Xref=Rhea:RHEA:18589, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:83624; EC=2.7.7.42; Evidence={ECO:0000269|PubMed:4920894,
CC ECO:0000305|PubMed:9312015};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578,
CC ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180};
CC Note=Can also use Mn(2+). {ECO:0000269|PubMed:4867671,
CC ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894,
CC ECO:0000269|PubMed:4934180};
CC -!- ACTIVITY REGULATION: The adenylation activity is stimulated by
CC glutamine and PII (GlnB), and inhibited by 2-oxoglutarate
CC (PubMed:4867671, PubMed:4920894, PubMed:33597, PubMed:9312015).
CC Deadenylation activity is stimulated by PII-UMP (GlnB-UMP) and 2-
CC oxoglutarate, and inhibited by glutamine (PubMed:4893578,
CC PubMed:4934180, PubMed:33597, PubMed:9312015, PubMed:14766310).
CC {ECO:0000269|PubMed:14766310, ECO:0000269|PubMed:33597,
CC ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578,
CC ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180,
CC ECO:0000269|PubMed:9312015}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for adenylyl {ECO:0000269|PubMed:4893578};
CC KM=5 uM for [L-glutamate:ammonia ligase (ADP-forming)]
CC {ECO:0000269|PubMed:4920894};
CC KM=150 uM for ATP {ECO:0000269|PubMed:4920894};
CC pH dependence:
CC Optimum pH is between 7.3 and 7.6 (PubMed:4893578, PubMed:4920894).
CC The enzyme is stable between pH 4 and 9 (PubMed:4920894).
CC {ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:4920894}.
CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000305}.
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DR EMBL; Z21844; CAA79892.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76089.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77104.1; -; Genomic_DNA.
DR PIR; C65093; C65093.
DR RefSeq; NP_417525.1; NC_000913.3.
DR RefSeq; WP_001301081.1; NZ_SSZK01000028.1.
DR PDB; 1V4A; X-ray; 2.00 A; A=1-440.
DR PDB; 3K7D; X-ray; 2.40 A; A/B=449-946.
DR PDBsum; 1V4A; -.
DR PDBsum; 3K7D; -.
DR AlphaFoldDB; P30870; -.
DR SMR; P30870; -.
DR BioGRID; 4261515; 4.
DR DIP; DIP-9780N; -.
DR IntAct; P30870; 2.
DR STRING; 511145.b3053; -.
DR jPOST; P30870; -.
DR PaxDb; P30870; -.
DR PRIDE; P30870; -.
DR EnsemblBacteria; AAC76089; AAC76089; b3053.
DR EnsemblBacteria; BAE77104; BAE77104; BAE77104.
DR GeneID; 947552; -.
DR KEGG; ecj:JW3025; -.
DR KEGG; eco:b3053; -.
DR PATRIC; fig|1411691.4.peg.3678; -.
DR EchoBASE; EB1559; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_1_6; -.
DR InParanoid; P30870; -.
DR OMA; EFMVQYA; -.
DR PhylomeDB; P30870; -.
DR BioCyc; EcoCyc:GLNE-MON; -.
DR BioCyc; MetaCyc:GLNE-MON; -.
DR BRENDA; 2.7.7.42; 2026.
DR BRENDA; 2.7.7.89; 2026.
DR EvolutionaryTrace; P30870; -.
DR PRO; PR:P30870; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 2.
DR HAMAP; MF_00802; GlnE; 1.
DR InterPro; IPR023057; GlnE.
DR InterPro; IPR005190; GlnE_rpt_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR PANTHER; PTHR30621; PTHR30621; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; SSF81301; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..946
FT /note="Bifunctional glutamine synthetase
FT adenylyltransferase/adenylyl-removing enzyme"
FT /id="PRO_0000209244"
FT REGION 1..440
FT /note="Adenylyl removase"
FT /evidence="ECO:0000305|PubMed:20026075"
FT REGION 441..448
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:20026075"
FT REGION 449..946
FT /note="Adenylyl transferase"
FT /evidence="ECO:0000305|PubMed:20026075"
FT CONFLICT 524
FT /note="Missing (in Ref. 1; CAA79892)"
FT /evidence="ECO:0000305"
FT CONFLICT 624..625
FT /note="QL -> PV (in Ref. 1; CAA79892)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:1V4A"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 83..106
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 112..141
FT /evidence="ECO:0007829|PDB:1V4A"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1V4A"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1V4A"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1V4A"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:1V4A"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:1V4A"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 364..385
FT /evidence="ECO:0007829|PDB:1V4A"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 414..434
FT /evidence="ECO:0007829|PDB:1V4A"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 474..493
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 498..515
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 521..535
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 549..561
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 563..571
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 573..580
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 582..585
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:3K7D"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 610..633
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 642..669
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 702..708
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 715..720
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 724..740
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 759..761
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 764..767
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 781..788
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 797..811
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 817..834
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:3K7D"
FT TURN 845..847
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 852..866
FT /evidence="ECO:0007829|PDB:3K7D"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 871..874
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 879..888
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 894..916
FT /evidence="ECO:0007829|PDB:3K7D"
FT STRAND 921..924
FT /evidence="ECO:0007829|PDB:3K7D"
FT TURN 925..928
FT /evidence="ECO:0007829|PDB:3K7D"
FT HELIX 929..943
FT /evidence="ECO:0007829|PDB:3K7D"
SQ SEQUENCE 946 AA; 108418 MW; 6FD2D7BDC619DB83 CRC64;
MKPLSSPLQQ YWQTVVERLP EPLAEESLSA QAKSVLTFSD FVQDSVIAHP EWLTELESQP
PQADEWQHYA AWLQEALCNV SDEAGLMREL RLFRRRIMVR IAWAQTLALV TEESILQQLS
YLAETLIVAA RDWLYDACCR EWGTPCNAQG EAQPLLILGM GKLGGGELNF SSDIDLIFAW
PEHGCTQGGR RELDNAQFFT RMGQRLIKVL DQPTQDGFVY RVDMRLRPFG ESGPLVLSFA
ALEDYYQEQG RDWERYAMVK ARIMGDSEGV YANELRAMLR PFVFRRYIDF SVIQSLRNMK
GMIAREVRRR GLTDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIAELH
LLSENDAEQL RVAYLFLRRL ENLLQSINDE QTQTLPSDEL NRARLAWAMD FADWPQLTGA
LTAHMTNVRR VFNELIGDDE SETQEESLSE QWRELWQDAL QEDDTTPVLA HLSEDDRKQV
LTLIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCARED AAVTLSRITA LLVGIVTRTT
YLELLSEFPA ALKHLISLCA ASPMIASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
YLLRVPEDDE EQQLEALRQF KQAQLLRIAA ADIAGTLPVM KVSDHLTWLA EAMIDAVVQQ
AWVQMVARYG KPNHLNEREG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDAMTDGER
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
TWEHQALVRA RVVYGDPQLT AHFDAVRREI MTLPREGKTL QTEVREMREK MRAHLGNKHR
DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMEEQEAMAL
TRAYTTLRDE LHHLALQELP GHVSEDCFTA ERELVRASWQ KWLVEE
