PATOX_PHOAA
ID PATOX_PHOAA Reviewed; 2957 AA.
AC C7BKP9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Toxin PAU_02230 {ECO:0000305};
DE AltName: Full=Photorhabdus asymbiotica toxin {ECO:0000303|PubMed:24141704};
DE Short=PaTox {ECO:0000303|PubMed:24141704};
DE Includes:
DE RecName: Full=Protein N-acetylglucosaminyltransferase {ECO:0000305|PubMed:24141704};
DE Short=Protein O-GlcNAc transferase {ECO:0000305|PubMed:24141704};
DE EC=2.4.1.- {ECO:0000269|PubMed:24141704};
DE AltName: Full=PaToxG {ECO:0000303|PubMed:24141704};
DE AltName: Full=Tyrosine glycosyltransferase {ECO:0000303|PubMed:24141704};
DE Includes:
DE RecName: Full=Protein-glutamine amidohydrolase {ECO:0000305|PubMed:24141704};
DE EC=3.5.1.44 {ECO:0000269|PubMed:24141704};
DE AltName: Full=Glutamine deamidase {ECO:0000303|PubMed:24141704};
DE AltName: Full=PaToxD {ECO:0000303|PubMed:24141704};
DE AltName: Full=Protein-glutamine glutaminase {ECO:0000305};
GN OrderedLocusNames=PAU_02230 {ECO:0000312|EMBL:CAQ84322.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000312|Proteomes:UP000002747};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77;
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
RN [2]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2134-ARG-LYS-2135 AND
RP 2139-ARG-LYS-2140.
RC STRAIN=ATCC 43950;
RX PubMed=25782990; DOI=10.1096/fj.14-269381;
RA Jank T., Trillhaase C., Brozda N., Steinemann M., Schwan C., Suess R.,
RA Aktories K.;
RT "Intracellular plasma membrane guidance of Photorhabdus asymbiotica toxin
RT is crucial for cell toxicity.";
RL FASEB J. 29:2789-2802(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2114-2449 IN COMPLEX WITH CALCIUM
RP AND UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, DOMAIN, AND MUTAGENESIS OF TRP-2170; ASP-2260; ARG-2263;
RP ASP-2276; ASP-2278; ASP-2279; 2276-ASP--ASP-2279; ASN-2312 AND CYS-2509.
RC STRAIN=ATCC 43950;
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
CC -!- FUNCTION: Toxin that acts on host cells by modifying Rho proteins by
CC tyrosine GlcNAcylation and heterotrimeric G alpha proteins by
CC deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases of the
CC Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in eukaryotic
CC host cells at the conserved tyrosine residue located in the switch I
CC region (Tyr-32/34), using UDP-N-acetylglucosamine (UDP-GlcNAc) as the
CC sugar donor; other GTPases of the Rho, Ras or Rab families are not
CC substrates. Tyrosine glycosylation inhibits Rho activation and prevents
CC interaction with downstream effectors, resulting in actin disassembly,
CC inhibition of phagocytosis, cell rounding, and toxicity toward insects
CC and mammalian cells. Also catalyzes the deamidation of the catalytic
CC glutamine in heterotrimeric G alpha proteins (Gi, Gq/11), which blocks
CC GTP hydrolysis and arrests the G proteins in a permanent active state
CC leading to activation of Rho GTPases. Thus, PaTox hijacks host GTPase
CC signaling in a bidirectional manner by deamidation-induced activation
CC and glycosylation-induced inactivation of GTPases.
CC {ECO:0000269|PubMed:24141704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+)
CC + O-(N-acetyl-alpha-D-glucosaminyl)-L-tyrosyl-[protein] + UDP;
CC Xref=Rhea:RHEA:51536, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13016,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:134208;
CC Evidence={ECO:0000269|PubMed:24141704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44;
CC Evidence={ECO:0000269|PubMed:24141704};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24141704};
CC Note=A Ca(2+) ion is seen in the structure.
CC {ECO:0000269|PubMed:24141704};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cell membrane
CC {ECO:0000269|PubMed:25782990}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25782990}; Cytoplasmic side
CC {ECO:0000269|PubMed:25782990}. Note=Associates with the negatively
CC charged inner leaflet of the plasma membrane via interaction with
CC phosphatidylserine and phosphatidylinositolphosphates. Plasma membrane
CC localization of PaTox is essential for cytotoxicity. The
CC glycosyltransferase domain alone is sufficient to localize at the
CC plasma membrane. {ECO:0000269|PubMed:25782990}.
CC -!- DOMAIN: In the C-terminal region, contains two catalytic domains: a
CC glycosyltransferase (PaToxG) and a deamidase domain (PaToxD). The N-
CC terminal region contains a receptor-translocation domain necessary for
CC toxin entry into the cytoplasm of host cell.
CC {ECO:0000269|PubMed:24141704}.
CC -!- MISCELLANEOUS: The active GTP-bound conformation of Rho is the
CC preferred substrate for PaTox-induced glycosylation.
CC {ECO:0000269|PubMed:24141704}.
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DR EMBL; FM162591; CAQ84322.1; -; Genomic_DNA.
DR PDB; 4MIX; X-ray; 1.80 A; A/B=2114-2449.
DR PDB; 6HV6; X-ray; 2.00 A; A=1701-2114.
DR PDBsum; 4MIX; -.
DR PDBsum; 6HV6; -.
DR SMR; C7BKP9; -.
DR STRING; 291112.PAU_02230; -.
DR PRIDE; C7BKP9; -.
DR EnsemblBacteria; CAQ84322; CAQ84322; PAU_02230.
DR KEGG; pay:PAU_02230; -.
DR eggNOG; COG3774; Bacteria.
DR eggNOG; COG5539; Bacteria.
DR Proteomes; UP000002747; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0036210; P:protein modification process in another organism; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR028907; Tox-PLDMTX_dom.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR Pfam; PF15645; Tox-PLDMTX; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Glycosyltransferase; Host cell membrane;
KW Host membrane; Hydrolase; Membrane; Metal-binding; Multifunctional enzyme;
KW Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..2957
FT /note="Toxin PAU_02230"
FT /id="PRO_0000434568"
FT REGION 949..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2449
FT /note="Tyrosine glycosyltransferase PaToxG"
FT /evidence="ECO:0000305|PubMed:24141704"
FT REGION 2115..2144
FT /note="Membrane localization domain that interacts with the
FT inner leaflet of the plasma membrane"
FT /evidence="ECO:0000269|PubMed:25782990"
FT REGION 2450..2672
FT /note="SseI-like deamidase PaToxD"
FT /evidence="ECO:0000305|PubMed:24141704"
FT REGION 2667..2705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2276..2279
FT /note="DxDD motif"
FT /evidence="ECO:0000305|PubMed:24141704"
FT COMPBIAS 2671..2702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2509
FT /note="For deamidase activity"
FT /evidence="ECO:0000305|PubMed:24141704"
FT ACT_SITE 2547
FT /note="For deamidase activity"
FT /evidence="ECO:0000305|PubMed:24141704"
FT ACT_SITE 2562
FT /note="For deamidase activity"
FT /evidence="ECO:0000305|PubMed:24141704"
FT BINDING 2169..2171
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:24141704"
FT BINDING 2259..2260
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:24141704"
FT BINDING 2276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:24141704,
FT ECO:0007744|PDB:4MIX"
FT BINDING 2278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|PubMed:24141704,
FT ECO:0007744|PDB:4MIX"
FT BINDING 2312
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2134..2135
FT /note="RK->EE: Abrogates plasma membrane localization,
FT resulting in a cytosolic distribution of this mutant
FT protein. Loss of toxic activity on host cells during the
FT first hours of incubation. No effect on glycosyltransferase
FT activity and interaction with RhoA."
FT /evidence="ECO:0000269|PubMed:25782990"
FT MUTAGEN 2139..2140
FT /note="RK->EE: Abrogates plasma membrane localization,
FT resulting in a cytosolic distribution of this mutant
FT protein. Loss of toxic activity on host cells during the
FT first hours of incubation. No effect on glycosyltransferase
FT activity and interaction with RhoA."
FT /evidence="ECO:0000269|PubMed:25782990"
FT MUTAGEN 2170
FT /note="W->A: 7-fold reduction in glycosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2260
FT /note="D->A: 10000-fold reduction in glycosyltransferase
FT activity. Reduced cell toxicity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2263
FT /note="R->A: 2000-fold reduction in glycosyltransferase
FT activity. Reduced cell toxicity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2276..2278
FT /note="DID->NIN: Loss of glycosyltransferase activity.
FT Reduced toxicity in insect larvae. Loss of the ability to
FT block phagocytosis in mammalian macrophages. Loss of effect
FT on actin skeleton."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2276
FT /note="D->N: 16700-fold reduction in glycosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2278
FT /note="D->N: 333-fold reduction in glycosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2279
FT /note="D->N: 700-fold reduction in glycosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2312
FT /note="N->A: 1.3-fold reduction in glycosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT MUTAGEN 2509
FT /note="C->S: Loss of deamidase activity."
FT /evidence="ECO:0000269|PubMed:24141704"
FT STRAND 1731..1734
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1737..1740
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1746..1759
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1767..1781
FT /evidence="ECO:0007829|PDB:6HV6"
FT TURN 1782..1784
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1786..1791
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1796..1804
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1810..1842
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1847..1851
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1854..1857
FT /evidence="ECO:0007829|PDB:6HV6"
FT TURN 1858..1860
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1865..1877
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1881..1890
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1891..1893
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1897..1899
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1901..1910
FT /evidence="ECO:0007829|PDB:6HV6"
FT TURN 1912..1914
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1915..1918
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1933..1935
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1937..1940
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1942..1952
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1955..1962
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1970..1975
FT /evidence="ECO:0007829|PDB:6HV6"
FT TURN 1976..1978
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 1979..1985
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 1986..2000
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 2004..2006
FT /evidence="ECO:0007829|PDB:6HV6"
FT STRAND 2008..2012
FT /evidence="ECO:0007829|PDB:6HV6"
FT TURN 2015..2019
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 2027..2031
FT /evidence="ECO:0007829|PDB:6HV6"
FT HELIX 2132..2153
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2164..2169
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2172..2174
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2178..2189
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2194..2200
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2208..2218
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2221..2227
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2228..2230
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2234..2239
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2241..2251
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2255..2270
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2272..2274
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2291..2293
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2312..2317
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2322..2337
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2343..2346
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2348..2358
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2360..2362
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2364..2382
FT /evidence="ECO:0007829|PDB:4MIX"
FT HELIX 2399..2412
FT /evidence="ECO:0007829|PDB:4MIX"
FT TURN 2413..2417
FT /evidence="ECO:0007829|PDB:4MIX"
FT STRAND 2418..2420
FT /evidence="ECO:0007829|PDB:4MIX"
SQ SEQUENCE 2957 AA; 334884 MW; AE0C52A8C11E4C6B CRC64;
MKGIEGVIML SHDILPEKLL VSEKKHENVG SYFSDDIGEQ SEQTEVSHFN LSLDDAFDIY
ADISIENQQE LKNKDNNTNI WSSLGRGDDD HNLKKIINDA FKEKLPQLME YRRKGYNVIG
LDKEGIKKLE GMLKAVPPEI QQPTMKNLYS AAQELLNTLK QHPLLPENQD MIQQSNLVIR
NLSDALEAIN AVSKVNQVEW WEEVHKTNKA QSDRLIAATL EELFFKVKDK RLPGSNDDYC
QQEREETERK IKDLLLYDGY QLTAEHFKFG RLRKSLLAES RVTRLKLAEY LEKKSVGILT
AARDAKMYAM KILLAQTRNN GFNAKDLINA GQVNDRLLSF QQYARHIRAV DGEIDGIILS
NPLVVACIKE TNDEPAHIKI ARAILPVSEE LGTVSKVLRE TKEKVQPSKP KEELNHPHQD
WWNRGDELWK YIKKTSWNIK ETSVHVTQMV GYEASKTASR AKHKLKESSY SESINGAVKG
TALLLLDEIQ QAENRIRQIP QFAWDVQEAV EQHSSVIQRT AYPDELPELS ELLNEQLKHE
EARWQAVKKQ SRDKLQELIA PITRLAQEKW AQDLYFQLGE ELRKERQDRW KDIQQFDEIM
AEAVGQFAEM ARELDSEAVR LAEHGHSGGK ELQEKVAKWL RDLSKLKGKV KAGVAKITGT
SLDNFSRSGM LARGMSEWAE DLKQSYLQET LQEGSAVAAE LFERTLMEVV EENRTHFAKE
SDPEAERFLK RLALALKHAA ENTTVYPPTP EEILAGSRSL PEDIRHWAEK KVVSGAISAA
FRGGFKLVTG TFSLPVRVVI RGAKTGGTLY RGVRAINRSV RLGQGPATQV KSKFINQELS
KTAFRLTLSL SPLVAWGMAA SITAGRLYNE KDYPEKIIKN IVIDLPEELL WIGGYAGINA
AIRAHAEKAI QQAIQHALDE QADKLALRIN KEIAGKSADV NVEIIPQETS VSPAETAQST
PEPLSDFAST SQLTMPELID IQDNNSAQQP KVRRKRDVSV ESEISIDNLN IINANTREDK
VNSEIKSELR SELKRFENSD ANSPMSDVER AIFIDLFLYK NKYEVSESQQ DYKNTWLKFR
RELESQENKE IKEYLRFRSI IEAYEIYDKK RLDDDTIPEA GTIIKEVIDF FQKLKKENPI
TFMKLAEAMV KFQYYYEEED ENEDRYFKMA EIYYFLNKTE NEKKSKTFHL DIIDKYPNEN
NRLLDEFFLN KNNNNPDLDE IIYKLQSMQE KYRESYEMLS KVENIHQVLS DDSKNEENIF
LDNRIIAAQV FDGSINISLQ DKKKWLNRYD QIRNEEGSDG WKLMHIESIL INLRRINTAI
NLTAMKSESA LLLIDKLLNF QKKARENILH ISETPHEDFT SYSQFKTRKE LGNDDSKYYA
QFDNYKDNHD AEKEAKEILS QVVARASLSF SELFDKVESI KLFSFVYKNR DGGAPLAAPG
RTVVIKFPGK DTGGLVISNL FLRNHVKRIS TKEMEDLKPL TEGMYTRATQ HRSLGSYYHI
GSQSEHTNAL EILSGMNKEE LKTHLKKQGI WFGEPALFSN EYPKQENTGH LENTTLKNAI
IGVSTIQNNA AANYLRSTMY ESTGWEKLGD RFIPFYEIGR RKHYDREYEI NSEQLTLDII
TSIAIAYPAA RGIVATIRSS AIPSILKSGL RGSALFKSLS LELGKMGFNA SKVFGGAVYE
LIEPYPINSH LNRHNVFNKV KDTAWEFHTD VGLKGGGLKD FIDRFTKEPK EITISGYKFK
RIKYNQENFD TMQRMALDYA YNPDSKGKIA QAQQAYKTGK EDYNAPQYDN FNGLSLDKKI
ERYISPDTDA TTKGVLAGKM NESIKDINAF QTAKDAQSWK KSANKANKVV LTPQNLYLKG
KPSECLPESV LMGWALQSSQ DAKLSKMLMG IYSSNDITSN PLYKSLKELH ANGNASKFNA
SATSISNINV SNLATSETKL FPTEISSVRV DAPKHTMLIS KIKNRENKIK YVFYDPNYGM
AYFDKHSDMA AFFQKKMQQY DFPDDSVSFH PLDYSNVSDI KISGRNLNEI IDGEIPLLYK
QEGVQLEGIT PRDGIYRVPP KNTLGVQETK HYIIVNNDIY QVEWDQTNNT WRVFDPSNTN
RSRPTVPVKQ DTNGEWFKHS ETGLKGGGPI DDIRKYIARK SAIKIFNQSI NYSATKWPPE
PIDKNIHMIW IGTKNISEKN IKLSIDTAKK NPDYNTSIIY DSGISGHEGA KKFMLEKFQD
SNVNIIDFRK KSYFSQLKQE PSFAYYEQVI AENKYAQASD ILRLLVLKYE GGIYKDIDDI
QVKGFGSLTF PKGIGVMREY APEAGKATAF PNTPIAVTKN NPIINKTLDL AVSNYQRGEK
NVLKLAGPDV FTQALYQEIP GLDSKVLNAQ LYQLELAKRQ ALGVPLEKPK NFADEQLTSA
EKEKINRPYQ SIRGLSGYVE NGADHSWAVD TNIPSTSTQT STIVTPLAPK TEMLPPVPSS
STKSSTSAPV LQEKISYNLA TDIDATDYLN QLKQKTNINN KISSPAGQCE SLMKPVSDFM
RENGFTDIRY RGMFIWNNAT EQIPMNHFVV VGKKVGKDYV FDVSAHQFEN KGMPDLNGPL
ILAAEDWAKK YRGATTRKLI YYSDFKNAST ATNTYNALPR ELVLESMEGK TFITSPNWYQ
TFKRTHNIHP EVTVSDPATF SLNYSVNPTA ENLSPPPPPP IPSHGQVPKT VTPPPPPMRS
PLSLSQPLER LPANKTKPIG FNPGENKASF SKLEEAGKHY YKDDKSRQAA PVNTMSDFDN
RYLSHTTEAP APSNVAHLAP GNIYNTKVTA KGAEKPAYDI YISKDGESLI TSSSYKVDDI
TTDSKFGKPL PYSEIMFNSL KKSGVDPKNL KRSVQASIEN KVTQDVISAI GTRIQRGQVI
RVSPTENPDA FYTLLGTDNC KATLHMLNQH AEEFGHKVVT SIEFKGTGYL VMNIGTSTQT
STIVTPPPMP GTSQLVQ
