MARTX_VIBVL
ID MARTX_VIBVL Reviewed; 5206 AA.
AC A0A2S3R7M0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Multifunctional-autoprocessing repeats-in-toxin {ECO:0000250|UniProtKB:Q9KS12};
DE Short=MARTX {ECO:0000250|UniProtKB:Q9KS12};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9KS12};
DE Contains:
DE RecName: Full=Actin cross-linking toxin F1 {ECO:0000250|UniProtKB:Q9KS12};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q9KS12};
DE Contains:
DE RecName: Full=N-epsilon-fatty acyltransferase F2;
DE EC=2.3.1.- {ECO:0000269|PubMed:29074776};
DE AltName: Full=Rho inactivation domain-containing toxin F2 {ECO:0000250|UniProtKB:Q9KS12};
DE Short=RIDvc {ECO:0000303|PubMed:29074776};
DE Contains:
DE RecName: Full=ABH effector region toxin F5 {ECO:0000250|UniProtKB:Q9KS12};
DE Contains:
DE RecName: Full=Cysteine protease domain-containing toxin F3 {ECO:0000250|UniProtKB:Q9KS12};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9KS12};
DE Flags: Precursor;
GN ORFNames=CRN52_02910 {ECO:0000312|EMBL:POB49698.1};
OS Vibrio vulnificus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT4608;
RX PubMed=29358930; DOI=10.3389/fmicb.2017.02613;
RA Roig F.J., Gonzalez-Candelas F., Sanjuan E., Fouz B., Feil E.J.,
RA Llorens C., Baker-Austin C., Oliver J.D., Danin-Poleg Y., Gibas C.J.,
RA Kashi Y., Gulig P.A., Morrison S.S., Amaro C.;
RT "Phylogeny of Vibrio vulnificus from the Analysis of the Core-Genome:
RT Implications for Intra-Species Taxonomy.";
RL Front. Microbiol. 8:2613-2613(2018).
RN [2] {ECO:0007744|PDB:5XN7}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2286-2901 (N-EPSILON-FATTY
RP ACYLTRANSFERASE F2).
RC STRAIN=ATCC 27562 / DSM 10143 / JCM 3725 / BCRC 12905 / KCTC 2959 / LMG
RC 13545 / NBRC 15645 / NCIMB 2046 / WDCM 00139;
RX PubMed=29074776; DOI=10.1126/science.aam8659;
RA Zhou Y., Huang C., Yin L., Wan M., Wang X., Li L., Liu Y., Wang Z., Fu P.,
RA Zhang N., Chen S., Liu X., Shao F., Zhu Y.;
RT "Nepsilon-fatty acylation of Rho GTPases by a MARTX toxin effector.";
RL Science 358:528-531(2017).
CC -!- FUNCTION: [Multifunctional-autoprocessing repeats-in-toxin]: Precursor
CC of a multifunctional toxin that causes destruction of the actin
CC cytoskeleton by covalent cross-linking of actin and inactivation of Rho
CC GTPases when translocated into the host cytoplasm. Upon translocation
CC into the host cell, undergoes autoprocessing in cis mediated by the
CC peptidase C80 domain (also named CPD domain): the protease activity is
CC activated upon binding inositol hexakisphosphate (InsP6) present at the
CC host cell membrane and delivers the Cysteine protease domain-containing
CC toxin F3 chain to the host cytosol. The Cysteine protease domain-
CC containing toxin F3 chain will then further cleave and release effector
CC toxin chains that cause disassembly of the actin cytoskeleton and
CC enhance V.vulnificus colonization of the small intestine, possibly by
CC facilitating evasion of phagocytic cells.
CC {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- FUNCTION: [Cysteine protease domain-containing toxin F3]: Following
CC autocatalytic cleavage in cis, this chain mediates processing in trans
CC to release other individual toxin chains to the host cytosol. Released
CC effector toxin chains cause disassembly of the actin cytoskeleton and
CC enhance V.vulnificus colonization of the small intestine, possibly by
CC facilitating evasion of phagocytic cells.
CC {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- FUNCTION: [Actin cross-linking toxin F1]: Actin-directed toxin that
CC catalyzes the covalent cross-linking of host cytoplasmic monomeric
CC actin. Mediates the cross-link between 'Lys-50' of one monomer and
CC 'Glu-270' of another actin monomer, resulting in formation of highly
CC toxic actin oligomers that cause cell rounding. The toxin can be highly
CC efficient at very low concentrations by acting on formin homology
CC family proteins: toxic actin oligomers bind with high affinity to
CC formins and adversely affect both nucleation and elongation abilities
CC of formins, causing their potent inhibition in both profilin-dependent
CC and independent manners. Acts as an acid--amino-acid ligase that
CC transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin
CC residue, resulting in the formation of an activated acyl phosphate
CC intermediate. This intermediate is further hydrolyzed and the energy of
CC hydrolysis is utilized for the formation of the amide bond between
CC actin subunits. {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- FUNCTION: [N-epsilon-fatty acyltransferase F2]: N-epsilon-fatty
CC acyltransferase that mediates lysine-palmitoylation of host Rho GTPase
CC proteins, with a strong preference for host Rac1. After delivery to the
CC host cytosol, localizes to the host cell membrane where it
CC palmitoylates host Rho GTPase proteins, resulting in loss of all active
CC GTP-bound Rho and subsequent actin depolymerization. Prenylation of
CC host Rac1 at the C-terminus is required for lysine-palmitoylation.
CC {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- FUNCTION: [ABH effector region toxin F5]: Indirectly activates the
CC small GTPase CDC42. {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]:
CC Reaction=hexadecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-
CC cysteinyl-[protein] = CoA + H(+) + N(6)-hexadecanoyl-L-lysyl-/S-
CC (2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:59768, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17953,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:86021, ChEBI:CHEBI:138936;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59769;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC -!- CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]:
CC Reaction=dodecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-
CC cysteinyl-[protein] = CoA + H(+) + N(6)-dodecanoyl-L-lysyl-/S-
CC (2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:59796, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17954,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:86021, ChEBI:CHEBI:143221;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59797;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC -!- CATALYTIC ACTIVITY: [N-epsilon-fatty acyltransferase F2]:
CC Reaction=decanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-
CC cysteinyl-[protein] = CoA + H(+) + N(6)-decanoyl-L-lysyl-/S-
CC (2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:59800, Rhea:RHEA-COMP:17936, Rhea:RHEA-COMP:17955,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:86021, ChEBI:CHEBI:143222;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59801;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9KS12};
CC Note=Binds 2 Mg(2+) ions per subunit. Mg(2+) is required for actin
CC cross-linking activity. Can also use Mn(2+) ions instead of Mg(2+).
CC {ECO:0000250|UniProtKB:A0A0H3AIG7};
CC -!- SUBCELLULAR LOCATION: [Multifunctional-autoprocessing repeats-in-
CC toxin]: Secreted {ECO:0000250|UniProtKB:Q9KS12}. Host cytoplasm, host
CC cytosol {ECO:0000250|UniProtKB:Q9KS12}. Note=Secreted via the type I
CC secretion system. {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- SUBCELLULAR LOCATION: [N-epsilon-fatty acyltransferase F2]: Host cell
CC membrane {ECO:0000250|UniProtKB:Q9KS12}. Note=Targeted to the host cell
CC membrane via the membrane localization region (MLD).
CC {ECO:0000250|UniProtKB:Q9KS12}.
CC -!- SUBCELLULAR LOCATION: [Actin cross-linking toxin F1]: Host cytoplasm,
CC host cytosol {ECO:0000250|UniProtKB:Q9KS12}.
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DR EMBL; PDGH01000027; POB49698.1; -; Genomic_DNA.
DR PDB; 2N9W; NMR; -; A=3591-3669.
DR PDB; 5XN7; X-ray; 2.70 A; A/B=380-995.
DR PDBsum; 2N9W; -.
DR PDBsum; 5XN7; -.
DR SMR; A0A2S3R7M0; -.
DR EnsemblBacteria; POB49698; POB49698; CRN52_02910.
DR Proteomes; UP000237466; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; 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:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11050; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR020974; CPD_dom.
DR InterPro; IPR038383; CPD_dom_sf.
DR InterPro; IPR020972; Dermonecrotic/RTX_toxin_MLD.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR011509; RtxA_toxin.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF12146; Hydrolase_4; 1.
DR Pfam; PF11647; MLD; 2.
DR Pfam; PF11713; Peptidase_C80; 1.
DR Pfam; PF07634; RtxA; 39.
DR SUPFAM; SSF51120; SSF51120; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS51771; CGT_MARTX_CPD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Autocatalytic cleavage; Host cell membrane;
KW Host cytoplasm; Host membrane; Hydrolase; Ligase; Lipid-binding; Magnesium;
KW Membrane; Metal-binding; Multifunctional enzyme; Protease; Repeat;
KW Secreted; Signal; Thiol protease; Toxin; Transferase; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000305"
FT CHAIN 20..5206
FT /note="Multifunctional-autoprocessing repeats-in-toxin"
FT /id="PRO_0000455658"
FT CHAIN 20..1958
FT /note="Actin cross-linking toxin F1"
FT /id="PRO_0000455659"
FT CHAIN 2296..2901
FT /note="N-epsilon-fatty acyltransferase F2"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT /id="PRO_0000455660"
FT CHAIN 2902..3400
FT /note="ABH effector region toxin F5"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT /id="PRO_0000455661"
FT CHAIN 4091..5206
FT /note="Cysteine protease domain-containing toxin F3"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT /id="PRO_0000455662"
FT REPEAT 101..118
FT /note="RtxA 1"
FT /evidence="ECO:0000255"
FT REPEAT 121..138
FT /note="RtxA 2"
FT /evidence="ECO:0000255"
FT REPEAT 141..157
FT /note="RtxA 3"
FT /evidence="ECO:0000255"
FT REPEAT 161..184
FT /note="RtxA 4"
FT /evidence="ECO:0000255"
FT REPEAT 187..204
FT /note="RtxA 5"
FT /evidence="ECO:0000255"
FT REPEAT 207..224
FT /note="RtxA 6"
FT /evidence="ECO:0000255"
FT REPEAT 255..272
FT /note="RtxA 7"
FT /evidence="ECO:0000255"
FT REPEAT 275..291
FT /note="RtxA 8"
FT /evidence="ECO:0000255"
FT REPEAT 584..601
FT /note="RtxA 9"
FT /evidence="ECO:0000255"
FT REPEAT 604..620
FT /note="RtxA 10"
FT /evidence="ECO:0000255"
FT REPEAT 624..641
FT /note="RtxA 11"
FT /evidence="ECO:0000255"
FT REPEAT 644..658
FT /note="RtxA 12"
FT /evidence="ECO:0000255"
FT REPEAT 741..753
FT /note="RtxA 13"
FT /evidence="ECO:0000255"
FT REPEAT 759..771
FT /note="RtxA 14"
FT /evidence="ECO:0000255"
FT REPEAT 782..798
FT /note="RtxA 15"
FT /evidence="ECO:0000255"
FT REPEAT 801..816
FT /note="RtxA 16"
FT /evidence="ECO:0000255"
FT REPEAT 820..835
FT /note="RtxA 17"
FT /evidence="ECO:0000255"
FT REPEAT 841..855
FT /note="RtxA 18"
FT /evidence="ECO:0000255"
FT REPEAT 858..875
FT /note="RtxA 19"
FT /evidence="ECO:0000255"
FT REPEAT 877..891
FT /note="RtxA 20"
FT /evidence="ECO:0000255"
FT REPEAT 896..910
FT /note="RtxA 21"
FT /evidence="ECO:0000255"
FT REPEAT 915..932
FT /note="RtxA 22"
FT /evidence="ECO:0000255"
FT REPEAT 934..950
FT /note="RtxA 23"
FT /evidence="ECO:0000255"
FT REPEAT 972..984
FT /note="RtxA 24"
FT /evidence="ECO:0000255"
FT REPEAT 991..1006
FT /note="RtxA 25"
FT /evidence="ECO:0000255"
FT REPEAT 1031..1043
FT /note="RtxA 26"
FT /evidence="ECO:0000255"
FT REPEAT 1067..1079
FT /note="RtxA 27"
FT /evidence="ECO:0000255"
FT REPEAT 1087..1102
FT /note="RtxA 28"
FT /evidence="ECO:0000255"
FT REPEAT 1110..1122
FT /note="RtxA 29"
FT /evidence="ECO:0000255"
FT REPEAT 1125..1142
FT /note="RtxA 30"
FT /evidence="ECO:0000255"
FT REPEAT 1145..1159
FT /note="RtxA 31"
FT /evidence="ECO:0000255"
FT REPEAT 1163..1179
FT /note="RtxA 32"
FT /evidence="ECO:0000255"
FT REPEAT 1184..1199
FT /note="RtxA 33"
FT /evidence="ECO:0000255"
FT REPEAT 1201..1217
FT /note="RtxA 34"
FT /evidence="ECO:0000255"
FT REPEAT 1220..1236
FT /note="RtxA 35"
FT /evidence="ECO:0000255"
FT REPEAT 1242..1256
FT /note="RtxA 36"
FT /evidence="ECO:0000255"
FT REPEAT 1258..1275
FT /note="RtxA 37"
FT /evidence="ECO:0000255"
FT REPEAT 1296..1313
FT /note="RtxA 38"
FT /evidence="ECO:0000255"
FT REPEAT 1315..1332
FT /note="RtxA 39"
FT /evidence="ECO:0000255"
FT DOMAIN 4111..4295
FT /note="Peptidase C80"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01107"
FT REGION 1606..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2377..2461
FT /note="Membrane localization region (MLD)"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT REGION 2537..2901
FT /note="Rho inactivation domain (RID)"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT REGION 2998..3113
FT /note="ABH effector region"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT REGION 4333..4362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4738..4779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4749..4779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4181
FT /note="For cysteine protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01107"
FT ACT_SITE 4230
FT /note="Nucleophile; for cysteine protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01107"
FT BINDING 4117..4119
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4144..4145
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4175
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4226
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4259..4261
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4272..4273
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4285
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
FT BINDING 4290
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:Q9KS12"
SQ SEQUENCE 5206 AA; 556341 MW; 85BB805918FD1C5A CRC64;
MGKPFWRSVE YFFTGNYSAD DGNNSIVAIG FGGEIHAYGG DDHVTVGSIG ATVYTGSGND
TVVGGSAYLR VEDTTGHLSV KGAAGYADIN KSGDGNVSFA GAAGGVSIDH LGNNGDVSYG
GAAAYNGITR KGLSGNVTFK GAGGYNALWH ETNQGNLSFA GAGAGNKLDR TWFNRYQGSR
GDVTFDGAGA ANSISSRVET GNITFRGAGA DNHLVRKGKV GDITLQGAGA SNRIERTRQA
EDVYAQTRGN IRFEGVGGYN SLYSDVAHGD IHFSGGGAYN TITRKGSGSS FDAQGMEYAK
AEDIVLTAAQ MHGLSIDNGN KFHAVTAVKS EREPNTYLFA IADGTYTKIN KVRLYNDPET
GKLKYYSEAW FKRGNHLAEL ARSDVSSAGG FEVNPINGGY TLANIAVEHQ QSVTVHAVEK
NLTEYEWVTY ANGTLIDAKD VALSEAKMGG HAISTDGTTV DVQAVKSNRK PNTYVYAKVL
GPYTKIVVVE LANDPKTGAL KYQARSWYKE GDHTANLANE DISSANGYHS MGKGGYSLSD
LHYSVNAVRS TSETVADIDE YTDQTLFKPA TDSGESSGDV RFNGAGGGNV IKSNVTRGNV
YFNGGGIANV ILHSSQFGNT EFNGGGAANV IVKSGEEGDL TFRGAGLANV LVHQSKQGKM
DVYAGGAVNV LVRIGDGQYL AHLLAYGNIS VHKGNGNSRV VMLGGYNTHT QIGSGNGLWL
AAGGFNVMTQ VGKGDVASVL AGGANVLTKV GDGDLTAGML GGANVITHIS GDNETSNTTA
VALGGANILT KKGKGNTLAV MGGGANVLTH VGDGTTTGVM VGGANILTKV GNGDTTGIML
GVGNVLTHVG DGQTLGVMGA AGNIFTKVGD GTSIAVMIGA GNIFTHVGEG NAWALMGGLG
NVFTKVGNGD ALALMVAEAN VFTHIGDGMS VALMLAKGNV ATKVGNGTTL AAMVGNANIF
THVGSGSTFA AMIGQANIMT KVGNDLTAAL MVGKANIYTH VGDGTSLGIF AGEVNVMTKI
GNGTTLAAMF GKANIMTHVG DGLTGVLALG EANIVTKVGD DFMGVVAAAK ANVVTHVGDA
TTAAVLAGKG NILTKVGEGT TVGLLISDIG NVMTHVGDGT TIGIAKGKAN IITKVGDGLG
VNVAWGQANV FTQVGDGDRY NFAKGEANII TKVGDGKEVS VVQGKANIIT HVGNGDDYTG
AWGKANVITK VGNGRNVVLA KGEANIVTQV GDGDSFNALW SKGNIVTKVG DGMQVTAAKG
KANITTTVGD GLSVTAAYGD ANINTKVGDG VSVNVAWGKY NINTKVGDGL NVAVMKGKAN
ANIHVGDGLN INASYAQNNV AIKVGNGDFY SLAVASSNTS SNKLSALFDN IKQTLLGVGG
SQAINYLVQG DEASSSGTQK GRGAIATPEI TKLDGFQMEA IEEVGSDLGD SLTGSVTKVD
TPDLNKMQNA LDVDGSSDQT QAPNLIVNGD FEQGDRGWKS THGVEASYSG NVYGVNGEGH
GARVTELDTY TNTSLYQDLT DLTEGEVIAV SFDFAKRAGL SNNEGIEVLW NGEVVFSSSG
DASAWQQKTL KLTAHAGSNR IEFKGTGHND GLGYILDNVV AKSESSQQAN AVSEHATQNQ
ASQNALSDKE RAEADRQRLE QEKQKQLDAV AGSQSQLEST DQQALGNNGQ AQRDAVKEES
EAVTAELTKL AQGLDVLDGQ ATHTGESGDQ WRNDFAGGLL DGVQSQLDDA KQLANDKIAA
AKQTQSDNNS KVKESVAKSE AGVAQGEQNR AGAEQDIAEA KADAETRKAD AVAKSNDAKQ
AESDAHSAAN DAQSRGDRDA MNAENKANQA QNDAKGTKQN EGDRPDREGV AGSGLSGNAH
SVEGAGETGS HITTDSQTNA DGRFSEGLSE QEQEALEGAT NAVNRLQINA GIRGKNSGST
ITSMFTETNS DSIVVPTTAS QDVVRKEIRI SGVNLEGLGE ASHDSAESLV AARAEKVANL
YRWLDTDNDV ATDKYVPVPG FERVDVDVSD EVKQRMIQSM SGYIEHTDNQ VPKDQAEALA
TLFVESTLDY DWDKRVEFLT KLESYGYSFE APHAEKSIVS FWSGKNFKQY RDILDNAQTD
GKKVVYDIDV KGNAFAIDLN KHLMRWGGLF LDPDNAEQNQ LKSSIDAATF SNTGFWSSVY
ATGAQNDVYV IAEGGVRLGN YFWNVELPAL RQLQREGLVG EIRLLDKPVS EYKDLPADQI
GRRLTDAGVA VKVRFDALSH ERQAELLADN PDGYKADTLV ELDVKLSAID SMLRESLPFY
SLRTERNLLV QEGEEGFEVR SWPGIDGKSK TILLDNPEDA AQQKSIERFI LANFDNFEQM
PDELFLVDNK VLSHHDGRTR IIAQKEDGAW TYNTNVELMS VTELLDAAHV NGKVRGDSYQ
QVIDALTEYH ASTVEHADYE LESVEKLLNL RKQIEGYVLG HPDSGRVEAM NSLLNQVNSR
LEEVSVLAVS EQSIKAHDSF SRLYDQLDNA NLKESKHLYL DGNGDFVTKG KGNLATIDQL
GGSDAVLEKV KAAVTHEYGQ VVADTIFARL SANDLAKDGK GIDIAGLNKV HQAIEQHMSP
VSATMYIWKP SDHSTLGHAA LQIGQGRTQL EGQAAADFNK QNYVSWWPLG SKSSNIRNIF
NVATEDQPDL KLRWSDFSQP AHQNDTLEHD MASEENDGFG LKDGETKLKR FIEKLNAAKG
IDASYKDASE GYASVLLGNP DMLASTGIPA HVFQPFVDQW NDTSYDMMDV ANRFAEELQK
QAQASGDPAL VEKRIDNVVR LFAERALEEI EAFKASQADE GRVFRINLEG LDVAAMQAEW
NRLSNDPDAR YQLLTKNCSS TVAKVLKAGG ADKLIGHTWR PKFGVWTPTE LFNFGQALQE
AQLEIAAKKQ SHQVTDVLDA LSGNEKHKEN VTIENDGTPP RDKESLSPLT RFLNNELYGE
KDARRKIGEI TQTLLDHAVE NGESQKVTLK GEAGRLTGYY HQGAASSEGE TSATSGKVVL
FLHGSGSSAE EQASAIRNHY QKQGIDMLAV NLRGYGESDG GPSEKGLYQD ARTMFNYLVN
DKGIDPSNII IHGYSMGGPI AADLARYAAQ NGQAVSGLLL DRPMPSMTKA ITAHEMANPA
GIVGAIAKAV NGQFSVEKNL KGLPKETPIL LLTDNEGLGE EGEKLRAKLA IAGYNVTGEQ
TFYGHEASNR LMGQYADQIV SGLFNAEQAA VEAGEVLKGL EKDFKRYGDA LKPDTSVPGK
SKDIRTTKDF LNGYKNDHAK EIVDGFRSDM SIKQLVDLFV KGNWSAEQKG ALAWEIESRA
LKVTFQNKSE KYNRLFREIA SAGVVDAKAT EQLAPQLMLL NLSNDGFGGR CDPLSKLVLV
AKQLENDGQV GVARQLLEKM YSAAAVLSNP TLYSDSEKAN ASKLLSSLAA IHAKNPMHDT
SMKVWQEKLE GKQALTVNGV VEKITDASAN GKPVLLELDA PGHAMAAWAK DSGDDRVYGF
YDPNAGIVEF SSAEKFGDYL TRFFGKSDLD MAQSYKLGKN DAGEAIFNRV VVMDGNTLAS
YKPTFGDKTT MQGILDLPVF DATPIKKPTG GVASDLEALG DKTKVVVDLA QIFTVQELKE
RAKVFAKPIG ASYQGILDQL DLVHQAKGRD QIAASFELNK KINDYIAEHP TSGRNQALTQ
LKEQVTSALF IGKMQVAQAG IDAIAQTRPE LAARIFMVAI EEANGKHVGL TDMMVRWANE
DPYLAPKHGY KGETPSDLGF DAKYHVDLGE HYADFKQWLE TSQSNGLLSK ATLDESTKTV
HLGYSYQELQ DLTGAESVQM AFYFLKEAAK KADPISGDSA EMILLKKFAD QSYLSQLDSD
RMDQIEGIYR SSHETDIDAW DRRYSGTGYD ELTNKLASAT GVDEQLAVLL DDRKGLLIGE
VHGSDVNGLR FVNEQMDALK KQGVTVIGLE HLRSDLAQPL IDRYLATGVM SSELSAMLKT
KHLDVTLFEN ARANGIRIVA LDANSSARPN VQGTEHGLMY RAGAANNIAV EVLQNLPDGE
KFVAIYGKAH LQSHKGIEGF VPGITHRLDL PALKVSDSNQ FTVEQDDVSL RVVYDDVANK
PKITFKDSLS GANTALHNQN VNDWERVVVT PTADGGESRF DGQIIVQMEN DDVVAKAAAN
LAGKHPESSV VVQIDSDGNY RVVYGDPSKL DGKLRWQLVG HGRDDSESNN TRLSGYSADE
LAVKLAKFQQ SFNQAENINN KPDHISIVGC SLVSDDKQKG FGHQFINAMD ANGLRVDVSV
RSSELAVDEA GRKHTKDANG DWVQKAENNK VSLSWDEQGE VVAKDERIRN GIAEGDIDLS
RIGVSDVDEP ARGAIGDNND VFDAPEKRKA ETETSSSSAN NKLSYSGNIQ VNVGDGEFTA
VNWGTSNVGI KVGTGGFKSL AFGDNNVMVH IGNGESKHSF DIGGYQALEG AQMFIGNRNV
SFNLGRSNDL IVMMDKSIPT PPLVNPFDGA ARISGVLQSI ATSGEGQDWL AAQEQQWTLS
GAKKFVKDMS GLDQSSSVDY TSLVELDSQN ERSSRGLKHD AEAALNKQYN QWLSGNSDSD
TSKLSRADKL RQANEKLAFN FAVGGQGADI QVTTGNWNFM FGDNIQSILD TNLGSLFGLM
TQQFSATGQA KTTFTYTPED LPRQLKNKLL GQLAGVGAET TLADIFGVDY TASGQIVSRN
GEAVDGVAIL KEMLEVIGEF SGDQLQAFVD PAKLLDSLKS GINMGADGIK SFAETHGLKE
KAPEEEEDNS SVSVNGASVN SAQGATVADG STETAETPDR AFGFNSLNLP NLFATIFSQD
KQKEMKSLVE NLKENLTADL LNMKEKTFDF LRNSGHLQGD GDINISLGNY NFNWGGDGKD
LGAYLGDNNN FWGGRGDDVF YATGTSNIFT GGEGNDMGVL MGRENMMFGG DGNDTAVVAG
RINHVFLGAG DDQSFVFGEG GEIDTGSGRD YVVTSGNFNR VDTGDDQDYS VTIGNNNQVE
LGAGNDFANV FGNYNRINAS AGNDVVKLMG YHAVLNGGEG EDHLIAAAIS KFSQFNGGEG
RDLMVLGGYQ NTFKGGTDVD SFVVSGDVID NLVEDIRSED NIVFNGIDWQ KLWFERSGYD
LKLSILRDPA SDSDQAKFEH IGSVTFSDYF NGNRAQVIIA MGEKDATGER EYTTLSESAI
DALVQAMSGF DPQAGDNGFM DNLDSKSRVA ITTAWADVVH KKGITV
