GLFT2_MYCTU
ID GLFT2_MYCTU Reviewed; 637 AA.
AC O53585; L0TFB5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Galactofuranosyltransferase GlfT2 {ECO:0000305};
DE Short=GalTr 2 {ECO:0000305};
DE EC=2.4.1.288 {ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:16704275};
DE AltName: Full=Arabinogalactan galactosyltransferase 2 {ECO:0000305};
DE AltName: Full=Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase;
DE AltName: Full=Polymerizing galactofuranosyltransferase GlfT2 {ECO:0000305};
GN Name=glfT2 {ECO:0000303|PubMed:18423586, ECO:0000312|EMBL:CCP46637.1};
GN Synonyms=glfT {ECO:0000303|PubMed:11304545, ECO:0000303|PubMed:16704275};
GN OrderedLocusNames=Rv3808c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE.
RX PubMed=10934214; DOI=10.1074/jbc.m006875200;
RA Mikusova K., Yagi T., Stern R., McNeil M.R., Besra G.S., Crick D.C.,
RA Brennan P.J.;
RT "Biosynthesis of the galactan component of the mycobacterial cell wall.";
RL J. Biol. Chem. 275:33890-33897(2000).
RN [3]
RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, SUBCELLULAR LOCATION, AND
RP PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11304545; DOI=10.1074/jbc.m102022200;
RA Kremer L., Dover L.G., Morehouse C., Hitchin P., Everett M., Morris H.R.,
RA Dell A., Brennan P.J., McNeil M.R., Flaherty C., Duncan K., Besra G.S.;
RT "Galactan biosynthesis in Mycobacterium tuberculosis. Identification of a
RT bifunctional UDP-galactofuranosyltransferase.";
RL J. Biol. Chem. 276:26430-26440(2001).
RN [4]
RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=16704275; DOI=10.1021/ja058254d;
RA Rose N.L., Completo G.C., Lin S.J., McNeil M., Palcic M.M., Lowary T.L.;
RT "Expression, purification, and characterization of a
RT galactofuranosyltransferase involved in Mycobacterium tuberculosis
RT arabinogalactan biosynthesis.";
RL J. Am. Chem. Soc. 128:6721-6729(2006).
RN [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18423586; DOI=10.1016/j.carres.2008.03.023;
RA Rose N.L., Zheng R.B., Pearcey J., Zhou R., Completo G.C., Lowary T.L.;
RT "Development of a coupled spectrophotometric assay for GlfT2, a
RT bifunctional mycobacterial galactofuranosyltransferase.";
RL Carbohydr. Res. 343:2130-2139(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18055597; DOI=10.1128/jb.01326-07;
RA Belanova M., Dianiskova P., Brennan P.J., Completo G.C., Rose N.L.,
RA Lowary T.L., Mikusova K.;
RT "Galactosyl transferases in mycobacterial cell wall synthesis.";
RL J. Bacteriol. 190:1141-1145(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND POLYMER LENGTH CONTROL.
RC STRAIN=H37Rv;
RX PubMed=19571009; DOI=10.1073/pnas.0901407106;
RA May J.F., Splain R.A., Brotschi C., Kiessling L.L.;
RT "A tethering mechanism for length control in a processive carbohydrate
RT polymerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11851-11856(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEXES WITH UDP AND MANGANESE
RP IONS, MUTAGENESIS OF GLU-300; ASP-371; ASP-372; TRP-399 AND HIS-413,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX PubMed=22707726; DOI=10.1074/jbc.m112.347484;
RA Wheatley R.W., Zheng R.B., Richards M.R., Lowary T.L., Ng K.K.;
RT "Tetrameric structure of the GlfT2 galactofuranosyltransferase reveals a
RT scaffold for the assembly of mycobacterial arabinogalactan.";
RL J. Biol. Chem. 287:28132-28143(2012).
CC -!- FUNCTION: Involved in the galactan polymerization of the
CC arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan
CC (mAGP) complex, an essential component of the mycobacteria cell wall.
CC Thus, successively transfers approximately 28 galactofuranosyl (Galf)
CC residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-
CC galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-
CC GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and
CC 1->6 links, forming a galactan domain with approximately 30
CC galactofuranosyl residues. {ECO:0000269|PubMed:18055597,
CC ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:10934214,
CC ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275,
CC ECO:0000305|PubMed:18423586}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-
CC alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D-
CC galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-
CC galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-
CC rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC trans,octa-cis-decaprenol + 28 H(+) + 28 UDP; Xref=Rhea:RHEA:34391,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915,
CC ChEBI:CHEBI:67210, ChEBI:CHEBI:67212; EC=2.4.1.288;
CC Evidence={ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009,
CC ECO:0000305|PubMed:16704275};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:22707726};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:22707726};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for UDP-Galf {ECO:0000269|PubMed:18423586,
CC ECO:0000269|PubMed:22707726};
CC KM=0.60 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-
CC octyl {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726};
CC KM=1.7 mM for beta-D-Galf-(1->5)-beta-D-Galf-octyl
CC {ECO:0000269|PubMed:16704275};
CC KM=0.635 mM for beta-D-Galf-(1->6)-beta-D-Galf-octyl
CC {ECO:0000269|PubMed:16704275};
CC KM=0.208 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf-
CC octyl {ECO:0000269|PubMed:16704275};
CC KM=0.204 mM for beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf-
CC octyl {ECO:0000269|PubMed:16704275};
CC Vmax=4.4 umol/min/mg enzyme for galtactose transfer on beta-D-Galf-
CC (1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl
CC {ECO:0000269|PubMed:16704275, ECO:0000269|PubMed:18423586};
CC Note=kcat is 430 min(-1) for galtactose transfer on beta-D-Galf-
CC (1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl.
CC {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22707726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11304545}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000305|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46637.1; -; Genomic_DNA.
DR PIR; D70888; D70888.
DR RefSeq; NP_218325.1; NC_000962.3.
DR RefSeq; WP_003900761.1; NZ_NVQJ01000022.1.
DR PDB; 4FIX; X-ray; 2.45 A; A/B=1-637.
DR PDB; 4FIY; X-ray; 3.10 A; A/B=1-637.
DR PDBsum; 4FIX; -.
DR PDBsum; 4FIY; -.
DR AlphaFoldDB; O53585; -.
DR SMR; O53585; -.
DR STRING; 83332.Rv3808c; -.
DR BindingDB; O53585; -.
DR ChEMBL; CHEMBL1075096; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; O53585; -.
DR DNASU; 886136; -.
DR GeneID; 886136; -.
DR KEGG; mtu:Rv3808c; -.
DR TubercuList; Rv3808c; -.
DR eggNOG; COG1216; Bacteria.
DR OMA; NGWWMCL; -.
DR PhylomeDB; O53585; -.
DR BioCyc; MetaCyc:G185E-8104-MON; -.
DR BRENDA; 2.4.1.288; 3445.
DR UniPathway; UPA00963; -.
DR PRO; PR:O53585; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035496; F:lipopolysaccharide-1,5-galactosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0008921; F:lipopolysaccharide-1,6-galactosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
DR GO; GO:0070592; P:cell wall polysaccharide biosynthetic process; IDA:MTBBASE.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:MTBBASE.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IDA:MTBBASE.
DR GO; GO:0052573; P:UDP-D-galactose metabolic process; IDA:MTBBASE.
DR InterPro; IPR045699; GlfT2_C.
DR InterPro; IPR040492; GlfT2_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF19320; GlfT2_domain3; 1.
DR Pfam; PF17994; Glft2_N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Magnesium; Manganese; Membrane; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..637
FT /note="Galactofuranosyltransferase GlfT2"
FT /id="PRO_0000395356"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:22707726"
FT BINDING 171
FT /ligand="UDP-alpha-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:66915"
FT /evidence="ECO:0000305|PubMed:22707726"
FT BINDING 200
FT /ligand="UDP-alpha-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:66915"
FT /evidence="ECO:0000305|PubMed:22707726"
FT BINDING 229
FT /ligand="UDP-alpha-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:66915"
FT /evidence="ECO:0000305|PubMed:22707726"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22707726"
FT BINDING 256
FT /ligand="UDP-alpha-D-galactofuranose"
FT /ligand_id="ChEBI:CHEBI:66915"
FT /evidence="ECO:0000305|PubMed:22707726"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22707726"
FT BINDING 396
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22707726"
FT MUTAGEN 300
FT /note="E->S: 1400-fold decrease in transferase activity. No
FT effect on affinity for the substrate UDP-Galf."
FT /evidence="ECO:0000269|PubMed:22707726"
FT MUTAGEN 371
FT /note="D->S: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:22707726"
FT MUTAGEN 372
FT /note="D->S: Loss of transferase activity."
FT /evidence="ECO:0000269|PubMed:22707726"
FT MUTAGEN 399
FT /note="W->S: 1200-fold decrease in transferase activity. No
FT effect on affinity for the substrate UDP-Galf."
FT /evidence="ECO:0000269|PubMed:22707726"
FT MUTAGEN 413
FT /note="H->S: 1700-fold decrease in transferase activity. No
FT effect on affinity for the substrate UDP-Galf."
FT /evidence="ECO:0000269|PubMed:22707726"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:4FIX"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4FIX"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 75..94
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:4FIX"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4FIX"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4FIY"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 432..448
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 452..466
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:4FIX"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:4FIY"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 518..532
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:4FIX"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 581..611
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 613..617
FT /evidence="ECO:0007829|PDB:4FIX"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:4FIX"
SQ SEQUENCE 637 AA; 71507 MW; D7C9AB28B5005B66 CRC64;
MSELAASLLS RVILPRPGEP LDVRKLYLEE STTNARRAHA PTRTSLQIGA ESEVSFATYF
NAFPASYWRR WTTCKSVVLR VQVTGAGRVD VYRTKATGAR IFVEGHDFTG TEDQPAAVET
EVVLQPFEDG GWVWFDITTD TAVTLHSGGW YATSPAPGTA NIAVGIPTFN RPADCVNALR
ELTADPLVDQ VIGAVIVPDQ GERKVRDHPD FPAAAARLGS RLSIHDQPNL GGSGGYSRVM
YEALKNTDCQ QILFMDDDIR LEPDSILRVL AMHRFAKAPM LVGGQMLNLQ EPSHLHIMGE
VVDRSIFMWT AAPHAEYDHD FAEYPLNDNN SRSKLLHRRI DVDYNGWWTC MIPRQVAEEL
GQPLPLFIKW DDADYGLRAA EHGYPTVTLP GAAIWHMAWS DKDDAIDWQA YFHLRNRLVV
AAMHWDGPKA QVIGLVRSHL KATLKHLACL EYSTVAIQNK AIDDFLAGPE HIFSILESAL
PQVHRIRKSY PDAVVLPAAS ELPPPLHKNK AMKPPVNPLV IGYRLARGIM HNLTAANPQH
HRRPEFNVPT QDARWFLLCT VDGATVTTAD GCGVVYRQRD RAKMFALLWQ SLRRQRQLLK
RFEEMRRIYR DALPTLSSKQ KWETALLPAA NQEPEHG
