PURL_THEMA
ID PURL_THEMA Reviewed; 603 AA.
AC Q9X0X3;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; OrderedLocusNames=TM_1246;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-72 IN
RP COMPLEX WITH SUBSTRATE ANALOGS; ATP AND MAGNESIUM, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF HIS-32 AND HIS-72, ACTIVE SITE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=17154526; DOI=10.1021/bi061591u;
RA Morar M., Anand R., Hoskins A.A., Stubbe J., Ealick S.E.;
RT "Complexed structures of formylglycinamide ribonucleotide amidotransferase
RT from Thermotoga maritima describe a novel ATP binding protein
RT superfamily.";
RL Biochemistry 45:14880-14895(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=16544324; DOI=10.1002/prot.20650;
RA Mathews I.I., Krishna S.S., Schwarzenbacher R., McMullan D., Abdubek P.,
RA Ambing E., Canaves J.M., Chiu H.J., Deacon A.M., DiDonato M.,
RA Elsliger M.A., Godzik A., Grittini C., Grzechnik S.K., Hale J., Hampton E.,
RA Han G.W., Haugen J., Jaroszewski L., Klock H.E., Koesema E., Kreusch A.,
RA Kuhn P., Lesley S.A., Levin I., Miller M.D., Moy K., Nigoghossian E.,
RA Paulsen J., Quijano K., Reyes R., Spraggon G., Stevens R.C.,
RA van den Bedem H., Velasquez J., White A., Wolf G., Xu Q., Hodgson K.O.,
RA Wooley J., Wilson I.A.;
RT "Crystal structure of phosphoribosylformylglycinamidine synthase II
RT (smPurL) from Thermotoga maritima at 2.15 A resolution.";
RL Proteins 63:1106-1111(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH ATP, FUNCTION, AND
RP SUBUNIT.
RX PubMed=18597481; DOI=10.1021/bi800329p;
RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.;
RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga
RT maritima: structural insights into complex formation.";
RL Biochemistry 47:7816-7830(2008).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526,
CC ECO:0000269|PubMed:18597481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00420, ECO:0000269|PubMed:17154526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for ATP (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17154526};
CC KM=1.05 mM for FGAR (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17154526};
CC KM=158 mM for NH(4)Cl (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17154526};
CC Note=kcat is 0.39 sec(-1) for FGAM synthase activity with NH(4)Cl as
CC substrate (at pH 8 and 37 degrees Celsius). kcat is 0.40 sec(-1) for
CC FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees
CC Celsius). kcat is 0.41 sec(-1) for FGAM synthase activity with ATP as
CC substrate (at pH 8 and 37 degrees Celsius).;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00420}.
CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00420,
CC ECO:0000269|PubMed:16544324, ECO:0000269|PubMed:17154526,
CC ECO:0000269|PubMed:18597481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC -!- MISCELLANEOUS: Purl possesses an auxiliary ATP Binding region which is
CC not catalytic, but able to bind additional ATP. The conformational
CC changes associated with its binding could have a regulatory role in
CC formation of the PurLSQ complex (PubMed:17154526).
CC {ECO:0000305|PubMed:17154526}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC Rule:MF_00420}.
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DR EMBL; AE000512; AAD36321.1; -; Genomic_DNA.
DR PIR; H72276; H72276.
DR RefSeq; NP_229051.1; NC_000853.1.
DR RefSeq; WP_004080021.1; NC_023151.1.
DR PDB; 1VK3; X-ray; 2.15 A; A=1-603.
DR PDB; 2HRU; X-ray; 2.80 A; A=1-603.
DR PDB; 2HRY; X-ray; 2.80 A; A=1-603.
DR PDB; 2HS0; X-ray; 2.52 A; A=1-603.
DR PDB; 2HS3; X-ray; 2.30 A; A=1-603.
DR PDB; 2HS4; X-ray; 2.70 A; A=1-603.
DR PDB; 3D54; X-ray; 3.50 A; A/E/I=1-603.
DR PDBsum; 1VK3; -.
DR PDBsum; 2HRU; -.
DR PDBsum; 2HRY; -.
DR PDBsum; 2HS0; -.
DR PDBsum; 2HS3; -.
DR PDBsum; 2HS4; -.
DR PDBsum; 3D54; -.
DR AlphaFoldDB; Q9X0X3; -.
DR SMR; Q9X0X3; -.
DR STRING; 243274.THEMA_08105; -.
DR EnsemblBacteria; AAD36321; AAD36321; TM_1246.
DR KEGG; tma:TM1246; -.
DR KEGG; tmw:THMA_1271; -.
DR PATRIC; fig|243274.19.peg.1249; -.
DR eggNOG; COG0046; Bacteria.
DR InParanoid; Q9X0X3; -.
DR OMA; EHCGYSH; -.
DR BRENDA; 6.3.5.3; 6331.
DR UniPathway; UPA00074; UER00128.
DR EvolutionaryTrace; Q9X0X3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.30.70.1670; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR031652; PurL_C.
DR InterPro; IPR038411; PurL_C_sf.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR43555; PTHR43555; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF16904; PurL_C; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..603
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000100501"
FT ACT_SITE 32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:17154526"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:17154526,
FT ECO:0000269|PubMed:18597481"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:17154526,
FT ECO:0000269|PubMed:18597481"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526"
FT BINDING 71..74
FT /ligand="substrate"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT /evidence="ECO:0000305|PubMed:17154526"
FT BINDING 136..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT BINDING 189
FT /ligand="substrate"
FT BINDING 208
FT /ligand="substrate"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526"
FT BINDING 280..282
FT /ligand="substrate"
FT BINDING 388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT /evidence="ECO:0000305|PubMed:17154526"
FT BINDING 429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT /evidence="ECO:0000305|PubMed:17154526"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:17154526,
FT ECO:0000269|PubMed:18597481"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420,
FT ECO:0000269|PubMed:17154526"
FT BINDING 480
FT /ligand="substrate"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT /evidence="ECO:0000305|PubMed:17154526"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="auxiliary"
FT /evidence="ECO:0000305|PubMed:17154526"
FT MUTAGEN 32
FT /note="H->A: Loss of FGAM synthase activity."
FT /evidence="ECO:0000269|PubMed:17154526"
FT MUTAGEN 32
FT /note="H->Q: Loss of FGAM synthase activity."
FT /evidence="ECO:0000269|PubMed:17154526"
FT MUTAGEN 72
FT /note="H->A: Strong decrease of the binding affinity and
FT 20-fold decrease of the catalytic efficiency for FGAR. It
FT has no effect on the ATP binding site, however it affects
FT binding of FGAR."
FT /evidence="ECO:0000269|PubMed:17154526"
FT MUTAGEN 72
FT /note="H->Q: 200-fold decrease of the catalytic efficiency
FT for FGAR. It has no effect on the ATP binding site, however
FT it affects binding of FGAR."
FT /evidence="ECO:0000269|PubMed:17154526"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1VK3"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 56..71
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2HS3"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2HRY"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3D54"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1VK3"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:2HS3"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2HS3"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1VK3"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 415..432
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 436..445
FT /evidence="ECO:0007829|PDB:1VK3"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 453..470
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 493..502
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 512..522
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:1VK3"
FT HELIX 528..540
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:2HS4"
FT HELIX 554..562
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 579..587
FT /evidence="ECO:0007829|PDB:1VK3"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:2HS3"
FT STRAND 595..602
FT /evidence="ECO:0007829|PDB:1VK3"
SQ SEQUENCE 603 AA; 65969 MW; A9F85FE258EE4914 CRC64;
MKLRYLNILK EKLGREPTFV ELQAFSVMWS EHCGYSHTKK YIRRLPKTGF EGNAGVVNLD
DYYSVAFKIE SHNHPSAIEP YNGAATGVGG IIRDVLAMGA RPTAIFDSLH MSRIIDGIIE
GIADYGNSIG VPTVGGELRI SSLYAHNPLV NVLAAGVVRN DMLVDSKASR PGQVIVIFGG
ATGRDGIHGA SFASEDLTGD KATKLSIQVG DPFAEKMLIE AFLEMVEEGL VEGAQDLGAG
GVLSATSELV AKGNLGAIVH LDRVPLREPD MEPWEILISE SQERMAVVTS PQKASRILEI
ARKHLLFGDV VAEVIEEPVY RVMYRNDLVM EVPVQLLANA PEEDIVEYTP GKIPEFKRVE
FEEVNAREVF EQYDHMVGTD TVVPPGFGAA VMRIKRDGGY SLVTHSRADL ALQDTYWGTL
IAVLESVRKT LSVGAEPLAI TNCVNYGDPD VDPVGLSAMM TALKNACEFS GVPVASGNAS
LYNTYQGKPI PPTLVVGMLG KVNPQKVAKP KPSKVFAVGW NDFELEREKE LWRAIRKLSE
EGAFILSSSQ LLTRTHVETF REYGLKIEVK LPEVRPAHQM VLVFSERTPV VDVPVKEIGT
LSR
