ID M9NFH8_DROME Unreviewed; 2115 AA.
AC M9NFH8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN Name=GS {ECO:0000313|EMBL:AFH04475.1};
GN Synonyms=Dmel\CG9674 {ECO:0000313|EMBL:AFH04475.1};
GN ORFNames=CG9674 {ECO:0000313|EMBL:AFH04475.1,
GN ECO:0000313|FlyBase:FBgn0036663}, Dmel_CG9674
GN {ECO:0000313|EMBL:AFH04475.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [9] {ECO:0000313|EMBL:AFH04475.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
RN [10] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109357; DOI=.1534/g3.115.018929;
RG FlyBase Consortium;
RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA Gelbart W.M., null;
RT "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT Throughput Data.";
RL G3 (Bethesda) 5:1721-1736(2015).
RN [11] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109356; DOI=.1534/g3.115.018937;
RG FlyBase Consortium;
RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA null;
RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL G3 (Bethesda) 5:1737-1749(2015).
RN [12] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25589440;
RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA Karpen G.H., Celniker S.E.;
RT "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL Genome Res. 25:445-458(2015).
RN [13] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RG Berkeley Drosophila Genome Project;
RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA Rubin G.;
RT "Drosophila melanogaster release 4 sequence.";
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [14] {ECO:0000313|EMBL:AFH04475.1}
RP NUCLEOTIDE SEQUENCE.
RG FlyBase;
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024267};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|PIRSR:PIRSR000187-2};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; AE014296; AFH04475.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94666.1; -; Genomic_DNA.
DR RefSeq; NP_001246804.1; NM_001259875.2.
DR RefSeq; NP_001261973.1; NM_001275044.1.
DR AlphaFoldDB; M9NFH8; -.
DR SMR; M9NFH8; -.
DR STRING; 7227.FBpp0297083; -.
DR PaxDb; 7227-FBpp0297083; -.
DR DNASU; 39878; -.
DR EnsemblMetazoa; FBtr0305916; FBpp0297083; FBgn0036663.
DR EnsemblMetazoa; FBtr0333608; FBpp0305785; FBgn0036663.
DR GeneID; 39878; -.
DR AGR; FB:FBgn0036663; -.
DR FlyBase; FBgn0036663; CG9674.
DR VEuPathDB; VectorBase:FBgn0036663; -.
DR eggNOG; KOG0399; Eukaryota.
DR GeneTree; ENSGT00940000172171; -.
DR InParanoid; M9NFH8; -.
DR OMA; TVFRLQH; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR BioGRID-ORCS; 39878; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Galphas; fly.
DR GenomeRNAi; 39878; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036663; Expressed in head capsule and 29 other cell types or tissues.
DR ExpressionAtlas; M9NFH8; baseline and differential.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR012220; Glu_synth_euk.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000187; GOGAT; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000187-2};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000187-
KW 2}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFH04475.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9NFH8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT DOMAIN 88..481
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 26..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1203
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1209
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1214
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2115 AA; 232205 MW; AE4C0C94C74B091C CRC64;
MAPTITDNCE FECATVEATT TSAITIGDSD NFDSSAIGGS GDNFEESNEL HLNGQQDQDV
QEEQQQQMPW EAPGKQGLYD PQNEHEACGV GFIVAIDGKR SHKILRDAQT LSERMNHRGA
CACDNDTGDG AGVLASIPHG LYSKALAKQG VTLPELGDYA TGIFYLDEAQ HAAAEKEFDD
LAKSLGLEVI AWRTVPSNQS AIGVVARKSE PLSRQVFVRR PAGSDEKAFE RQVFVLRKRA
SHELIKPGRR FYICSLSDRT VVYKGLFTSD QLWDYYTDLK DPEFETYLAL VHTRFSTNTF
PSWERAHPLR VLAHNGEINT LRGNVNLMKA REGVMQSDLF GDQLKKLYPV VEPNLSDSGS
FDCVLEFLTM ASDRSLPESV MTMVPEAWQN DKTMPQEKRD FYQWAACVME PWDGPALISF
TDGRYIGAVL DRNGLRPSRF YVTKENVLVM ASEVGVYDVD PSQVTLKSRL KPGRMLLVDT
KEKKLIQDIE LKAKIAKSRP HSEWLQQKMI TLDEIRNANV LNTPPVDELA KLPASERGIF
DPRLSLFGYS TETVNMLLIP MFKNKKEALG SMGNDAPLAC LSNFQPIPYE YFKQLFAQVT
NPPIDPFREK VVMSMQCPLG PEANLLQPSA QQVHRIWLTN PILSIPDTQL LKRNTHRGWR
TKVLDITFQY NEGVQGYIDA IDRICREGYA AAQAGYQLLV ISDRGAGIDG KVAVSALLAL
GALHHHLIET LQRMKVGIVV ETAEAREVHH ICVLLGYGAD AICPYLAFEL AQALRDDGVI
APEVNDKQIY AAYAQAIDTG IAKVMAKMGI STLQSYKSAQ IFEAVGLGSD LVAKCFRGTQ
SRIGGVTLEI LAKEGLQRYQ LTYGKATPDT RILRNPGQYH WRHGGEAHIN EPSSIGSLQE
AAVNKNLDAF EAFKKTTLDS VKKCALRGQL EFVTDRQSID ISEVEPASEI VKRFATGAMS
FGSISLEAHQ TLSITMNRIG GKSNTGEGGE DSDRYLNQDP NNSRRSAIKQ VASGRFGVTA
SYLANADDLQ IKMAQGAKPG EGGELPGYKV TKDIAKTRKS VPGVGLISPP PHHDIYSIED
LAELIYDLKC SNPNARISVK LVSEVGVGVV ASGVAKGKAE HIVISGHDGG TGASSWTGIK
NAGLPWELGV AETHQVLVLN NLRSRVIVQA DGQLRTGFDV VVAALLGADE FGFSTAPLIV
MGCTMMRKCH LNTCPVGIAT QDPELRKKFT GKPEHVINFF FMLAEDIRKI MAGLGIRKFQ
DLIGRTDLLR VASQRDAKAS NLDLKLLLQP ALELRPGTNI VGGSVKQDFQ LEKRSDNELI
AKAQQIFSGA DDNVTVKMRI HNEERAFGST LSYHIACKYG EAGLPAGKSI DIFLEGSAGQ
SFCAFLARGV NVTLKGDAND YVGKGLCGGN VVIMPQDTVP FESHLNVIVG NVCLYGATEG
TAYFRGIASE RFCVRNSGVT AVVEGVGDHG CEYMTGGVVV ILGLTGRNFA AGMSGGIAYV
YDLDGSFKPK VNPESVELLP LEIEKDVLLV KELLADFIEK TGSKVAKELL DNWAEAQGKF
VKVFPYEYQK ALKDMAEQQA VEQPLKSAIE NGNGKHEPHI KDIEEAIQDV VLEQKRADRV
LDKTRGFVKY KRESAPYRDA GERQKDWDEV YNFPHVRKNL KVQAARCMEC GVPFCQSNST
GCPLGNIIPK WNDLVFHGEW QEALRQLLQT NNFPEFTGRV CPAPCEGSCV LGISEPAVTI
KNIECAIIDH AFEQGWIKPE IPEVRTGKRV AIVGSGPSGL AASQQLNRAG HFVTVFERND
RVGGLLQYGI PTMKLSKEVV KRRVDLMADE GIEFRTNVHV GKDLKAEQLL QEYDAVLLTT
GSTWPRDLPL ANRDLKGIHF AMEFLEAQQK KQLGGKNDII SAAGKNVIII GGGDTGCDCI
ATSLRQGAKS ITTFEILPEP PQKRAQDNPW PQWPKVFRVD YGHEEVKLKW GKDPRQYCTT
TKEFVGENGA IKGVNTVEVE WTKTETGQWR MQEVAGSEKY FPADLILLAM GFLGPEKTVP
SELGLELDPR GNIKASNGQY GTSNSKVFAA GDCRRGQSLV VWAITEGRQA ARQVDSYLTG
RPSGLPGPGG VIATS
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