PYRG_DROME
ID PYRG_DROME Reviewed; 627 AA.
AC Q9VUL1; Q9VUL0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=CTP synthase;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase;
DE AltName: Full=UTP--ammonia ligase;
GN Name=CTPsyn; ORFNames=CG45070;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., 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.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; SER-570; SER-571;
RP SER-588 AND THR-595, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20513629; DOI=10.1016/s1673-8527(09)60046-1;
RA Liu J.L.;
RT "Intracellular compartmentation of CTP synthase in Drosophila.";
RL J. Genet. Genomics 37:281-296(2010).
RN [7]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1 AND 2), TISSUE
RP SPECIFICITY (ISOFORM 1 AND 2), DEVELOPMENTAL STAGE (ISOFORM 1 AND 2), AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23459760; DOI=10.1371/journal.pgen.1003256;
RA Azzam G., Liu J.L.;
RT "Only one isoform of Drosophila melanogaster CTP synthase forms the
RT cytoophidium.";
RL PLoS Genet. 9:E1003256-E1003256(2013).
RN [8]
RP FUNCTION (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=25223282; DOI=10.15252/embr.201438688;
RA Strochlic T.I., Stavrides K.P., Thomas S.V., Nicolas E., O'Reilly A.M.,
RA Peterson J.R.;
RT "Ack kinase regulates CTP synthase filaments during Drosophila oogenesis.";
RL EMBO Rep. 15:1184-1191(2014).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC the rate-limiting enzyme in the synthesis of cytosine nucleotides.
CC {ECO:0000250|UniProtKB:Q9NRF8}.
CC -!- FUNCTION: [Isoform 1]: Required for assembly of cytoophidium in female
CC germline cells (PubMed:23459760, PubMed:25223282). In nurse cells,
CC CTPsyn filament assembly in the cytoophidium is regulated by Ack kinase
CC which may thereby contribute to the control of CTP production at
CC specific stages of oogenesis and development of the nurse cell membrane
CC (PubMed:25223282). {ECO:0000269|PubMed:23459760,
CC ECO:0000269|PubMed:25223282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:20513629, ECO:0000269|PubMed:23459760}.
CC Note=Localizes to cytoophidium, a subcellular filamentary structure
CC where CTP synthase is compartmentalized. {ECO:0000269|PubMed:23459760,
CC ECO:0000269|PubMed:25223282}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:23459760}. Note=Does not localize to cytoophidium.
CC {ECO:0000269|PubMed:23459760}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305}; Synonyms=C {ECO:0000303|PubMed:23459760,
CC ECO:0000312|FlyBase:FBgn0266452};
CC IsoId=Q9VUL1-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=B {ECO:0000303|PubMed:23459760,
CC ECO:0000312|FlyBase:FBgn0266452};
CC IsoId=Q9VUL1-2; Sequence=VSP_019897;
CC -!- TISSUE SPECIFICITY: In ovary, expressed in oocytes, follicle cells and
CC nurse cells. Also expressed in larval and adult testis (at protein
CC level). In larvae, expressed in lymph gland, salivary gland, regions of
CC the midgut, testis, optical lobe and trachea. Isoform 1 is expressed in
CC adult testis, ovary, accessory gland and head. Isoform 2 is weakly
CC expressed in ovary. {ECO:0000269|PubMed:20513629,
CC ECO:0000269|PubMed:23459760}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 expression is high during embryogenesis,
CC modest during larval and pupal stages and abundant in adult. Isoform 2
CC is expressed at low levels in 0-4h embryos and at very low levels
CC during the rest of developmental stages and in adult.
CC {ECO:0000269|PubMed:23459760}.
CC -!- DISRUPTION PHENOTYPE: Larval lethal. {ECO:0000269|PubMed:23459760}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49665.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49666.1; -; Genomic_DNA.
DR EMBL; AY058581; AAL13810.1; -; mRNA.
DR EMBL; BT003255; AAO25012.1; -; mRNA.
DR RefSeq; NP_001287067.1; NM_001300138.1. [Q9VUL1-1]
DR RefSeq; NP_648747.1; NM_140490.4. [Q9VUL1-2]
DR RefSeq; NP_730023.1; NM_168606.2. [Q9VUL1-1]
DR PDB; 6L6Z; EM; 6.09 A; A/B/C/D/E/F/G/H=1-562.
DR PDB; 6LFG; EM; 9.58 A; A/B/C/D/E/F/G/H=1-562.
DR PDB; 7DPT; EM; 2.48 A; A/B/C/D=1-627.
DR PDB; 7DPW; EM; 2.65 A; A/B/C/D=1-556.
DR PDBsum; 6L6Z; -.
DR PDBsum; 6LFG; -.
DR PDBsum; 7DPT; -.
DR PDBsum; 7DPW; -.
DR AlphaFoldDB; Q9VUL1; -.
DR SMR; Q9VUL1; -.
DR BioGRID; 64967; 18.
DR IntAct; Q9VUL1; 30.
DR STRING; 7227.FBpp0075387; -.
DR MEROPS; C26.A36; -.
DR iPTMnet; Q9VUL1; -.
DR PaxDb; Q9VUL1; -.
DR PRIDE; Q9VUL1; -.
DR DNASU; 39645; -.
DR EnsemblMetazoa; FBtr0344431; FBpp0310803; FBgn0266452. [Q9VUL1-1]
DR EnsemblMetazoa; FBtr0344432; FBpp0310804; FBgn0266452. [Q9VUL1-2]
DR EnsemblMetazoa; FBtr0345691; FBpp0311740; FBgn0266452. [Q9VUL1-1]
DR GeneID; 39645; -.
DR KEGG; dme:Dmel_CG45070; -.
DR UCSC; CG6854-RB; d. melanogaster. [Q9VUL1-1]
DR CTD; 39645; -.
DR FlyBase; FBgn0266452; CTPsyn.
DR VEuPathDB; VectorBase:FBgn0266452; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_4_1_1; -.
DR InParanoid; Q9VUL1; -.
DR OMA; EFNNAYR; -.
DR PhylomeDB; Q9VUL1; -.
DR Reactome; R-DME-499943; Interconversion of nucleotide di- and triphosphates.
DR SignaLink; Q9VUL1; -.
DR UniPathway; UPA00159; UER00277.
DR BioGRID-ORCS; 39645; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 39645; -.
DR PRO; PR:Q9VUL1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0266452; Expressed in wing disc and 55 other tissues.
DR ExpressionAtlas; Q9VUL1; baseline and differential.
DR Genevisible; Q9VUL1; DM.
DR GO; GO:0097268; C:cytoophidium; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IDA:FlyBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..627
FT /note="CTP synthase"
FT /id="PRO_0000247038"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 599..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..56
FT /note="MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSP
FT YEHG -> MAPKKSTIVLNVEQFIHDIEERPAIWNRNFHCNKAFLEQMWDELSGAHKLP
FT S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_019897"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 401..413
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 472..484
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:7DPT"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:7DPT"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 538..547
FT /evidence="ECO:0007829|PDB:7DPT"
FT HELIX 551..555
FT /evidence="ECO:0007829|PDB:7DPT"
SQ SEQUENCE 627 AA; 69448 MW; 4F0DFCF2CFC113B0 CRC64;
MKYILVTGGV ISGVGKGVIA SSFGTLLKSC GLDVTSIKID PYINIDAGTF SPYEHGEVYV
LDDGAEVDLD LGNYERFLDV TLHRDNNITT GKIYKLVIEK ERTGEYLGKT VQVVPHITDA
IQEWVERVAQ TPVQGSSKPQ VCIVELGGTI GDIEGMPFVE AFRQFQFRVK RENFCLAHVS
LVPLPKATGE PKTKPTQSSV RELRGCGLSP DLIVCRSEKP IGLEVKEKIS NFCHVGPDQV
ICIHDLNSIY HVPLLMEQNG VIEYLNERLQ LNIDMSKRTK CLQQWRDLAR RTETVRREVC
IAVVGKYTKF TDSYASVVKA LQHAALAVNR KLELVFIESC LLEEETLHSE PSKYHKEWQK
LCDSHGILVP GGFGSRGMEG KIRACQWARE NQKPLLGICL GLQAAVIEFA RNKLGLKDAN
TTEIDPNTAN ALVIDMPEHH TGQLGGTMRL GKRITVFSDG PSVIRQLYGN PKSVQERHRH
RYEVNPKYVH LLEEQGMRFV GTDVDKTRME IIELSGHPYF VATQYHPEYL SRPLKPSPPF
LGLILASVDR LNQYIQRGCR LSPRQLSDAS SDEEDSVVGL AGATKSLSSL KIPITPTNGI
SKSCNGSIST SDSEGACGGV DPTNGHK
