GenomeNet

Database: UniProt
Entry: Q18990
LinkDB: Q18990
Original site: Q18990 
ID   PYR1_CAEEL              Reviewed;        2198 AA.
AC   Q18990;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   13-FEB-2019, entry version 152.
DE   RecName: Full=CAD protein {ECO:0000250|UniProtKB:P27708};
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase {ECO:0000250|UniProtKB:P27708};
DE              EC=6.3.5.5 {ECO:0000250|UniProtKB:P27708};
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase {ECO:0000250|UniProtKB:P27708};
DE              EC=2.1.3.2 {ECO:0000250|UniProtKB:P27708};
DE   Includes:
DE     RecName: Full=Dihydroorotase {ECO:0000250|UniProtKB:P27708};
DE              EC=3.5.2.3 {ECO:0000250|UniProtKB:P27708};
GN   Name=pyr-1 {ECO:0000303|PubMed:16828468,
GN   ECO:0000312|WormBase:D2085.1};
GN   ORFNames=D2085.1 {ECO:0000312|WormBase:D2085.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF HIS-1602.
RX   PubMed=16828468; DOI=10.1016/j.ydbio.2006.06.008;
RA   Franks D.M., Izumikawa T., Kitagawa H., Sugahara K., Okkema P.G.;
RT   "C. elegans pharyngeal morphogenesis requires both de novo synthesis
RT   of pyrimidines and synthesis of heparan sulfate proteoglycans.";
RL   Dev. Biol. 296:409-420(2006).
RN   [3] {ECO:0000305}
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-1602.
RX   PubMed=20148972; DOI=10.1111/j.1742-4658.2010.07573.x;
RA   Levitte S., Salesky R., King B., Coe Smith S., Depper M., Cole M.,
RA   Hermann G.J.;
RT   "A Caenorhabditis elegans model of orotic aciduria reveals enlarged
RT   lysosome-related organelles in embryos lacking umps-1 function.";
RL   FEBS J. 277:1420-1439(2010).
CC   -!- FUNCTION: This protein is a "fusion" protein encoding four
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       ATCase and DHOase) (By similarity). Involved in the elongation of
CC       the pharyngeal isthmus during development, probably by providing
CC       precursors of UDP-sugars required for heparan sulfate proteoglycan
CC       biosynthesis (PubMed:16828468). Regulates the organization of the
CC       actin and intermediate filaments cytoskeleton in the pharyngeal
CC       muscles (PubMed:16828468). {ECO:0000250|UniProtKB:P27708,
CC       ECO:0000269|PubMed:16828468}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000250|UniProtKB:P27708};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000250|UniProtKB:P27708};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-
CC         aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814;
CC         EC=3.5.2.3; Evidence={ECO:0000250|UniProtKB:P27708};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P27708};
CC       Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase
CC       activity). {ECO:0000250|UniProtKB:P27708};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Note=Binds 4 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000250|UniProtKB:P27708}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000250|UniProtKB:P27708}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000250|UniProtKB:P27708}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P27708}.
CC   -!- TISSUE SPECIFICITY: Expressed in the intestine.
CC       {ECO:0000269|PubMed:16828468}.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in gut precursor
CC       cells from the 4E embryonic stage until the bean stage. Expression
CC       resumes at the L1 larval stage and continues into adulthood.
CC       {ECO:0000269|PubMed:16828468}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at
CC       the embryonic stage or at the L1 larval stage (PubMed:16828468).
CC       The few surviving animals grow more slowly (PubMed:16828468). L1
CC       larvae have incomplete pharyngeal isthmus elongation, 36 percent
CC       of which have the pharynx detached from the buccal cavity
CC       (PubMed:16828468). In an umps-1 zu456 mutant background embryo,
CC       prevents the formation of abnormally enlarged gut granules
CC       (PubMed:20148972). {ECO:0000269|PubMed:16828468,
CC       ECO:0000269|PubMed:20148972}.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) form together the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5). {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-
CC       dependent hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000305}.
DR   EMBL; BX284602; CAA91059.2; -; Genomic_DNA.
DR   RefSeq; NP_495838.2; NM_063437.4.
DR   UniGene; Cel.33265; -.
DR   ProteinModelPortal; Q18990; -.
DR   SMR; Q18990; -.
DR   STRING; 6239.D2085.1; -.
DR   EPD; Q18990; -.
DR   PaxDb; Q18990; -.
DR   PeptideAtlas; Q18990; -.
DR   EnsemblMetazoa; D2085.1; D2085.1; WBGene00004259.
DR   GeneID; 174385; -.
DR   KEGG; cel:CELE_D2085.1; -.
DR   UCSC; D2085.1; c. elegans.
DR   CTD; 174385; -.
DR   WormBase; D2085.1; CE41886; WBGene00004259; pyr-1.
DR   eggNOG; KOG0370; Eukaryota.
DR   eggNOG; COG0458; LUCA.
DR   eggNOG; COG0505; LUCA.
DR   eggNOG; COG0540; LUCA.
DR   GeneTree; ENSGT00940000157241; -.
DR   HOGENOM; HOG000234584; -.
DR   InParanoid; Q18990; -.
DR   KO; K11540; -.
DR   OMA; FTNANDH; -.
DR   OrthoDB; 273358at2759; -.
DR   PhylomeDB; Q18990; -.
DR   Reactome; R-CEL-500753; Pyrimidine biosynthesis.
DR   UniPathway; UPA00070; UER00115.
DR   UniPathway; UPA00070; UER00116.
DR   UniPathway; UPA00070; UER00117.
DR   PRO; PR:Q18990; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004259; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR   GO; GO:1905905; P:pharyngeal gland morphogenesis; IMP:UniProtKB.
DR   GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IMP:WormBase.
DR   GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Glutamine amidotransferase; Hydrolase;
KW   Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat; Transferase; Zinc.
FT   CHAIN         1   2198       CAD protein. {ECO:0000305}.
FT                                /FTId=PRO_0000438771.
FT   DOMAIN      180    366       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   DOMAIN      516    708       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1054   1245       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1318   1474       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     542    597       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND    1080   1137       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION        3    368       GATase (Glutamine amidotransferase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION      392   1467       CPSase (Carbamoyl-phosphate synthase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION      392    934       CPSase A. {ECO:0000250|UniProtKB:P08955}.
FT   REGION      935   1467       CPSase B. {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1468   1799       DHOase (dihydroorotase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1800   1870       Linker. {ECO:0000250|UniProtKB:P08955}.
FT   REGION     1871   2196       ATCase (Aspartate transcarbamylase).
FT                                {ECO:0000250|UniProtKB:P08955}.
FT   ACT_SITE    255    255       Nucleophile; for GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    339    339       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    341    341       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   METAL       665    665       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       679    679       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       679    679       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       681    681       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1204   1204       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1216   1216       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1216   1216       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1218   1218       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1483   1483       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1483   1483       Zinc 2; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1485   1485       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1568   1568       Zinc 1; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1568   1568       Zinc 3; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1602   1602       Zinc 3; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1626   1626       Zinc 3; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1649   1649       Zinc 2. {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1695   1695       Zinc 1. {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1487   1487       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1517   1517       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1670   1670       N-carbamoyl-L-aspartate; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1695   1695       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1699   1699       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1568   1568       N6-carboxylysine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MUTAGEN    1602   1602       H->Q: In cu8; probable loss of
FT                                dihydroorotase activity. Severe late
FT                                stage embryonic lethality. The few
FT                                surviving mutants have a shorter and
FT                                thicker pharyngeal isthmus, an abnormal
FT                                knobbed tail, mild egg-laying defects,
FT                                moderate fluid accumulation in the coelom
FT                                and a slower growth. Actin and
FT                                intermediate filaments are disorganized
FT                                in the pharynx. Moderate reduction in
FT                                heparan sulfate levels and increased
FT                                levels of chondroitin sulfate. In an
FT                                umps-1 zu456 mutant background embryo,
FT                                prevents the formation of abnormally
FT                                enlarged gut granules.
FT                                {ECO:0000269|PubMed:16828468,
FT                                ECO:0000269|PubMed:20148972}.
SQ   SEQUENCE   2198 AA;  242582 MW;  31CFC62E64D21B1E CRC64;
     MRATLHLEDG STFVGSIYGA TKSVVGEIVF QTGMVGYVES LTDPSYAKQL LTLTYPLIGN
     YGVPSAEILD QFKLPAEFES DRIWPAALIV EKICVDGEHS HWQAVQSLSE WLRKADVPCL
     SGIDVRQLVK KIRETGTMKA KLVIESDNAQ NFDYVDVNAE NLVDFVSRKE PVVYGSGDQT
     ILAVDCGLKN NQIRCLAKRG FRVKVVPWNH PIDTESDYDG LFLSNGPGDP EICAPLVDRL
     AKVIARGDKP IFGICLGHQI LSRAIGAKTY KLKYGNRGHN QPCTHYATGR CYITSQNHGY
     AVDPDSLPAD WKALFTNEND KTNEGIVHSS KPFFSVQFHP EHTAGPTDCE FLFDVFADSV
     RQAKSGTFMN VDQELTRLMT FTPIYHAKEQ RKVLVLGSGG LTIGQAGEFD YSGAQALKAL
     REEGIRTVLI NPNIATVQTS KGFADFTYFL PITKEYVTDV IKKERPTGIL CTFGGQTALN
     CAIDLYKDGI FEQYDVQVLG TQINTIMKTE DRDLFNQEIS AIGEKVAPSK AATTMEGAIE
     AAEELGYPVL VRAAYALGGL GSGFADNREE LIAIAQQALA HSNQVLVDKS LKGWKEVEYE
     VVRDAYDNCI TVCNMENVDP LGIHTGESVV VAPSQTLSDR EYNALRTCAI KVIRHLGIIG
     ECNIQYALDP YSLTYYIIEV NARLSRSSAL ASKATGYPLA YVAAKLALGQ HLPVIRNSVT
     GTTTACFEPS LDYCVVKIPR WDLGKFARVS TQIGSSMKSV GEVMGIGRCF EEALQKALRM
     VSDHADGFSP YTFSRPTTAD DLSKPTDKRM FALARGMYYG DFDVEKAHEL TRIDRWFLFR
     MQNIVDIYHR LEKTDVNTVS AELLLEAKQA GFSDRQIAKK IGSNEYTVRE ARFVKGITPC
     VKQIDTVAGE WPAQTNYLYT TFNGIENDVS FNMKNAVMVL GSGVYRIGSS VEFDSSCVGC
     IRELKALGYS TITVNCNPET VSTDYDICDR LYFEEISFET VLDVYHLEKP KGVILAFGGQ
     APNNIAMSLS RAQVKIFGTS PNDIDNAEDR FKFSRKLESL KISQPQWKKS ENMEDAKNFC
     AQVGYPCLIR PSYVLSGAAM NVAHNAEDLE VFLKQAAVVA KEHPVVVSKF INEAKELDVD
     AVALDGKLVV MAVSEHIENA GVHSGDATLV TPAQDMNKLT LDRIKDITFR IAEAFNVNGP
     FNMQLIAKNN ELKVIECNLR VSRSFPFVSK TLDYDFVALA TRAMMASDSP AIRATIKPTA
     TLLKGKGRVG VKVPQFSFSR LAGADVMLGV EMASTGEVAC FGTSRCDAYL KALLSTGFVV
     PKQNIFISIG GYHAKAEMLK SVEALLKLGY ELYGSKGTAD YFQSNKINVK PVDWPFEEGS
     SDEKTASGTR SVVEFLENKE FHLVINLPIR GSGAYRVSAF RTHGYKTRRM AIDNGIPLIT
     DIKCAKTFIQ ALEMVGKRPT MNSLVDCVTS KSLKRLPGMV DIHVHVREPG ATHKEDWATC
     SKAALAGGVT TILAMPNTSP VLVDTDSFYQ TEQLASAKSV VDYALYIGAT PNNSKFAAEF
     ADKAAGLKMY LNETFSTLKM DNISDWAKHL SAFPANRPIV CHAEKQTLAA ILCMAQMANR
     AVHIAHVATA DEINLVKEAK QRGWNVTCEV CPHHLFLIEE DLPDGIREVR PRLVKPEDRQ
     ALWDNMEYID CFATDHAPHT WAEKTGKDGK IPPGFPGVEY MLPLLLTAVH DGKLTMKELT
     DRMSTNPRRI FNLPPQDDTY IEVDLNEEWT IPENGGQSKA GWTPFAGRKV FGKVHNVIIR
     GEEAVIDGRI VAIPGFGKNV RLYPHSGTAH RGDSDFDQIL EPIPQQMIES SSDEQSPLHT
     PPRAHTPIAF PGELLAKNCI SVKHLDKGQI NRIFELADRY KHDVEKGHPL THILNGKVLV
     NLFYEVSTRT SCSFSAAMQR LGGSVISVDS QSSSVQKGET LEDTVQVLGS YGDILVLRSN
     ENGAADRAAR VCDQPVINGG DGTGEHPTQA LLDVYTIRQE MGTVNGLTIA LVGDLKNGRT
     VHSLAKLLCL YKDITLHYVA PSTELEMPQE VLDYVSSKSN FVQKKFTSLA EGINHVDVVY
     VTRIQKERFS SPDEYNKVKG SYVINAKLLN EAARDVEEPS SLLVPARSLP IVMHPLPRVD
     EIAVELDHDE RAAYFRQAKN GVFVRMSILS LLLGRGHL
//
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