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Database: UniProt
Entry: P53131
LinkDB: P53131
Original site: P53131 
ID   PRP43_YEAST             Reviewed;         767 AA.
AC   P53131; D6VU28;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-OCT-2019, entry version 190.
DE   RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43;
DE            EC=3.6.4.13;
DE   AltName: Full=Helicase JA1;
GN   Name=PRP43; OrderedLocusNames=YGL120C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP   GLY-194; SER-247 AND GLY-395.
RC   STRAIN=SS330;
RX   PubMed=9342317; DOI=10.1073/pnas.94.22.11798;
RA   Arenas J.E., Abelson J.N.;
RT   "Prp43: an RNA helicase-like factor involved in spliceosome
RT   disassembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11798-11802(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPP382.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
RA   Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
RA   Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
RA   Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of
RT   technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION IN THE NTC-RELATED COMPLEX, AND INTERACTION WITH NTR1
RP   AND NTR2.
RX   PubMed=16357217; DOI=10.1101/gad.1377405;
RA   Tsai R.-T., Fu R.-H., Yeh F.-L., Tseng C.-K., Lin Y.-C., Huang Y.-H.,
RA   Cheng S.-C.;
RT   "Spliceosome disassembly catalyzed by Prp43 and its associated
RT   components Ntr1 and Ntr2.";
RL   Genes Dev. 19:2991-3003(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
RA   Mann M., Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone
RT   signaling pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH NTR1 AND NTR2.
RX   PubMed=16880513; DOI=10.1128/mcb.02347-05;
RA   Boon K.-L., Auchynnikava T., Edwalds-Gilbert G., Barrass J.D.,
RA   Droop A.P., Dez C., Beggs J.D.;
RT   "Yeast ntr1/spp382 mediates prp43 function in postspliceosomes.";
RL   Mol. Cell. Biol. 26:6016-6023(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-9, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC       spliceosomes after the release of mature mRNA.
CC       {ECO:0000269|PubMed:16880513, ECO:0000269|PubMed:9342317}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Component of the NTR complex (NTC-related complex),
CC       composed of NTR1, NTR2 and PRP43. Interacts with NTR1 and NTR2.
CC       Interacts with SPP382. {ECO:0000269|PubMed:14690591,
CC       ECO:0000269|PubMed:16357217, ECO:0000269|PubMed:16880513}.
CC   -!- INTERACTION:
CC       P36009:DHR2; NbExp=2; IntAct=EBI-505, EBI-5844;
CC       P36049:EBP2; NbExp=3; IntAct=EBI-505, EBI-6289;
CC       P43586:LOC1; NbExp=3; IntAct=EBI-505, EBI-22906;
CC       P47035:NET1; NbExp=2; IntAct=EBI-505, EBI-25953;
CC       Q08208:NOP12; NbExp=2; IntAct=EBI-505, EBI-35895;
CC       P53927:NOP15; NbExp=3; IntAct=EBI-505, EBI-28853;
CC       P37838:NOP4; NbExp=3; IntAct=EBI-505, EBI-12122;
CC       P40078:NSA2; NbExp=3; IntAct=EBI-505, EBI-22681;
CC       P53335:PXR1; NbExp=6; IntAct=EBI-505, EBI-23652;
CC       P10964:RPA190; NbExp=2; IntAct=EBI-505, EBI-15730;
CC       Q06411:SPP382; NbExp=11; IntAct=EBI-505, EBI-576;
CC       P53866:SQS1; NbExp=11; IntAct=EBI-505, EBI-29168;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 16900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX15/PRP43 sub-subfamily. {ECO:0000305}.
DR   EMBL; U41851; AAB86458.1; -; Genomic_DNA.
DR   EMBL; Z72642; CAA96828.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07989.1; -; Genomic_DNA.
DR   PIR; S64130; S64130.
DR   RefSeq; NP_011395.1; NM_001180985.1.
DR   PDB; 2XAU; X-ray; 1.90 A; A/B=1-767.
DR   PDB; 3KX2; X-ray; 2.20 A; A/B=1-767.
DR   PDB; 5I8Q; X-ray; 4.20 A; A/B=1-767.
DR   PDB; 5JPT; X-ray; 2.94 A; A/B=1-767.
DR   PDB; 5Y88; EM; 3.70 A; W=1-767.
DR   PDBsum; 2XAU; -.
DR   PDBsum; 3KX2; -.
DR   PDBsum; 5I8Q; -.
DR   PDBsum; 5JPT; -.
DR   PDBsum; 5Y88; -.
DR   SMR; P53131; -.
DR   BioGrid; 33131; 464.
DR   ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR   ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR   ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR   ComplexPortal; CPX-1886; Post-mRNA release spliceosomal complex.
DR   DIP; DIP-5152N; -.
DR   IntAct; P53131; 172.
DR   MINT; P53131; -.
DR   STRING; 4932.YGL120C; -.
DR   iPTMnet; P53131; -.
DR   MaxQB; P53131; -.
DR   PaxDb; P53131; -.
DR   PRIDE; P53131; -.
DR   EnsemblFungi; YGL120C_mRNA; YGL120C; YGL120C.
DR   GeneID; 852757; -.
DR   KEGG; sce:YGL120C; -.
DR   EuPathDB; FungiDB:YGL120C; -.
DR   SGD; S000003088; PRP43.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; P53131; -.
DR   KO; K12820; -.
DR   OMA; QWCVDFA; -.
DR   BioCyc; YEAST:G3O-30617-MONOMER; -.
DR   EvolutionaryTrace; P53131; -.
DR   PRO; PR:P53131; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IMP:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IGI:SGD.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   GO; GO:0000390; P:spliceosomal complex disassembly; IDA:SGD.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    767       Pre-mRNA-splicing factor ATP-dependent
FT                                RNA helicase PRP43.
FT                                /FTId=PRO_0000055145.
FT   DOMAIN      103    268       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      293    473       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     116    123       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       215    218       DEAH box.
FT   MOD_RES       8      8       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES       9      9       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN     194    194       G->D: In PRP43-DN1; dominant-negative
FT                                phenotype. {ECO:0000269|PubMed:9342317}.
FT   MUTAGEN     247    247       S->L: In PRP43-DN2; dominant-negative
FT                                phenotype. {ECO:0000269|PubMed:9342317}.
FT   MUTAGEN     395    395       G->E: In PRP43-1; temperature-sensitive.
FT                                {ECO:0000269|PubMed:9342317}.
FT   STRAND        9     11       {ECO:0000244|PDB:2XAU}.
FT   TURN         14     17       {ECO:0000244|PDB:2XAU}.
FT   HELIX        19     33       {ECO:0000244|PDB:2XAU}.
FT   TURN         49     52       {ECO:0000244|PDB:2XAU}.
FT   HELIX        60     68       {ECO:0000244|PDB:2XAU}.
FT   STRAND       69     71       {ECO:0000244|PDB:2XAU}.
FT   TURN         73     75       {ECO:0000244|PDB:2XAU}.
FT   STRAND       76     78       {ECO:0000244|PDB:5JPT}.
FT   HELIX        81     90       {ECO:0000244|PDB:2XAU}.
FT   HELIX        94     98       {ECO:0000244|PDB:2XAU}.
FT   HELIX        99    108       {ECO:0000244|PDB:2XAU}.
FT   STRAND      110    115       {ECO:0000244|PDB:2XAU}.
FT   HELIX       122    134       {ECO:0000244|PDB:2XAU}.
FT   HELIX       136    139       {ECO:0000244|PDB:2XAU}.
FT   STRAND      142    148       {ECO:0000244|PDB:2XAU}.
FT   HELIX       150    163       {ECO:0000244|PDB:2XAU}.
FT   TURN        169    171       {ECO:0000244|PDB:2XAU}.
FT   STRAND      172    176       {ECO:0000244|PDB:2XAU}.
FT   STRAND      179    181       {ECO:0000244|PDB:2XAU}.
FT   STRAND      187    192       {ECO:0000244|PDB:2XAU}.
FT   HELIX       193    202       {ECO:0000244|PDB:2XAU}.
FT   STRAND      209    214       {ECO:0000244|PDB:2XAU}.
FT   HELIX       217    219       {ECO:0000244|PDB:2XAU}.
FT   HELIX       222    237       {ECO:0000244|PDB:2XAU}.
FT   STRAND      242    248       {ECO:0000244|PDB:2XAU}.
FT   HELIX       253    258       {ECO:0000244|PDB:2XAU}.
FT   STRAND      264    266       {ECO:0000244|PDB:2XAU}.
FT   STRAND      274    277       {ECO:0000244|PDB:2XAU}.
FT   HELIX       286    300       {ECO:0000244|PDB:2XAU}.
FT   STRAND      305    309       {ECO:0000244|PDB:2XAU}.
FT   HELIX       313    334       {ECO:0000244|PDB:2XAU}.
FT   STRAND      339    344       {ECO:0000244|PDB:2XAU}.
FT   HELIX       350    353       {ECO:0000244|PDB:2XAU}.
FT   HELIX       354    357       {ECO:0000244|PDB:2XAU}.
FT   STRAND      364    367       {ECO:0000244|PDB:2XAU}.
FT   STRAND      370    375       {ECO:0000244|PDB:2XAU}.
FT   HELIX       378    381       {ECO:0000244|PDB:2XAU}.
FT   STRAND      388    393       {ECO:0000244|PDB:2XAU}.
FT   STRAND      395    403       {ECO:0000244|PDB:2XAU}.
FT   TURN        404    407       {ECO:0000244|PDB:2XAU}.
FT   STRAND      408    415       {ECO:0000244|PDB:2XAU}.
FT   HELIX       418    426       {ECO:0000244|PDB:2XAU}.
FT   HELIX       427    429       {ECO:0000244|PDB:2XAU}.
FT   STRAND      430    440       {ECO:0000244|PDB:2XAU}.
FT   HELIX       442    447       {ECO:0000244|PDB:2XAU}.
FT   HELIX       456    459       {ECO:0000244|PDB:2XAU}.
FT   HELIX       463    471       {ECO:0000244|PDB:2XAU}.
FT   HELIX       477    479       {ECO:0000244|PDB:2XAU}.
FT   HELIX       488    500       {ECO:0000244|PDB:2XAU}.
FT   HELIX       512    517       {ECO:0000244|PDB:2XAU}.
FT   STRAND      520    522       {ECO:0000244|PDB:2XAU}.
FT   HELIX       524    532       {ECO:0000244|PDB:2XAU}.
FT   HELIX       533    536       {ECO:0000244|PDB:2XAU}.
FT   HELIX       539    549       {ECO:0000244|PDB:2XAU}.
FT   STRAND      559    561       {ECO:0000244|PDB:5JPT}.
FT   HELIX       562    570       {ECO:0000244|PDB:2XAU}.
FT   HELIX       578    589       {ECO:0000244|PDB:2XAU}.
FT   HELIX       592    597       {ECO:0000244|PDB:2XAU}.
FT   HELIX       599    605       {ECO:0000244|PDB:2XAU}.
FT   HELIX       610    629       {ECO:0000244|PDB:2XAU}.
FT   HELIX       644    656       {ECO:0000244|PDB:2XAU}.
FT   STRAND      659    663       {ECO:0000244|PDB:2XAU}.
FT   TURN        665    667       {ECO:0000244|PDB:3KX2}.
FT   STRAND      670    672       {ECO:0000244|PDB:2XAU}.
FT   TURN        673    675       {ECO:0000244|PDB:2XAU}.
FT   STRAND      678    681       {ECO:0000244|PDB:2XAU}.
FT   STRAND      692    712       {ECO:0000244|PDB:2XAU}.
FT   HELIX       715    721       {ECO:0000244|PDB:2XAU}.
FT   TURN        723    725       {ECO:0000244|PDB:2XAU}.
FT   HELIX       728    730       {ECO:0000244|PDB:2XAU}.
FT   HELIX       735    748       {ECO:0000244|PDB:2XAU}.
SQ   SEQUENCE   767 AA;  87562 MW;  DA8A085EC50FF430 CRC64;
     MGSKRRFSSE HPDPVETSIP EQAAEIAEEL SKQHPLPSEE PLVHHDAGEF KGLQRHHTSA
     EEAQKLEDGK INPFTGREFT PKYVDILKIR RELPVHAQRD EFLKLYQNNQ IMVFVGETGS
     GKTTQIPQFV LFDEMPHLEN TQVACTQPRR VAAMSVAQRV AEEMDVKLGE EVGYSIRFEN
     KTSNKTILKY MTDGMLLREA MEDHDLSRYS CIILDEAHER TLATDILMGL LKQVVKRRPD
     LKIIIMSATL DAEKFQRYFN DAPLLAVPGR TYPVELYYTP EFQRDYLDSA IRTVLQIHAT
     EEAGDILLFL TGEDEIEDAV RKISLEGDQL VREEGCGPLS VYPLYGSLPP HQQQRIFEPA
     PESHNGRPGR KVVISTNIAE TSLTIDGIVY VVDPGFSKQK VYNPRIRVES LLVSPISKAS
     AQQRAGRAGR TRPGKCFRLY TEEAFQKELI EQSYPEILRS NLSSTVLELK KLGIDDLVHF
     DFMDPPAPET MMRALEELNY LACLDDEGNL TPLGRLASQF PLDPMLAVML IGSFEFQCSQ
     EILTIVAMLS VPNVFIRPTK DKKRADDAKN IFAHPDGDHI TLLNVYHAFK SDEAYEYGIH
     KWCRDHYLNY RSLSAADNIR SQLERLMNRY NLELNTTDYE SPKYFDNIRK ALASGFFMQV
     AKKRSGAKGY ITVKDNQDVL IHPSTVLGHD AEWVIYNEFV LTSKNYIRTV TSVRPEWLIE
     IAPAYYDLSN FQKGDVKLSL ERIKEKVDRL NELKQGKNKK KSKHSKK
//
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