GenomeNet

Database: UniProt
Entry: P23394
LinkDB: P23394
Original site: P23394 
ID   PRP28_YEAST             Reviewed;         588 AA.
AC   P23394; D6VSM3; P20450;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   16-OCT-2019, entry version 190.
DE   RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28;
DE            EC=3.6.4.13;
DE   AltName: Full=Helicase CA8;
GN   Name=PRP28; OrderedLocusNames=YDR243C; ORFNames=YD8419.10C;
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-297.
RC   STRAIN=YJJ48;
RX   PubMed=2010088; DOI=10.1101/gad.5.4.629;
RA   Strauss E.J., Guthrie C.;
RT   "A cold-sensitive mRNA splicing mutant is a member of the RNA helicase
RT   gene family.";
RL   Genes Dev. 5:629-641(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-526.
RX   PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
RA   Chang T.-H., Arenas J., Abelson J.;
RT   "Identification of five putative yeast RNA helicase genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=7520570; DOI=10.1093/nar/22.15.3187;
RA   Strauss E.J., Guthrie C.;
RT   "PRP28, a 'DEAD-box' protein, is required for the first step of mRNA
RT   splicing in vitro.";
RL   Nucleic Acids Res. 22:3187-3193(1994).
RN   [6]
RP   MUTAGENESIS OF ALA-221; THR-223; ARG-264; GLU-265; THR-317; GLY-319;
RP   MET-376; ALA-379; PRO-438; ILE-440; PHE-442; ALA-449; HIS-468;
RP   ASN-486; MET-491; ARG-499; ASP-502; TYR-521; ARG-527; VAL-541;
RP   ASP-546; LEU-549; LYS-580; ASN-584 AND ILE-586.
RX   PubMed=9396812; DOI=10.1093/nar/25.24.5033;
RA   Chang T.-H., Latus L.J., Liu Z., Abbott J.M.;
RT   "Genetic interactions of conserved regions in the DEAD-box protein
RT   Prp28p.";
RL   Nucleic Acids Res. 25:5033-5040(1997).
RN   [7]
RP   FUNCTION.
RX   PubMed=10024879; DOI=10.1016/s1097-2765(00)80174-4;
RA   Staley J.P., Guthrie C.;
RT   "An RNA switch at the 5' splice site requires ATP and the DEAD box
RT   protein Prp28p.";
RL   Mol. Cell 3:55-64(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=11172727; DOI=10.1016/s1097-2765(01)00170-8;
RA   Chen J.Y.-F., Stands L., Staley J.P., Jackups R.R. Jr., Latus L.J.,
RA   Chang T.-H.;
RT   "Specific alterations of U1-C protein or U1 small nuclear RNA can
RT   eliminate the requirement of Prp28p, an essential DEAD box splicing
RT   factor.";
RL   Mol. Cell 7:227-232(2001).
RN   [9]
RP   IDENTIFICATION IN THE U5 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=11720284;
RA   Stevens S.W., Barta I., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA   Abelson J.;
RT   "Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small
RT   nuclear ribonucleoproteins from Saccharomyces cerevisiae.";
RL   RNA 7:1543-1553(2001).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION
RP   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: ATP-dependent RNA helicase involved in mRNA splicing.
CC       May destabilize the U1/5'-splice site duplex to permit an
CC       effective competition for the 5'-splice site by the U6 snRNA,
CC       resulting in the switch between U1 and U6 at the 5'-splice site.
CC       May also act to unwind the U4/U6 base-pairing interaction in the
CC       U4/U6/U5 snRNP, facilitating the first covalent step of splicing.
CC       {ECO:0000269|PubMed:10024879, ECO:0000269|PubMed:11172727,
CC       ECO:0000269|PubMed:2010088}.
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 U5 snRNP complex, composed of at least
CC       BRR2, PRP8, PRP28, DIB1, LIN1, SMB1, SMD1, SMD2, SMD3, SME1, SMX2,
CC       SMX3, and SNU114, associated with the U5 snRNA.
CC       {ECO:0000269|PubMed:11720284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
DR   EMBL; X56934; CAA40255.1; -; Genomic_DNA.
DR   EMBL; Z49701; CAA89729.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12083.1; -; Genomic_DNA.
DR   PIR; A39624; A39624.
DR   RefSeq; NP_010529.3; NM_001180551.3.
DR   PDB; 4W7S; X-ray; 2.54 A; A/B=127-588.
DR   PDB; 5ZWN; EM; 3.30 A; y=1-588.
DR   PDBsum; 4W7S; -.
DR   PDBsum; 5ZWN; -.
DR   SMR; P23394; -.
DR   BioGrid; 32294; 246.
DR   ComplexPortal; CPX-25; U4/U6.U5 tri-snRNP complex.
DR   ComplexPortal; CPX-29; U5 snRNP.
DR   DIP; DIP-6324N; -.
DR   IntAct; P23394; 19.
DR   MINT; P23394; -.
DR   STRING; 4932.YDR243C; -.
DR   iPTMnet; P23394; -.
DR   MaxQB; P23394; -.
DR   PaxDb; P23394; -.
DR   PRIDE; P23394; -.
DR   EnsemblFungi; YDR243C_mRNA; YDR243C; YDR243C.
DR   GeneID; 851830; -.
DR   KEGG; sce:YDR243C; -.
DR   EuPathDB; FungiDB:YDR243C; -.
DR   SGD; S000002651; PRP28.
DR   HOGENOM; HOG000268796; -.
DR   InParanoid; P23394; -.
DR   KO; K12858; -.
DR   OMA; TEKKFNF; -.
DR   BioCyc; YEAST:G3O-29816-MONOMER; -.
DR   PRO; PR:P23394; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000384; F:first spliceosomal transesterification activity; IMP:SGD.
DR   GO; GO:0003723; F:RNA binding; IDA:SGD.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:SGD.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IMP:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1    588       Pre-mRNA-splicing ATP-dependent RNA
FT                                helicase PRP28.
FT                                /FTId=PRO_0000055127.
FT   DOMAIN      208    399       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      427    579       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     221    228       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       172    202       Q motif.
FT   MOTIF       341    344       DEAD box.
FT   MOD_RES      69     69       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN     221    221       A->V: In PRP28-103; no growth at 15 and
FT                                37 degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     223    223       T->I: In PRP28-117; no growth at 15
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     264    264       R->D,E: Lethal.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     265    265       E->Q: In PRP28-99; no growth at 15 and 37
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     297    297       G->E: In PRP28-1; no growth at 15 degrees
FT                                Celsius. {ECO:0000269|PubMed:2010088}.
FT   MUTAGEN     317    317       T->I: In PRP28-36; slow growth at 30
FT                                degrees Celsius, and no growth at 15 and
FT                                37 degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     317    317       T->Y: Lethal.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     319    319       G->E,V: No growth at 15 and 37 degrees
FT                                Celsius. {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     376    376       M->I: In PRP28-32; no growth at 15
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     379    379       A->W: In PRP28-102; no growth at 25
FT                                degrees Celsius or lower.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     438    438       P->L: In PRP28-61; no growth at 37
FT                                degrees Celsius; when associated with L-
FT                                468 and D-486.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     440    440       I->F: In PRP28-56; no growth at 37
FT                                degrees Celsius; when associated with S-
FT                                546 and E-584.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     442    442       F->G: In PRP28-101; no growth at 15 and
FT                                37 degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     442    442       F->S: In PRP28-55; no growth at 37
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     449    449       A->T: In PRP28-66; no growth at 37
FT                                degrees Celsius; when associated with A-
FT                                541; V-549; N-580 and V-586.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     468    468       H->L: In PRP28-61; no growth at 37
FT                                degrees Celsius; when associated with L-
FT                                438 and D-486.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     486    486       N->D: In PRP28-61; no growth at 37
FT                                degrees Celsius; when associated with L-
FT                                438 and L-468.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     491    491       M->K: In PRP28-52; no growth at 37
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     499    499       R->G: In PRP28-86; lethal.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     499    499       R->K: No growth at 15 degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     502    502       D->N: Lethal.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     521    521       Y->D: In PRP28-37; no growth at 37
FT                                degrees Celsius.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     527    527       R->D: Lethal.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     541    541       V->A: In PRP28-66; no growth at 37
FT                                degrees Celsius; when associated with T-
FT                                449; V-549; N-580 and V-586.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     546    546       D->S: In PRP28-56; no growth at 37
FT                                degrees Celsius; when associated with F-
FT                                440 and E-584.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     549    549       L->V: In PRP28-66; no growth at 37
FT                                degrees Celsius; when associated with T-
FT                                449; A-541; N-580 and V-586.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     580    580       K->N: In PRP28-66; no growth at 37
FT                                degrees Celsius; when associated with T-
FT                                449; A-541; V-549 and V-586.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     584    584       N->E: In PRP28-56; no growth at 37
FT                                degrees Celsius; when associated with F-
FT                                440 and S-546.
FT                                {ECO:0000269|PubMed:9396812}.
FT   MUTAGEN     586    586       I->V: In PRP28-66; no growth at 37
FT                                degrees Celsius; when associated with T-
FT                                449; A-541; V-549 and N-580.
FT                                {ECO:0000269|PubMed:9396812}.
FT   CONFLICT    493    493       A -> R (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
FT   HELIX       138    140       {ECO:0000244|PDB:4W7S}.
FT   HELIX       143    145       {ECO:0000244|PDB:4W7S}.
FT   HELIX       148    157       {ECO:0000244|PDB:4W7S}.
FT   STRAND      160    166       {ECO:0000244|PDB:4W7S}.
FT   STRAND      172    175       {ECO:0000244|PDB:4W7S}.
FT   HELIX       182    190       {ECO:0000244|PDB:4W7S}.
FT   HELIX       199    208       {ECO:0000244|PDB:4W7S}.
FT   STRAND      217    220       {ECO:0000244|PDB:4W7S}.
FT   HELIX       227    240       {ECO:0000244|PDB:4W7S}.
FT   HELIX       247    253       {ECO:0000244|PDB:4W7S}.
FT   STRAND      256    260       {ECO:0000244|PDB:4W7S}.
FT   HELIX       264    283       {ECO:0000244|PDB:4W7S}.
FT   STRAND      284    286       {ECO:0000244|PDB:4W7S}.
FT   STRAND      291    294       {ECO:0000244|PDB:4W7S}.
FT   HELIX       300    307       {ECO:0000244|PDB:4W7S}.
FT   STRAND      312    316       {ECO:0000244|PDB:4W7S}.
FT   HELIX       318    326       {ECO:0000244|PDB:4W7S}.
FT   STRAND      337    340       {ECO:0000244|PDB:4W7S}.
FT   HELIX       343    348       {ECO:0000244|PDB:4W7S}.
FT   HELIX       352    365       {ECO:0000244|PDB:4W7S}.
FT   STRAND      373    380       {ECO:0000244|PDB:4W7S}.
FT   HELIX       383    392       {ECO:0000244|PDB:4W7S}.
FT   STRAND      397    403       {ECO:0000244|PDB:4W7S}.
FT   STRAND      410    417       {ECO:0000244|PDB:4W7S}.
FT   HELIX       421    432       {ECO:0000244|PDB:4W7S}.
FT   STRAND      439    442       {ECO:0000244|PDB:4W7S}.
FT   HELIX       446    459       {ECO:0000244|PDB:4W7S}.
FT   STRAND      464    467       {ECO:0000244|PDB:4W7S}.
FT   HELIX       473    484       {ECO:0000244|PDB:4W7S}.
FT   STRAND      487    493       {ECO:0000244|PDB:4W7S}.
FT   TURN        495    500       {ECO:0000244|PDB:4W7S}.
FT   STRAND      506    513       {ECO:0000244|PDB:4W7S}.
FT   HELIX       518    525       {ECO:0000244|PDB:4W7S}.
FT   STRAND      534    541       {ECO:0000244|PDB:4W7S}.
FT   HELIX       547    559       {ECO:0000244|PDB:4W7S}.
FT   HELIX       570    576       {ECO:0000244|PDB:4W7S}.
SQ   SEQUENCE   588 AA;  66641 MW;  333ADBF9D7C75C99 CRC64;
     MARPIDVSQL IAGINKKKGL DENTSGKISK PRFLNKQERS KQERLKENEE SLTPTQSDSA
     KVEIKKVNSR DDSFFNETND KKRNPSKQNG SKFHFSWNES EDTLSGYDPI VSTRAIDLLW
     KGKTPKNAAE SSYMGKHWTE KSLHEMNERD WRILKEDYAI VTKGGTVENP LRNWEELNII
     PRDLLRVIIQ ELRFPSPTPI QRITIPNVCN MKQYRDFLGV ASTGSGKTLA FVIPILIKMS
     RSPPRPPSLK IIDGPKALIL APTRELVQQI QKETQKVTKI WSKESNYDCK VISIVGGHSL
     EEISFSLSEG CDILVATPGR LIDSLENHLL VMKQVETLVL DEADKMIDLG FEDQVTNILT
     KVDINADSAV NRQTLMFTAT MTPVIEKIAA GYMQKPVYAT IGVETGSEPL IQQVVEYADN
     DEDKFKKLKP IVAKYDPPII IFINYKQTAD WLAEKFQKET NMKVTILHGS KSQEQREHSL
     QLFRTNKVQI MIATNVAARG LDIPNVSLVV NFQISKKMDD YIHRIGRTGR AANEGTAVSF
     VSAAEDESLI RELYKYVRKH DPLNSNIFSE AVKNKYNVGK QLSNEIIY
//
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