GenomeNet

Database: UniProt
Entry: Q9VGI8
LinkDB: Q9VGI8
Original site: Q9VGI8 
ID   BLM_DROME               Reviewed;        1487 AA.
AC   Q9VGI8; Q9Y062;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-NOV-2019, entry version 160.
DE   RecName: Full=Bloom syndrome protein homolog;
DE            Short=Dmblm;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
DE   AltName: Full=Bloom syndrome helicase ortholog;
DE   AltName: Full=Mutagen-sensitive protein 309;
DE   AltName: Full=RecQ helicase homolog;
GN   Name=Blm; Synonyms=mus309; ORFNames=CG6920;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND REPEATS.
RC   STRAIN=Canton-S;
RX   PubMed=10049920;
RA   Kusano K., Berres M.E., Engels W.R.;
RT   "Evolution of the RECQ family of helicases: a Drosophila homolog,
RT   Dmblm, is similar to the human Bloom syndrome gene.";
RL   Genetics 151:1027-1039(1999).
RN   [2]
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   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   [3]
RP   GENOME REANNOTATION.
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-92;
RP   SER-94; SER-108; THR-113; SER-118; SER-120; SER-130; SER-151; SER-153;
RP   SER-180; SER-182; SER-197; SER-203; SER-328; SER-506; SER-509; SER-510
RP   AND SER-535, 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).
CC   -!- FUNCTION: Participates in DNA replication and repair. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that
CC       unwinds single- and double-stranded DNA in a 3'-5' direction (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and
CC       double-stranded DNA in a 3'-5' direction. Participates in DNA
CC       replication and repair. Negatively regulates sister chromatid
CC       exchange (SCE). Stimulates DNA 4-way junction branch migration and
CC       DNA Holliday junction dissolution. Binds single-stranded DNA
CC       (ssDNA), forked duplex DNA and DNA Holliday junction.
CC       {ECO:0000250|UniProtKB:P54132}.
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=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:P54132};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P54132};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P54132};
CC   -!- SUBUNIT: Monomer. Homodimer (via N-terminus). Homotetramer (via N-
CC       terminus); dimer of dimers. Homohexamer (via N-terminus). Self-
CC       association negatively regulates DNA unwinding amplitude and rate.
CC       Oligomer forms dissociate into monomer in presence of ATP.
CC       {ECO:0000250|UniProtKB:P54132}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region mediates dimerization and
CC       homooligomerization. Both the helicase ATP-binding domain and the
CC       helicase C-terminal domain form intramolecular interactions with
CC       the HRDC domain in a ATP-dependent manner. The HRDC domain is
CC       required for single-stranded DNA (ssDNA) and DNA Holliday junction
CC       binding. {ECO:0000250|UniProtKB:P54132}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000305}.
DR   EMBL; U92536; AAD41441.1; -; mRNA.
DR   EMBL; AE014297; AAF54691.1; -; Genomic_DNA.
DR   RefSeq; NP_524319.2; NM_079595.3.
DR   SMR; Q9VGI8; -.
DR   BioGrid; 66499; 20.
DR   DIP; DIP-23386N; -.
DR   IntAct; Q9VGI8; 7.
DR   MINT; Q9VGI8; -.
DR   STRING; 7227.FBpp0081910; -.
DR   iPTMnet; Q9VGI8; -.
DR   PaxDb; Q9VGI8; -.
DR   PRIDE; Q9VGI8; -.
DR   EnsemblMetazoa; FBtr0082434; FBpp0081910; FBgn0002906.
DR   GeneID; 41366; -.
DR   KEGG; dme:Dmel_CG6920; -.
DR   CTD; 641; -.
DR   FlyBase; FBgn0002906; Blm.
DR   eggNOG; KOG0351; Eukaryota.
DR   eggNOG; COG0514; LUCA.
DR   GeneTree; ENSGT00940000156800; -.
DR   InParanoid; Q9VGI8; -.
DR   KO; K10901; -.
DR   OMA; RIVGYCE; -.
DR   OrthoDB; 445763at2759; -.
DR   PhylomeDB; Q9VGI8; -.
DR   Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR   GenomeRNAi; 41366; -.
DR   PRO; PR:Q9VGI8; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002906; Expressed in 10 organ(s), highest expression level in testis.
DR   Genevisible; Q9VGI8; DM.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:FlyBase.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:FlyBase.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; ISS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000403; F:Y-form DNA binding; IDA:FlyBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:FlyBase.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IMP:FlyBase.
DR   GO; GO:0000733; P:DNA strand renaturation; IDA:FlyBase.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; IMP:FlyBase.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR   GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:FlyBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IGI:FlyBase.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:FlyBase.
DR   GO; GO:1901291; P:negative regulation of double-strand break repair via single-strand annealing; IMP:FlyBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:FlyBase.
DR   GO; GO:0000732; P:strand displacement; IDA:FlyBase.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; SSF47819; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN         1   1487       Bloom syndrome protein homolog.
FT                                /FTId=PRO_0000205044.
FT   REPEAT       89    112       1. {ECO:0000269|PubMed:10049920}.
FT   REPEAT      115    138       2. {ECO:0000269|PubMed:10049920}.
FT   DOMAIN      746    921       Helicase ATP-binding.
FT                                {ECO:0000250|UniProtKB:P54132,
FT                                ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      944   1093       Helicase C-terminal.
FT                                {ECO:0000250|UniProtKB:P54132,
FT                                ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1283   1363       HRDC. {ECO:0000250|UniProtKB:P54132,
FT                                ECO:0000255|PROSITE-ProRule:PRU00328}.
FT   NP_BIND     738    742       ATP. {ECO:0000250|UniProtKB:P54132}.
FT   NP_BIND     762    766       ATP. {ECO:0000250|UniProtKB:P54132}.
FT   REGION       89    138       2 X 24 AA repeats of L-D-L-S-V-S-P-L-A-E-
FT                                L-[SP]-A-K-K-K-[YS]-[AD]-R-D-[SP]-P-P-K-
FT                                P.
FT   REGION      967    969       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   REGION     1069   1072       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   REGION     1167   1169       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   REGION     1178   1182       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   MOTIF       865    868       DEAH box.
FT   MOTIF      1416   1432       Nuclear localization signal.
FT                                {ECO:0000250}.
FT   COMPBIAS    225    230       Poly-Pro.
FT   COMPBIAS    464    467       Poly-Ser.
FT   COMPBIAS   1369   1372       Poly-Glu.
FT   METAL      1105   1105       Zinc. {ECO:0000250|UniProtKB:P54132}.
FT   METAL      1123   1123       Zinc. {ECO:0000250|UniProtKB:P54132}.
FT   METAL      1131   1131       Zinc. {ECO:0000250|UniProtKB:P54132}.
FT   METAL      1134   1134       Zinc. {ECO:0000250|UniProtKB:P54132}.
FT   BINDING    1051   1051       ATP. {ECO:0000250|UniProtKB:P54132}.
FT   BINDING    1313   1313       ATP. {ECO:0000250|UniProtKB:P54132}.
FT   SITE        878    878       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   SITE        990    990       3' overhang DNA-binding; via amide
FT                                nitrogen. {ECO:0000250|UniProtKB:P54132}.
FT   SITE       1015   1015       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   SITE       1037   1037       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   SITE       1167   1167       3' overhang DNA-binding.
FT                                {ECO:0000250|UniProtKB:P54132}.
FT   MOD_RES      52     52       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      53     53       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      92     92       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES      94     94       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     113    113       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     120    120       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     151    151       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     153    153       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     180    180       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     182    182       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     197    197       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     203    203       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     328    328       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     506    506       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     509    509       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     510    510       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     535    535       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   CONFLICT     98     98       K -> E (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    110    110       K -> P (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    126    126       L -> P (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    134    136       SPK -> PPP (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    169    169       Q -> P (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       P -> S (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    299    299       Y -> N (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    417    417       M -> V (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    459    459       Q -> R (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    471    471       S -> C (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    496    496       H -> P (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    594    594       D -> G (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    614    614       G -> A (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT    805    805       K -> E (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
FT   CONFLICT   1116   1116       E -> G (in Ref. 1; AAD41441).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1487 AA;  166079 MW;  07361B8005E29432 CRC64;
     MSKKPVAQRK QLTLSSFIGL DGNSQSQPKS RAASVRSKPP AVYNPIFLDA SSSDDETTEI
     SSQSNNGTIA TKKSSRDPRT AKLKKHTYLD LSVSPLAKLS AKKYARDSPK KPTSLDLSVS
     PLAELLAKKS DRDSPKKPVQ NENSYTYRGL SESPVENKSI GDTLRKPPQK ERKTSIVWLS
     DSPEKKVTQN ERKILDSPLQ RFSFEDFPNK ENGNRHHLLT LPDSPPPPQP VKKPEKTMWQ
     NETKTIQDKD SPANPLVSNN LASISTLLDS SRAPNTYKGS SRNLFEDSPE KSGSGEQGYK
     LGSAKENEIP TKPATASLER NSVTSSPSPA APLKPRYSVA FDNSLADYLK DLAQNDNFSI
     DPNKQNTETL KSTLGFFRNT YVELMEKYCS LIDQIPAMHF NEIAGFQPNT FLKLKVMRQK
     FKARTQLVQN SLDKKESQLK AEQEALEKEE IEMQAEQAQQ TVLSSSSPEK SRPIMPLPKV
     QEIKDEKIPN RNQLIHDLCG EPDNFSPPSS PRDTQLIPKR QQLINDLCGE PDDFSPPSKQ
     NDPHLLRKCE ELVHDLCEEP DDYLAQSMML DGDLEEEQLN GPTQGTTTSG MDDDEDDLEG
     LLAEIEDEHQ KMQGRRSEFN GYSYKELEAV KVKEKHKETP INISLDDDGF PEYDEAMFEQ
     MHSQAAANKS RVSSAGPSTS KSVVPTKQTS ALHSQKLSGN FHANVHNDGI TGEFDGQKFE
     HSTRLMHGLS YSFGLKSFRP NQLQVINATL LGNDCFVLMP TGGGKSLCYQ LPAILTEGVT
     IVISPLKSLI FDQINKLASL DICAKSLSGE QKMADVMAIY RDLESQPPMV KLLYVTPEKI
     SSSARFQDTL DTLNSNNYIS RFVIDEAHCV SQWGHDFRPD YKKLGVLKKR FPNVPTIALT
     ATATPRVRLD ILAQLNLKNC KWFLSSFNRS NLRYRVLPKK GVSTLDDISR YIRSKPQHFS
     GIIYCLSRKE CDETSKKMCK DGVRAVSYHA GLTDTDRESR QKDWLTGKMR VICATVAFGM
     GIDKPDVRFV LHYSLPKSIE GYYQEAGRAG RDGDVADCIL YYNYSDMLRI KKMLDSDKAL
     QYNVKKIHVD NLYRIVGYCE NLTDCRRAQQ LDYFGEHFTS EQCLENRETA CDNCINKRAY
     KAVDALEHAR KAARAVKDLC SGRSRFTLLH IADVLKGSKI KKIIDFNHHK TPHHGVLKDW
     DKNDVHRLLR KMVIDGFLRE DLIFTNDFPQ AYLYLGNNIS KLMEGTPNFE FAVTKNAKEA
     KAAVGSVSDG ATSSTADGQS GMREIHERCY TDLLDLCRTI ASQRNVTMAS IMNIQALKSM
     AETLPITEKD MCSIPHVTKA NFDKYGAKLL EITSNYASEK LLMQAVLDEE EEQAAAKQRP
     STSGWNNESV DWDMAVASQG NANTSGASGF NSFRAGKRKK IYKSGASKRY KTSTTSPAAR
     KTTSARGRGG RAGAKRAESS ASSASGWKSK KTGNSFGFDL MPLPGSK
//
DBGET integrated database retrieval system