BLM_DROME
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 03-AUG-2022, entry version 170.
DE RecName: Full=RecQ-like DNA helicase Blm {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
DE AltName: Full=Bloom syndrome helicase ortholog;
DE AltName: Full=Bloom syndrome protein homolog;
DE Short=Dmblm;
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND REPEATS.
RC STRAIN=Canton-S;
RX PubMed=10049920; DOI=10.1093/genetics/151.3.1027;
RA Kusano K., Berres M.E., Engels W.R.;
RT "Evolution of the RECQ family of helicases: a Drosophila homolog, Dmblm, is
RT 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., 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 [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., 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-92; SER-94;
RP SER-108; THR-113; SER-118; SER-120; SER-130; SER-151; SER-153; SER-180;
RP SER-182; SER-197; SER-203; SER-328; SER-506; SER-509; SER-510 AND SER-535,
RP 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 unwinds
CC single- and double-stranded DNA in a 3'-5' direction (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-
CC stranded DNA in a 3'-5' direction. Participates in DNA replication and
CC repair. Negatively regulates sister chromatid exchange (SCE).
CC Stimulates DNA 4-way junction branch migration and DNA Holliday
CC junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex
CC DNA and DNA Holliday junction. {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 the
CC HRDC domain in a ATP-dependent manner. The HRDC domain is required for
CC single-stranded DNA (ssDNA) and DNA Holliday junction binding.
CC {ECO:0000250|UniProtKB:P54132}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; U92536; AAD41441.1; -; mRNA.
DR EMBL; AE014297; AAF54691.1; -; Genomic_DNA.
DR RefSeq; NP_524319.2; NM_079595.3.
DR AlphaFoldDB; Q9VGI8; -.
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 VEuPathDB; VectorBase:FBgn0002906; -.
DR eggNOG; KOG0351; Eukaryota.
DR GeneTree; ENSGT00940000156800; -.
DR HOGENOM; CLU_004162_0_0_1; -.
DR InParanoid; Q9VGI8; -.
DR OMA; KVMRQKF; -.
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 SignaLink; Q9VGI8; -.
DR BioGRID-ORCS; 41366; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41366; -.
DR PRO; PR:Q9VGI8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002906; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; Q9VGI8; baseline and differential.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; ISS:FlyBase.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:FlyBase.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
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: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 Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR044876; HRDC_dom_sf.
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; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1487
FT /note="RecQ-like DNA helicase Blm"
FT /id="PRO_0000205044"
FT REPEAT 89..112
FT /note="1"
FT /evidence="ECO:0000269|PubMed:10049920"
FT REPEAT 115..138
FT /note="2"
FT /evidence="ECO:0000269|PubMed:10049920"
FT DOMAIN 746..921
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 944..1093
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1283..1363
FT /note="HRDC"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 17..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..138
FT /note="2 X 24 AA repeats of L-D-L-S-V-S-P-L-A-E-L-[SP]-A-K-
FT K-K-[YS]-[AD]-R-D-[SP]-P-P-K-P"
FT REGION 126..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..969
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1069..1072
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1167..1169
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1178..1182
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1424..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 865..868
FT /note="DEAH box"
FT MOTIF 1416..1432
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 738..742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 762..766
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1051
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 878
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 990
FT /note="3' overhang DNA-binding; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 1015
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 1037
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 1167
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 98
FT /note="K -> E (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="K -> P (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> P (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..136
FT /note="SPK -> PPP (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="Q -> P (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="P -> S (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="Y -> N (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="M -> V (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="Q -> R (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="S -> C (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="H -> P (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="D -> G (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="G -> A (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="K -> E (in Ref. 1; AAD41441)"
FT /evidence="ECO:0000305"
FT CONFLICT 1116
FT /note="E -> G (in Ref. 1; AAD41441)"
FT /evidence="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
