Q9VGI8 (BLM_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bloom syndrome protein homolog
Short name=Dmblm
EC=3.6.4.12

Alternative name(s):
Mutagen-sensitive protein 309
RecQ helicase homolog

Gene names

Name:	mus309
Synonyms:	blm
ORF Names:	CG6920

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1487 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction By similarity.
Catalytic activity	ATP + H2O = ADP + phosphate.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the helicase family. RecQ subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HRDC domain.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW DNA strand renaturation Inferred from direct assay PubMed 17272294. Source: FlyBase DNA synthesis involved in DNA repair Inferred from mutant phenotype PubMed 12522255. Source: FlyBase double-strand break repair via synthesis-dependent strand annealing Inferred from mutant phenotype PubMed 15501916PubMed 17507683. Source: FlyBase negative regulation of double-strand break repair via single-strand annealing Inferred from mutant phenotype PubMed 18978019. Source: FlyBase reciprocal meiotic recombination Inferred from mutant phenotype PubMed 17507683. Source: FlyBase strand displacement Inferred from direct assay PubMed 17272294. Source: FlyBase
Cellular_component	nucleus Inferred from direct assay PubMed 17272294. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent 3'-5' DNA helicase activity Inferred from direct assay PubMed 17272294. Source: FlyBase Y-form DNA binding Inferred from direct assay PubMed 17272294. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1487	1487	Bloom syndrome protein homolog		PRO_0000205044
Regions
	Repeat	89 – 112	24	1
	Repeat	115 – 138	24	2
	Domain	746 – 921	176	Helicase ATP-binding
	Domain	944 – 1093	150	Helicase C-terminal
	Domain	1283 – 1363	81	HRDC
	Nucleotide binding	759 – 766	8	ATP By similarity
	Region	89 – 138	50	2 X 24 AA repeats of L-D-L-S-V-S-P-L-A-E-L-[SP]-A-K-K-K-[YS]-[AD]-R-D-[SP]-P-P-K-P
	Motif	865 – 868	4	DEAH box
	Motif	1416 – 1432	17	Nuclear localization signal By similarity
	Compositional bias	225 – 230	6	Poly-Pro
	Compositional bias	464 – 467	4	Poly-Ser
	Compositional bias	1369 – 1372	4	Poly-Glu
Amino acid modifications
	Modified residue	52	1	Phosphoserine Ref.4
	Modified residue	53	1	Phosphoserine Ref.4
	Modified residue	92	1	Phosphoserine Ref.4
	Modified residue	94	1	Phosphoserine Ref.4
	Modified residue	108	1	Phosphoserine Ref.4
	Modified residue	113	1	Phosphothreonine Ref.4
	Modified residue	118	1	Phosphoserine Ref.4
	Modified residue	120	1	Phosphoserine Ref.4
	Modified residue	130	1	Phosphoserine Ref.4
	Modified residue	151	1	Phosphoserine Ref.4
	Modified residue	153	1	Phosphoserine Ref.4
	Modified residue	180	1	Phosphoserine Ref.4
	Modified residue	182	1	Phosphoserine Ref.4
	Modified residue	197	1	Phosphoserine Ref.4
	Modified residue	203	1	Phosphoserine Ref.4
	Modified residue	328	1	Phosphoserine Ref.4
	Modified residue	506	1	Phosphoserine Ref.4
	Modified residue	509	1	Phosphoserine Ref.4
	Modified residue	510	1	Phosphoserine Ref.4
	Modified residue	535	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	98	1	K → E in AAD41441. Ref.1
	Sequence conflict	110	1	K → P in AAD41441. Ref.1
	Sequence conflict	126	1	L → P in AAD41441. Ref.1
	Sequence conflict	134 – 136	3	SPK → PPP in AAD41441. Ref.1
	Sequence conflict	169	1	Q → P in AAD41441. Ref.1
	Sequence conflict	222	1	P → S in AAD41441. Ref.1
	Sequence conflict	299	1	Y → N in AAD41441. Ref.1
	Sequence conflict	417	1	M → V in AAD41441. Ref.1
	Sequence conflict	459	1	Q → R in AAD41441. Ref.1
	Sequence conflict	471	1	S → C in AAD41441. Ref.1
	Sequence conflict	496	1	H → P in AAD41441. Ref.1
	Sequence conflict	594	1	D → G in AAD41441. Ref.1
	Sequence conflict	614	1	G → A in AAD41441. Ref.1
	Sequence conflict	805	1	K → E in AAD41441. Ref.1
	Sequence conflict	1116	1	E → G in AAD41441. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VGI8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 07361B8005E29432	FASTA	1,487	166,079
	10 20 30 40 50 60 MSKKPVAQRK QLTLSSFIGL DGNSQSQPKS RAASVRSKPP AVYNPIFLDA SSSDDETTEI 70 80 90 100 110 120 SSQSNNGTIA TKKSSRDPRT AKLKKHTYLD LSVSPLAKLS AKKYARDSPK KPTSLDLSVS 130 140 150 160 170 180 PLAELLAKKS DRDSPKKPVQ NENSYTYRGL SESPVENKSI GDTLRKPPQK ERKTSIVWLS 190 200 210 220 230 240 DSPEKKVTQN ERKILDSPLQ RFSFEDFPNK ENGNRHHLLT LPDSPPPPQP VKKPEKTMWQ 250 260 270 280 290 300 NETKTIQDKD SPANPLVSNN LASISTLLDS SRAPNTYKGS SRNLFEDSPE KSGSGEQGYK 310 320 330 340 350 360 LGSAKENEIP TKPATASLER NSVTSSPSPA APLKPRYSVA FDNSLADYLK DLAQNDNFSI 370 380 390 400 410 420 DPNKQNTETL KSTLGFFRNT YVELMEKYCS LIDQIPAMHF NEIAGFQPNT FLKLKVMRQK 430 440 450 460 470 480 FKARTQLVQN SLDKKESQLK AEQEALEKEE IEMQAEQAQQ TVLSSSSPEK SRPIMPLPKV 490 500 510 520 530 540 QEIKDEKIPN RNQLIHDLCG EPDNFSPPSS PRDTQLIPKR QQLINDLCGE PDDFSPPSKQ 550 560 570 580 590 600 NDPHLLRKCE ELVHDLCEEP DDYLAQSMML DGDLEEEQLN GPTQGTTTSG MDDDEDDLEG 610 620 630 640 650 660 LLAEIEDEHQ KMQGRRSEFN GYSYKELEAV KVKEKHKETP INISLDDDGF PEYDEAMFEQ 670 680 690 700 710 720 MHSQAAANKS RVSSAGPSTS KSVVPTKQTS ALHSQKLSGN FHANVHNDGI TGEFDGQKFE 730 740 750 760 770 780 HSTRLMHGLS YSFGLKSFRP NQLQVINATL LGNDCFVLMP TGGGKSLCYQ LPAILTEGVT 790 800 810 820 830 840 IVISPLKSLI FDQINKLASL DICAKSLSGE QKMADVMAIY RDLESQPPMV KLLYVTPEKI 850 860 870 880 890 900 SSSARFQDTL DTLNSNNYIS RFVIDEAHCV SQWGHDFRPD YKKLGVLKKR FPNVPTIALT 910 920 930 940 950 960 ATATPRVRLD ILAQLNLKNC KWFLSSFNRS NLRYRVLPKK GVSTLDDISR YIRSKPQHFS 970 980 990 1000 1010 1020 GIIYCLSRKE CDETSKKMCK DGVRAVSYHA GLTDTDRESR QKDWLTGKMR VICATVAFGM 1030 1040 1050 1060 1070 1080 GIDKPDVRFV LHYSLPKSIE GYYQEAGRAG RDGDVADCIL YYNYSDMLRI KKMLDSDKAL 1090 1100 1110 1120 1130 1140 QYNVKKIHVD NLYRIVGYCE NLTDCRRAQQ LDYFGEHFTS EQCLENRETA CDNCINKRAY 1150 1160 1170 1180 1190 1200 KAVDALEHAR KAARAVKDLC SGRSRFTLLH IADVLKGSKI KKIIDFNHHK TPHHGVLKDW 1210 1220 1230 1240 1250 1260 DKNDVHRLLR KMVIDGFLRE DLIFTNDFPQ AYLYLGNNIS KLMEGTPNFE FAVTKNAKEA 1270 1280 1290 1300 1310 1320 KAAVGSVSDG ATSSTADGQS GMREIHERCY TDLLDLCRTI ASQRNVTMAS IMNIQALKSM 1330 1340 1350 1360 1370 1380 AETLPITEKD MCSIPHVTKA NFDKYGAKLL EITSNYASEK LLMQAVLDEE EEQAAAKQRP 1390 1400 1410 1420 1430 1440 STSGWNNESV DWDMAVASQG NANTSGASGF NSFRAGKRKK IYKSGASKRY KTSTTSPAAR 1450 1460 1470 1480 KTTSARGRGG RAGAKRAESS ASSASGWKSK KTGNSFGFDL MPLPGSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolution of the RECQ family of helicases: a Drosophila homolog, Dmblm, is similar to the human Bloom syndrome gene." Kusano K., Berres M.E., Engels W.R. Genetics 151:1027-1039(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], REPEATS. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-92; SER-94; SER-108; THR-113; SER-118; SER-120; SER-130; SER-151; SER-153; SER-180; SER-182; SER-197; SER-203; SER-328; SER-506; SER-509; SER-510 AND SER-535, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U92536 mRNA. Translation: AAD41441.1. AE014297 Genomic DNA. Translation: AAF54691.1.
RefSeq	NP_524319.2. NM_079595.3.
UniGene	Dm.2444.
3D structure databases
ProteinModelPortal	Q9VGI8.
SMR	Q9VGI8. Positions 714-1256.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-23386N.
MINT	MINT-784091.
STRING	7227.FBpp0081910.
Proteomic databases
PaxDb	Q9VGI8.
PRIDE	Q9VGI8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082434; FBpp0081910; FBgn0002906.
GeneID	41366.
KEGG	dme:Dmel_CG6920.
Organism-specific databases
CTD	641.
FlyBase	FBgn0002906. mus309.
Phylogenomic databases
eggNOG	COG0514.
GeneTree	ENSGT00550000074520.
InParanoid	Q9VGI8.
KO	K10901.
OMA	KISSSAR.
OrthoDB	EOG4JDFNV.
PhylomeDB	Q9VGI8.
Gene expression databases
Bgee	Q9VGI8.
GermOnline	CG6920. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 1.10.150.80. 1 hit.
InterPro	IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR004589. DNA_helicase_ATP-dep_RecQ. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR010997. HRDC-like. IPR002121. HRDC_dom. IPR027417. P-loop_NTPase. IPR018982. RQC_domain. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. PF00570. HRDC. 1 hit. PF09382. RQC. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. SM00956. RQC. 1 hit. [Graphical view]
SUPFAM	SSF47819. HRDC_like. 1 hit. SSF52540. SSF52540. 2 hits.
TIGRFAMs	TIGR00614. recQ_fam. 1 hit.
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS50967. HRDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	BLM. drosophila.
GenomeRNAi	41366.
NextBio	823498.

Entry information

Entry name

BLM_DROME

Accession

Primary (citable) accession number: Q9VGI8
Secondary accession number(s): Q9Y062

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project