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Protein

Bloom syndrome protein homolog

Gene

Blm

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity
ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei8783' overhang DNA-bindingBy similarity1
Sitei9903' overhang DNA-binding; via amide nitrogenBy similarity1
Sitei10153' overhang DNA-bindingBy similarity1
Sitei10373' overhang DNA-bindingBy similarity1
Binding sitei1051ATPBy similarity1
Metal bindingi1105ZincBy similarity1
Metal bindingi1123ZincBy similarity1
Metal bindingi1131ZincBy similarity1
Metal bindingi1134ZincBy similarity1
Sitei11673' overhang DNA-bindingBy similarity1
Binding sitei1313ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi738 – 742ATPBy similarity5
Nucleotide bindingi762 – 766ATPBy similarity5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 3'-5' DNA helicase activity Source: FlyBase
  • ATP-dependent DNA helicase activity Source: FlyBase
  • DNA-dependent ATPase activity Source: FlyBase
  • DNA helicase activity Source: FlyBase
  • four-way junction helicase activity Source: GO_Central
  • helicase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • Y-form DNA binding Source: FlyBase

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • DNA duplex unwinding Source: FlyBase
  • DNA repair Source: FlyBase
  • DNA replication Source: UniProtKB-KW
  • DNA strand renaturation Source: FlyBase
  • DNA synthesis involved in DNA repair Source: FlyBase
  • double-strand break repair Source: FlyBase
  • double-strand break repair involved in meiotic recombination Source: FlyBase
  • double-strand break repair via homologous recombination Source: FlyBase
  • double-strand break repair via nonhomologous end joining Source: FlyBase
  • double-strand break repair via synthesis-dependent strand annealing Source: FlyBase
  • negative regulation of double-strand break repair via single-strand annealing Source: FlyBase
  • reciprocal meiotic recombination Source: FlyBase
  • strand displacement Source: FlyBase

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-3108214. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Bloom syndrome protein homolog (EC:3.6.4.12By similarity)
Short name:
Dmblm
Alternative name(s):
Bloom syndrome helicase ortholog
Mutagen-sensitive protein 309
RecQ helicase homolog
Gene namesi
Name:Blm
Synonyms:mus309
ORF Names:CG6920
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002906. Blm.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050441 – 1487Bloom syndrome protein homologAdd BLAST1487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52Phosphoserine1 Publication1
Modified residuei53Phosphoserine1 Publication1
Modified residuei92Phosphoserine1 Publication1
Modified residuei94Phosphoserine1 Publication1
Modified residuei108Phosphoserine1 Publication1
Modified residuei113Phosphothreonine1 Publication1
Modified residuei118Phosphoserine1 Publication1
Modified residuei120Phosphoserine1 Publication1
Modified residuei130Phosphoserine1 Publication1
Modified residuei151Phosphoserine1 Publication1
Modified residuei153Phosphoserine1 Publication1
Modified residuei180Phosphoserine1 Publication1
Modified residuei182Phosphoserine1 Publication1
Modified residuei197Phosphoserine1 Publication1
Modified residuei203Phosphoserine1 Publication1
Modified residuei328Phosphoserine1 Publication1
Modified residuei506Phosphoserine1 Publication1
Modified residuei509Phosphoserine1 Publication1
Modified residuei510Phosphoserine1 Publication1
Modified residuei535Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VGI8.
PRIDEiQ9VGI8.

PTM databases

iPTMnetiQ9VGI8.

Expressioni

Gene expression databases

BgeeiFBgn0002906.
ExpressionAtlasiQ9VGI8. differential.
GenevisibleiQ9VGI8. DM.

Interactioni

Subunit structurei

Monomer. Homodimer (via N-terminus). Homotetramer (via N-terminus); dimer of dimers. Homohexamer (via N-terminus). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomer forms dissociate into monomer in presence of ATP.By similarity

Protein-protein interaction databases

BioGridi66499. 19 interactors.
DIPiDIP-23386N.
IntActiQ9VGI8. 7 interactors.
MINTiMINT-784091.
STRINGi7227.FBpp0081910.

Structurei

3D structure databases

ProteinModelPortaliQ9VGI8.
SMRiQ9VGI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati89 – 11211 PublicationAdd BLAST24
Repeati115 – 13821 PublicationAdd BLAST24
Domaini746 – 921Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST176
Domaini944 – 1093Helicase C-terminalPROSITE-ProRule annotationBy similarityAdd BLAST150
Domaini1283 – 1363HRDCPROSITE-ProRule annotationBy similarityAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni89 – 1382 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-PAdd BLAST50
Regioni967 – 9693' overhang DNA-bindingBy similarity3
Regioni1069 – 10723' overhang DNA-bindingBy similarity4
Regioni1167 – 11693' overhang DNA-bindingBy similarity3
Regioni1178 – 11823' overhang DNA-bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi865 – 868DEAH box4
Motifi1416 – 1432Nuclear localization signalBy similarityAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi225 – 230Poly-Pro6
Compositional biasi464 – 467Poly-Ser4
Compositional biasi1369 – 1372Poly-Glu4

Domaini

The N-terminal region mediates dimerization and homooligomerization. Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner. The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding.By similarity

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
InParanoidiQ9VGI8.
KOiK10901.
OMAiCKWFLSS.
OrthoDBiEOG091G021X.
PhylomeDBiQ9VGI8.

Family and domain databases

CDDicd00079. HELICc. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR010997. HRDC-like_sf.
IPR002121. HRDC_dom.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR036388. WH-like_DNA-bd_sf.
PfamiView protein in Pfam
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
SUPFAMiSSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 4 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiView protein in PROSITE
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VGI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPVAQRK QLTLSSFIGL DGNSQSQPKS RAASVRSKPP AVYNPIFLDA
60 70 80 90 100
SSSDDETTEI SSQSNNGTIA TKKSSRDPRT AKLKKHTYLD LSVSPLAKLS
110 120 130 140 150
AKKYARDSPK KPTSLDLSVS PLAELLAKKS DRDSPKKPVQ NENSYTYRGL
160 170 180 190 200
SESPVENKSI GDTLRKPPQK ERKTSIVWLS DSPEKKVTQN ERKILDSPLQ
210 220 230 240 250
RFSFEDFPNK ENGNRHHLLT LPDSPPPPQP VKKPEKTMWQ NETKTIQDKD
260 270 280 290 300
SPANPLVSNN LASISTLLDS SRAPNTYKGS SRNLFEDSPE KSGSGEQGYK
310 320 330 340 350
LGSAKENEIP TKPATASLER NSVTSSPSPA APLKPRYSVA FDNSLADYLK
360 370 380 390 400
DLAQNDNFSI DPNKQNTETL KSTLGFFRNT YVELMEKYCS LIDQIPAMHF
410 420 430 440 450
NEIAGFQPNT FLKLKVMRQK FKARTQLVQN SLDKKESQLK AEQEALEKEE
460 470 480 490 500
IEMQAEQAQQ TVLSSSSPEK SRPIMPLPKV QEIKDEKIPN RNQLIHDLCG
510 520 530 540 550
EPDNFSPPSS PRDTQLIPKR QQLINDLCGE PDDFSPPSKQ NDPHLLRKCE
560 570 580 590 600
ELVHDLCEEP DDYLAQSMML DGDLEEEQLN GPTQGTTTSG MDDDEDDLEG
610 620 630 640 650
LLAEIEDEHQ KMQGRRSEFN GYSYKELEAV KVKEKHKETP INISLDDDGF
660 670 680 690 700
PEYDEAMFEQ MHSQAAANKS RVSSAGPSTS KSVVPTKQTS ALHSQKLSGN
710 720 730 740 750
FHANVHNDGI TGEFDGQKFE HSTRLMHGLS YSFGLKSFRP NQLQVINATL
760 770 780 790 800
LGNDCFVLMP TGGGKSLCYQ LPAILTEGVT IVISPLKSLI FDQINKLASL
810 820 830 840 850
DICAKSLSGE QKMADVMAIY RDLESQPPMV KLLYVTPEKI SSSARFQDTL
860 870 880 890 900
DTLNSNNYIS RFVIDEAHCV SQWGHDFRPD YKKLGVLKKR FPNVPTIALT
910 920 930 940 950
ATATPRVRLD ILAQLNLKNC KWFLSSFNRS NLRYRVLPKK GVSTLDDISR
960 970 980 990 1000
YIRSKPQHFS GIIYCLSRKE CDETSKKMCK DGVRAVSYHA GLTDTDRESR
1010 1020 1030 1040 1050
QKDWLTGKMR VICATVAFGM GIDKPDVRFV LHYSLPKSIE GYYQEAGRAG
1060 1070 1080 1090 1100
RDGDVADCIL YYNYSDMLRI KKMLDSDKAL QYNVKKIHVD NLYRIVGYCE
1110 1120 1130 1140 1150
NLTDCRRAQQ LDYFGEHFTS EQCLENRETA CDNCINKRAY KAVDALEHAR
1160 1170 1180 1190 1200
KAARAVKDLC SGRSRFTLLH IADVLKGSKI KKIIDFNHHK TPHHGVLKDW
1210 1220 1230 1240 1250
DKNDVHRLLR KMVIDGFLRE DLIFTNDFPQ AYLYLGNNIS KLMEGTPNFE
1260 1270 1280 1290 1300
FAVTKNAKEA KAAVGSVSDG ATSSTADGQS GMREIHERCY TDLLDLCRTI
1310 1320 1330 1340 1350
ASQRNVTMAS IMNIQALKSM AETLPITEKD MCSIPHVTKA NFDKYGAKLL
1360 1370 1380 1390 1400
EITSNYASEK LLMQAVLDEE EEQAAAKQRP STSGWNNESV DWDMAVASQG
1410 1420 1430 1440 1450
NANTSGASGF NSFRAGKRKK IYKSGASKRY KTSTTSPAAR KTTSARGRGG
1460 1470 1480
RAGAKRAESS ASSASGWKSK KTGNSFGFDL MPLPGSK
Length:1,487
Mass (Da):166,079
Last modified:May 1, 2000 - v1
Checksum:i07361B8005E29432
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti98K → E in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti110K → P in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti126L → P in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti134 – 136SPK → PPP in AAD41441 (PubMed:10049920).Curated3
Sequence conflicti169Q → P in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti222P → S in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti299Y → N in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti417M → V in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti459Q → R in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti471S → C in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti496H → P in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti594D → G in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti614G → A in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti805K → E in AAD41441 (PubMed:10049920).Curated1
Sequence conflicti1116E → G in AAD41441 (PubMed:10049920).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92536 mRNA. Translation: AAD41441.1.
AE014297 Genomic DNA. Translation: AAF54691.1.
RefSeqiNP_524319.2. NM_079595.3.
UniGeneiDm.2444.

Genome annotation databases

EnsemblMetazoaiFBtr0082434; FBpp0081910; FBgn0002906.
GeneIDi41366.
KEGGidme:Dmel_CG6920.

Similar proteinsi

Entry informationi

Entry nameiBLM_DROME
AccessioniPrimary (citable) accession number: Q9VGI8
Secondary accession number(s): Q9Y062
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 2000
Last modified: November 22, 2017
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families