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Protein

Bloom syndrome protein homolog

Gene

BLM

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:28228481). Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair (By similarity). Negatively regulates sister chromatid exchange (SCE) (By similarity). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (By similarity). Binds DNA (PubMed:28228481). Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity).By similarity1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4883' overhang DNA-bindingBy similarity1
Sitei5793' overhang DNA-bindingBy similarity1
Sitei6913' overhang DNA-binding; via amide nitrogenBy similarity1
Sitei7173' overhang DNA-bindingBy similarity1
Sitei7393' overhang DNA-bindingBy similarity1
Binding sitei753ATPBy similarity1
Metal bindingi807ZincBy similarity1
Metal bindingi826ZincBy similarity1
Metal bindingi834ZincBy similarity1
Metal bindingi837ZincBy similarity1
Sitei8813' overhang DNA-bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi439 – 443ATPBy similarity5
Nucleotide bindingi463 – 467ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

  • DNA double-strand break processing Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
  • DNA replication Source: UniProtKB-KW
  • double-strand break repair via homologous recombination Source: GO_Central
  • protein complex oligomerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • regulation of DNA-dependent DNA replication Source: UniProtKB

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Bloom syndrome protein homolog (EC:3.6.4.121 Publication)
Alternative name(s):
RecQ helicase homolog
Gene namesi
Name:BLM
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

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_00002050411 – 1183Bloom syndrome protein homologAdd BLAST1183

Proteomic databases

PaxDbiQ9I920
PRIDEiQ9I920

Interactioni

Subunit structurei

Monomer (PubMed:28228481). Homodimer (via N-terminus) (PubMed:28228481). Homotetramer (via N-terminus); dimer of dimers (PubMed:28228481). Homohexamer (via N-terminus) (PubMed:28228481). Self-association negatively regulates DNA unwinding amplitude and rate (PubMed:28228481). Oligomer complexes dissociate into monomer in presence of ATP (PubMed:28228481).1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9031.ENSGALP00000013422

Structurei

Secondary structure

11183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi115 – 132Combined sources18
Helixi136 – 141Combined sources6
Helixi145 – 161Combined sources17

3D structure databases

ProteinModelPortaliQ9I920
SMRiQ9I920
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini447 – 622Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST176
Domaini648 – 795Helicase C-terminalPROSITE-ProRule annotationBy similarityAdd BLAST148
Domaini983 – 1063HRDCPROSITE-ProRule annotationBy similarityAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 162Necessary for dimerization and homooligomerization1 PublicationAdd BLAST53
Regioni641 – 6443' overhang DNA-bindingBy similarity4
Regioni668 – 6703' overhang DNA-bindingBy similarity3
Regioni771 – 7743' overhang DNA-bindingBy similarity4
Regioni865 – 910DNA Holliday junction bindingBy similarityAdd BLAST46
Regioni881 – 8833' overhang DNA-bindingBy similarity3
Regioni892 – 8963' overhang DNA-bindingBy similarity5
Regioni931 – 9373' overhang DNA-bindingBy similarity7
Regioni998 – 1015Necessary for ssDNA and DNA Holliday junction bindingBy similarityAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi566 – 569DEAH box4
Motifi1104 – 1120Nuclear localization signalBy similarityAdd BLAST17

Domaini

The N-terminal region mediates dimerization and homooligomerization (PubMed:28228481). Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner (By similarity). The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding (By similarity).By similarity1 Publication

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated

Phylogenomic databases

eggNOGiKOG0351 Eukaryota
COG0514 LUCA
HOGENOMiHOG000095239
HOVERGENiHBG004850
InParanoidiQ9I920
KOiK10901

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR012532 BDHCT
IPR032437 BLM_N
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
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF08072 BDHCT, 1 hit
PF16202 BLM_N, 1 hit
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
SUPFAMiSSF46785 SSF46785, 1 hit
SSF47819 SSF47819, 1 hit
SSF52540 SSF52540, 3 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.

Q9I920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEARAATNG GSGESQKLSN GEKSSQLEPG DVGNELLADI ELEEDDYLDV
60 70 80 90 100
VPPSPEEELP SFSPSVRNVS NIFKESPTDG RSAVHGTESE PELMAPKQPA
110 120 130 140 150
AEQDSSAEHA DKGLHLEQQL YSVMEDICKL VDAIPLHELT SISCAKELLQ
160 170 180 190 200
QRELRRKLLA DSGALNTNSV NGPRNWKACV QQDPSSRPGT PLCSGPGRGV
210 220 230 240 250
SSVGSTPKST NLPSVLSRTV NSSSFSTIRN QTLDKLDTSY SSKETDQEVI
260 270 280 290 300
CLEPAALPSP KVNGKGSTSL SRPSEASFNG SWCEKPTGRD SGNWRVPERP
310 320 330 340 350
TASTALKAQH TAPAGNPASG CWDVNDTDFD LDHFDIDDFD EGWEEAVAPE
360 370 380 390 400
AAPEAPPAPQ WQPLREGSAS LRCRLLAAAA GSAPGPHPTA PKSGCGISAK
410 420 430 440 450
SSSEPLVHNP AHERFRGMKF SHSEEMLKIF HRKFGLHSFR TNQLEAINAA
460 470 480 490 500
LLGEDCFILM PTGGGKSLCY QLPACVSAGV TVVISPLRSL IIDQVQKLKT
510 520 530 540 550
LDIASTYLTG DITDADASKT YMQLSKKDPI IKLLYVTPEK VCASNRLLSA
560 570 580 590 600
LENLYNRKLL ARFVIDEAHC VSQWGHDFRK DYKRLNMLRK KFHSVPMMAL
610 620 630 640 650
TATANPRVQK DIQNQLEMLK PQVFTMSFNR HNLKYDVLPK KPKKVAMDCL
660 670 680 690 700
EWIKKYHPHD SGIIYCLSRH ECDTTAAILQ KEGLAALAYH AGLTDSNRDL
710 720 730 740 750
VQKKWVNQEG CQVICATIAF GMGIDKPDVR YVIHASLPKS IEGYYQESGR
760 770 780 790 800
AGRDGEMSHC LLFYSYSDVT RLRRLILMEK DGNSHTRQTH FNNLYSMVHY
810 820 830 840 850
CENVVDCRRI QLLAYFGETD FNPNFCKDHP EVICDNCSRK KDYKSRNVTD
860 870 880 890 900
EVKSIIRFVQ QHCGQVGGIN GNRNTGSGRY TLNMMVDIFL GAKSAKIQSG
910 920 930 940 950
IFGKGAAYSR HNVERLFRKL VLDKILDEDL YITANDQAVA YVVLGEKAQA
960 970 980 990 1000
VLNGLLQVEF HETENASAIR KQRASVTKMS QREEMVKKCL GELTDTCKTL
1010 1020 1030 1040 1050
GKIFDVHYFN IFSTSTLKKI AETLSSDAEV LLQIDGVTED KLEKYGAEII
1060 1070 1080 1090 1100
KVMDKYSEWT TPEDAACQSV DTAPGSAGTP GSEEEAADDV VTSSYFGGNA
1110 1120 1130 1140 1150
NQRRKRKRLP NSGESKRKKT SSGGSQQFYS KGARYRRARR APGSRAAAPA
1160 1170 1180
QSSALRGAGA RLGIMAPPKP SSRHFLQPSY AVL
Length:1,183
Mass (Da):130,294
Last modified:September 27, 2017 - v2
Checksum:iECB940035F08D117
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112K → R in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti198R → Q in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti223S → G in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti253E → K in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti289R → K in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti319S → L in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti339F → L in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti351A → T in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti358A → P in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti399A → V in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti505S → A in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti556N → D in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti741I → V in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti746Q → H in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti839R → T in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti866V → M in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti893K → E in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti898Q → H in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti921V → F in BAA96742 (PubMed:10880455).Curated1
Sequence conflicti1087A → E in BAA96742 (PubMed:10880455).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ720413 mRNA Translation: CAG32072.1
AB040747 mRNA Translation: BAA96742.1
RefSeqiNP_001007088.2, NM_001007087.1
UniGeneiGga.1914

Genome annotation databases

GeneIDi415577
KEGGigga:415577

Similar proteinsi

Entry informationi

Entry nameiBLM_CHICK
AccessioniPrimary (citable) accession number: Q9I920
Secondary accession number(s): Q5ZJM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: September 27, 2017
Last modified: May 23, 2018
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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