UniProtKB - Q9I920 (BLM_CHICK)
Protein
Bloom syndrome protein homolog
Gene
BLM
Organism
Gallus gallus (Chicken)
Status
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
- EC:3.6.4.121 Publication
Cofactori
Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 488 | 3' overhang DNA-bindingBy similarity | 1 | |
Sitei | 579 | 3' overhang DNA-bindingBy similarity | 1 | |
Sitei | 691 | 3' overhang DNA-binding; via amide nitrogenBy similarity | 1 | |
Sitei | 717 | 3' overhang DNA-bindingBy similarity | 1 | |
Sitei | 739 | 3' overhang DNA-bindingBy similarity | 1 | |
Binding sitei | 753 | ATPBy similarity | 1 | |
Metal bindingi | 807 | ZincBy similarity | 1 | |
Metal bindingi | 826 | ZincBy similarity | 1 | |
Metal bindingi | 834 | ZincBy similarity | 1 | |
Metal bindingi | 837 | ZincBy similarity | 1 | |
Sitei | 881 | 3' overhang DNA-bindingBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 439 – 443 | ATPBy similarity | 5 | |
Nucleotide bindingi | 463 – 467 | ATPBy similarity | 5 |
GO - Molecular functioni
- 3'-5' DNA helicase activity Source: GO_Central
- ATP binding Source: UniProtKB
- DNA binding Source: UniProtKB
- DNA-dependent ATPase activity Source: UniProtKB
- DNA helicase activity Source: UniProtKB
- forked DNA-dependent helicase activity Source: UniProtKB
- four-way junction DNA binding Source: UniProtKB
- four-way junction helicase activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- single-stranded DNA binding Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- DNA double-strand break processing Source: UniProtKB
- DNA duplex unwinding Source: UniProtKB
- DNA recombination Source: GO_Central
- DNA repair Source: GO_Central
- DNA unwinding involved in DNA replication Source: GO_Central
- double-strand break repair via homologous recombination Source: GO_Central
- G-quadruplex DNA unwinding Source: GO_Central
- protein complex oligomerization Source: UniProtKB
- protein homooligomerization Source: UniProtKB
- regulation of DNA-dependent DNA replication Source: UniProtKB
- telomere maintenance Source: GO_Central
Keywordsi
Molecular function | DNA-binding, Helicase, Hydrolase |
Biological process | DNA damage, DNA repair, DNA replication |
Ligand | ATP-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 |
Organismi | Gallus gallus (Chicken) |
Taxonomic identifieri | 9031 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus |
Proteomesi |
|
Subcellular locationi
Nucleus
- Nucleus By similarity
Nucleus
- nucleus Source: GO_Central
Other locations
- chromosome Source: GO_Central
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000205041 | 1 – 1183 | Bloom syndrome protein homologAdd BLAST | 1183 |
Proteomic databases
PaxDbi | Q9I920 |
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 PublicationGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 9031.ENSGALP00000013422 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9I920 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 447 – 622 | Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST | 176 | |
Domaini | 648 – 795 | Helicase C-terminalPROSITE-ProRule annotationBy similarityAdd BLAST | 148 | |
Domaini | 983 – 1063 | HRDCPROSITE-ProRule annotationBy similarityAdd BLAST | 81 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 110 – 162 | Necessary for dimerization and homooligomerization1 PublicationAdd BLAST | 53 | |
Regioni | 641 – 644 | 3' overhang DNA-bindingBy similarity | 4 | |
Regioni | 668 – 670 | 3' overhang DNA-bindingBy similarity | 3 | |
Regioni | 771 – 774 | 3' overhang DNA-bindingBy similarity | 4 | |
Regioni | 865 – 910 | DNA Holliday junction bindingBy similarityAdd BLAST | 46 | |
Regioni | 881 – 883 | 3' overhang DNA-bindingBy similarity | 3 | |
Regioni | 892 – 896 | 3' overhang DNA-bindingBy similarity | 5 | |
Regioni | 931 – 937 | 3' overhang DNA-bindingBy similarity | 7 | |
Regioni | 998 – 1015 | Necessary for ssDNA and DNA Holliday junction bindingBy similarityAdd BLAST | 18 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 566 – 569 | DEAH box | 4 | |
Motifi | 1104 – 1120 | Nuclear localization signalBy similarityAdd BLAST | 17 |
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
Phylogenomic databases
eggNOGi | KOG0351, Eukaryota |
InParanoidi | Q9I920 |
OrthoDBi | 445763at2759 |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View 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 |
Pfami | View 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 |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit SM00341, HRDC, 1 hit SM00956, RQC, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF47819, SSF47819, 1 hit SSF52540, SSF52540, 2 hits |
TIGRFAMsi | TIGR00614, recQ_fam, 1 hit |
PROSITEi | View 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 |
i Sequence
Sequence statusi: Complete.
Q9I920-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 112 | K → R in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 198 | R → Q in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 223 | S → G in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 253 | E → K in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 289 | R → K in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 319 | S → L in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 339 | F → L in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 351 | A → T in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 358 | A → P in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 399 | A → V in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 505 | S → A in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 556 | N → D in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 741 | I → V in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 746 | Q → H in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 839 | R → T in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 866 | V → M in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 893 | K → E in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 898 | Q → H in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 921 | V → F in BAA96742 (PubMed:10880455).Curated | 1 | |
Sequence conflicti | 1087 | A → E in BAA96742 (PubMed:10880455).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ720413 mRNA Translation: CAG32072.1 AB040747 mRNA Translation: BAA96742.1 |
RefSeqi | NP_001007088.2, NM_001007087.1 |
Genome annotation databases
GeneIDi | 415577 |
KEGGi | gga:415577 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ720413 mRNA Translation: CAG32072.1 AB040747 mRNA Translation: BAA96742.1 |
RefSeqi | NP_001007088.2, NM_001007087.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5LUT | X-ray | 2.72 | A/B/C/D/E/F/G/H/I/J/K | 97-162 | [»] | |
SMRi | Q9I920 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9031.ENSGALP00000013422 |
Proteomic databases
PaxDbi | Q9I920 |
Genome annotation databases
GeneIDi | 415577 |
KEGGi | gga:415577 |
Organism-specific databases
CTDi | 641 |
Phylogenomic databases
eggNOGi | KOG0351, Eukaryota |
InParanoidi | Q9I920 |
OrthoDBi | 445763at2759 |
Miscellaneous databases
PROi | PR:Q9I920 |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View 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 |
Pfami | View 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 |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit SM00341, HRDC, 1 hit SM00956, RQC, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF47819, SSF47819, 1 hit SSF52540, SSF52540, 2 hits |
TIGRFAMsi | TIGR00614, recQ_fam, 1 hit |
PROSITEi | View 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BLM_CHICK | |
Accessioni | Q9I920Primary (citable) accession number: Q9I920 Secondary accession number(s): Q5ZJM1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 2, 2001 |
Last sequence update: | September 27, 2017 | |
Last modified: | December 2, 2020 | |
This is version 116 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families