BLM_CHICK
ID BLM_CHICK Reviewed; 1183 AA.
AC Q9I920; Q5ZJM1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=RecQ-like DNA helicase BLM {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:28228481};
DE AltName: Full=Bloom syndrome protein homolog;
DE AltName: Full=RecQ helicase homolog;
GN Name=BLM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-1183.
RC TISSUE=Testis;
RX PubMed=10880455; DOI=10.1093/emboj/19.13.3428;
RA Wang W., Seki M., Narita Y., Sonoda E., Takeda S., Yamada K., Masuko T.,
RA Katada T., Enomoto T.;
RT "Possible association of BLM in decreasing DNA double strand breaks during
RT DNA replication.";
RL EMBO J. 19:3428-3435(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 97-162 OF HOMODIMER, FUNCTION,
RP DNA-BINDING, CATALYTIC ACTIVITY, SUBUNIT, HOMOOLIGOMERIZATION, AND REGION.
RX PubMed=28228481; DOI=10.1074/jbc.m116.761510;
RA Shi J., Chen W.F., Zhang B., Fan S.H., Ai X., Liu N.N., Rety S., Xi X.G.;
RT "A helical bundle in the N-terminal domain of the BLM helicase mediates
RT dimer and potentially hexamer formation.";
RL J. Biol. Chem. 292:5909-5920(2017).
CC -!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-
CC stranded DNA in a 3'-5' direction (PubMed:28228481). Participates in
CC DNA replication and repair (By similarity). Involved in 5'-end
CC resection of DNA during double-strand break (DSB) repair (By
CC similarity). Negatively regulates sister chromatid exchange (SCE) (By
CC similarity). Stimulates DNA 4-way junction branch migration and DNA
CC Holliday junction dissolution (By similarity). Binds DNA
CC (PubMed:28228481). Binds single-stranded DNA (ssDNA), forked duplex DNA
CC and DNA Holliday junction (By similarity).
CC {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:28228481}.
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:0000269|PubMed:28228481};
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 (PubMed:28228481). Homodimer (via N-terminus)
CC (PubMed:28228481). Homotetramer (via N-terminus); dimer of dimers
CC (PubMed:28228481). Homohexamer (via N-terminus) (PubMed:28228481).
CC Self-association negatively regulates DNA unwinding amplitude and rate
CC (PubMed:28228481). Oligomer complexes dissociate into monomer in
CC presence of ATP (PubMed:28228481). {ECO:0000269|PubMed:28228481}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region mediates dimerization and
CC homooligomerization (PubMed:28228481). Both the helicase ATP-binding
CC domain and the helicase C-terminal domain form intramolecular
CC interactions with the HRDC domain in a ATP-dependent manner (By
CC similarity). The HRDC domain is required for single-stranded DNA
CC (ssDNA) and DNA Holliday junction binding (By similarity).
CC {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:28228481}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ720413; CAG32072.1; -; mRNA.
DR EMBL; AB040747; BAA96742.1; -; mRNA.
DR RefSeq; NP_001007088.2; NM_001007087.1.
DR PDB; 5LUT; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I/J/K=97-162.
DR PDBsum; 5LUT; -.
DR AlphaFoldDB; Q9I920; -.
DR SMR; Q9I920; -.
DR STRING; 9031.ENSGALP00000013422; -.
DR PaxDb; Q9I920; -.
DR GeneID; 415577; -.
DR KEGG; gga:415577; -.
DR CTD; 641; -.
DR VEuPathDB; HostDB:geneid_415577; -.
DR eggNOG; KOG0351; Eukaryota.
DR InParanoid; Q9I920; -.
DR OrthoDB; 445763at2759; -.
DR PRO; PR:Q9I920; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0061749; F:forked DNA-dependent helicase activity; ISS:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:UniProtKB.
DR GO; GO:0009378; F:four-way junction helicase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0090329; P:regulation of DNA-templated DNA replication; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012532; BDHCT.
DR InterPro; IPR032437; BLM_N.
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 InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF08072; BDHCT; 1.
DR Pfam; PF16202; BLM_N; 1.
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; SSF46785; SSF46785; 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 3D-structure; ATP-binding; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1..1183
FT /note="RecQ-like DNA helicase BLM"
FT /id="PRO_0000205041"
FT DOMAIN 447..622
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 648..795
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 983..1063
FT /note="HRDC"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..162
FT /note="Necessary for dimerization and homooligomerization"
FT /evidence="ECO:0000269|PubMed:28228481"
FT REGION 164..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..644
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 668..670
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 771..774
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 865..910
FT /note="DNA Holliday junction binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 881..883
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 892..896
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 931..937
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 998..1015
FT /note="Necessary for ssDNA and DNA Holliday junction
FT binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1068..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 566..569
FT /note="DEAH box"
FT MOTIF 1104..1120
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 463..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 753
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 834
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 837
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 488
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 579
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 691
FT /note="3' overhang DNA-binding; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 717
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 739
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 881
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT CONFLICT 112
FT /note="K -> R (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="R -> Q (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> G (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="E -> K (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="R -> K (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> L (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="F -> L (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="A -> T (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> P (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="A -> V (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="S -> A (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="N -> D (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="I -> V (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="Q -> H (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="R -> T (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="V -> M (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="K -> E (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="Q -> H (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="V -> F (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT CONFLICT 1087
FT /note="A -> E (in Ref. 2; BAA96742)"
FT /evidence="ECO:0000305"
FT HELIX 115..132
FT /evidence="ECO:0007829|PDB:5LUT"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:5LUT"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:5LUT"
SQ SEQUENCE 1183 AA; 130294 MW; ECB940035F08D117 CRC64;
MEEARAATNG GSGESQKLSN GEKSSQLEPG DVGNELLADI ELEEDDYLDV VPPSPEEELP
SFSPSVRNVS NIFKESPTDG RSAVHGTESE PELMAPKQPA AEQDSSAEHA DKGLHLEQQL
YSVMEDICKL VDAIPLHELT SISCAKELLQ QRELRRKLLA DSGALNTNSV NGPRNWKACV
QQDPSSRPGT PLCSGPGRGV SSVGSTPKST NLPSVLSRTV NSSSFSTIRN QTLDKLDTSY
SSKETDQEVI CLEPAALPSP KVNGKGSTSL SRPSEASFNG SWCEKPTGRD SGNWRVPERP
TASTALKAQH TAPAGNPASG CWDVNDTDFD LDHFDIDDFD EGWEEAVAPE AAPEAPPAPQ
WQPLREGSAS LRCRLLAAAA GSAPGPHPTA PKSGCGISAK SSSEPLVHNP AHERFRGMKF
SHSEEMLKIF HRKFGLHSFR TNQLEAINAA LLGEDCFILM PTGGGKSLCY QLPACVSAGV
TVVISPLRSL IIDQVQKLKT LDIASTYLTG DITDADASKT YMQLSKKDPI IKLLYVTPEK
VCASNRLLSA LENLYNRKLL ARFVIDEAHC VSQWGHDFRK DYKRLNMLRK KFHSVPMMAL
TATANPRVQK DIQNQLEMLK PQVFTMSFNR HNLKYDVLPK KPKKVAMDCL EWIKKYHPHD
SGIIYCLSRH ECDTTAAILQ KEGLAALAYH AGLTDSNRDL VQKKWVNQEG CQVICATIAF
GMGIDKPDVR YVIHASLPKS IEGYYQESGR AGRDGEMSHC LLFYSYSDVT RLRRLILMEK
DGNSHTRQTH FNNLYSMVHY CENVVDCRRI QLLAYFGETD FNPNFCKDHP EVICDNCSRK
KDYKSRNVTD EVKSIIRFVQ QHCGQVGGIN GNRNTGSGRY TLNMMVDIFL GAKSAKIQSG
IFGKGAAYSR HNVERLFRKL VLDKILDEDL YITANDQAVA YVVLGEKAQA VLNGLLQVEF
HETENASAIR KQRASVTKMS QREEMVKKCL GELTDTCKTL GKIFDVHYFN IFSTSTLKKI
AETLSSDAEV LLQIDGVTED KLEKYGAEII KVMDKYSEWT TPEDAACQSV DTAPGSAGTP
GSEEEAADDV VTSSYFGGNA NQRRKRKRLP NSGESKRKKT SSGGSQQFYS KGARYRRARR
APGSRAAAPA QSSALRGAGA RLGIMAPPKP SSRHFLQPSY AVL
