BLM_XENLA
ID BLM_XENLA Reviewed; 1364 AA.
AC Q9DEY9;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RecQ-like DNA helicase BLM {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
DE AltName: Full=Bloom syndrome protein homolog;
DE Short=xBLM;
DE AltName: Full=RecQ helicase homolog;
GN Name=blm;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Oocyte;
RX PubMed=11040210; DOI=10.1101/gad.822400;
RA Liao S., Graham J., Yan H.;
RT "The function of Xenopus Bloom's syndrome protein homolog (xBLM) in DNA
RT replication.";
RL Genes Dev. 14:2570-2575(2000).
CC -!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-
CC stranded DNA in a 3'-5' direction. Participates in DNA replication and
CC repair (PubMed:11040210). Involved in 5'-end resection of DNA during
CC double-strand break (DSB) repair. Negatively regulates sister chromatid
CC exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA
CC Holliday junction dissolution. Binds single-stranded DNA (ssDNA),
CC forked duplex DNA and DNA Holliday junction.
CC {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:11040210}.
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:0000250|UniProtKB:P54132};
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. Homodimer (via N-terminus). Homotetramer (via N-
CC terminus); dimer of dimers. Homohexamer (via N-terminus). Self-
CC association negatively regulates DNA unwinding amplitude and rate.
CC Oligomer complexes dissociate into monomer in presence of ATP.
CC {ECO:0000250|UniProtKB:P54132}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region mediates dimerization and
CC homooligomerization. Both the helicase ATP-binding domain and the
CC helicase C-terminal domain form intramolecular interactions with the
CC HRDC domain in a ATP-dependent manner. The HRDC domain is required for
CC single-stranded DNA (ssDNA) and DNA Holliday junction binding.
CC {ECO:0000250|UniProtKB:P54132}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AF307841; AAG30928.1; -; mRNA.
DR RefSeq; NP_001079095.1; NM_001085626.1.
DR AlphaFoldDB; Q9DEY9; -.
DR SMR; Q9DEY9; -.
DR BioGRID; 96849; 1.
DR PRIDE; Q9DEY9; -.
DR GeneID; 373628; -.
DR KEGG; xla:373628; -.
DR CTD; 373628; -.
DR Xenbase; XB-GENE-982565; blm.S.
DR OrthoDB; 445763at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 373628; Expressed in blastula and 18 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
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; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0090329; P:regulation of DNA-templated DNA replication; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..1364
FT /note="RecQ-like DNA helicase BLM"
FT /id="PRO_0000205042"
FT DOMAIN 628..803
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 829..976
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1164..1244
FT /note="HRDC"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..377
FT /note="Necessary for dimerization and homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 380..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..825
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 849..851
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 952..955
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1046..1090
FT /note="DNA Holliday junction binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1061..1063
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1072..1076
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1111..1117
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1179..1196
FT /note="Necessary for ssDNA and DNA Holliday junction
FT binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 1251..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 747..750
FT /note="DEAH box"
FT MOTIF 1285..1301
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 620..624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 644..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 934
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 988
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1018
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 1194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 669
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 760
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 872
FT /note="3' overhang DNA-binding; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 898
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 920
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 1061
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
SQ SEQUENCE 1364 AA; 152324 MW; 208486CF189502E0 CRC64;
MAALPQNNLQ KQLELFPAKG TSNKLSLQKT KSSVFTFKKK CSPNVSASTG FIPFQQHVLK
DKNVNVKQDG THTALPKATE RNKINCFFTP VYTKSGQPPQ VVALKDHVHG NDSANKPPST
EDAASKKTGI NTSFGSVTSL EEWDDLDDFD TSVSPPKSHA GKGGKTPQKC KNTSPVASFK
IQSISPEGPT TEKHDCAKLL YDNNEVASEP RKNLHAKTAE SPDQSLVCLA SVEPTNLERD
MCRNTDYLGT DDLEHDQETL SQVLIEEEDD CEPDFIPPSP SDESLSSPPV LKVISAQRKH
KVSSLTDVND CENTTDHLQG QSVSTSLDSK VPSQLLTLML EICDLVDKIP ISELHVLSCG
LDLKKKRDMR KRLLSNDSVF RSSPADSSTV SLTSCTSSTQ NRDFNVNAPK GAESLSGSSV
SKVFKFNKLA VHDIGTKESE NSANSAPNFM EKIGNKTSFS FRAGGDSIME NSFNFHSSVL
SNSRFNTPQN EKPISSSTCT RPYSQPIDDM DNPDLDFDID NFDIEDLDDI HCLDSPAAPS
VSSKNVPQYP TIREAQLDSR NKEKNTRNNT GDTTNPSLLS DSLLKPQIEN PAHERFRGFN
FPHSKEMMKI FHKKFGLHRF RTNQLEAINA CLCGEDCFIL MPTGGGKSLC YQLPGCISPG
VTIVISPLRS LIVDQVQKLT SLDIPATYLT GDKTDAEAAS IYLQLSKKDP IIKLLYVTPE
KVCASTRLIS TMENLYERQL LARFVIDEAH CVSQWGHDFR PDYKRLNVLR QKFQSVPMMA
LTATANPRVK KDILNQLKMT KPQIFTMSFN RDNLKYEVLP KKPKRVALDC VEWIKKHHPN
DSGIIYCLSR HECDTMADTL QKEGLAALAY HAGLADSNRD YVQHKWINQD DCQVICATIA
FGMGIDKPDV RYVIHASLPK SVEGYYQESG RAGRDGETSH CLLFYSYHDV TRIRRLIQME
KDGNSHTKQT HFNNLYSMVH YCENVVECRR MQLLSYFGEN NFNPNFCKEH TQVACDNCLG
KKNYKSRDVT DDVGNIVRFV QDNCSLVQGR GKGRSNNTRL TLNMMVDIFL GSKSAKIQTG
LFGKGAAYSR HNAERLFRKL VLDRIIDEEL YITFNDQAVA YVKMGERAQA VLNGFLKVDF
QDTESASSIR KQKASVVTNT SQREEMVKKC QAELTELCKR LGKIFGVHYF NIFNTATIRR
IAESLSPEPE VLLQIDGVTE DKLDKYGAEL IDVLQKYSEW TLPVEDICQK SGGPANVSAR
RSNSDHDDES CDKSSYFSSN NKKGPKRKNS SYFGKSKKRK TGGDGQQSRS KNGNSSYARK
NSTAKTSSSY ISGSKTGADK RPGFMAPPMP QPNRRFLKPS YSMF
