BLM_CAEEL
ID BLM_CAEEL Reviewed; 988 AA.
AC O18017; Q8MZK2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=RecQ-like DNA helicase blm-1 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
DE AltName: Full=Bloom syndrome protein homolog;
DE AltName: Full=High incidence of males protein 6;
DE AltName: Full=RecQ helicase homolog;
GN Name=him-6 {ECO:0000312|WormBase:T04A11.6};
GN Synonyms=blm-1 {ECO:0000312|WormBase:T04A11.6};
GN ORFNames=T04A11.6 {ECO:0000312|WormBase:T04A11.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wicky C., Passannante M., Rose A., Mueller F.;
RT "The C. elegans homolog of the human Bloom syndrome protein is required for
RT normal level of meiotic recombination and for genomic stability.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP REPEATS.
RX PubMed=10049920; DOI=10.1093/genetics/151.3.1027;
RA Kusano K., Berres M.E., Engels W.R.;
RT "Evolution of the RECQ family of helicases: a Drosophila homolog, Dmblm, is
RT similar to the human Bloom syndrome gene.";
RL Genetics 151:1027-1039(1999).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH CDC-48.1 AND CRP-1, AND INTERACTION WITH
RP CDC-48.1.
RX PubMed=18458060; DOI=10.1128/mcb.02252-07;
RA Caruso M.E., Jenna S., Bouchecareilh M., Baillie D.L., Boismenu D.,
RA Halawani D., Latterich M., Chevet E.;
RT "GTPase-mediated regulation of the unfolded protein response in
RT Caenorhabditis elegans is dependent on the AAA+ ATPase CDC-48.";
RL Mol. Cell. Biol. 28:4261-4274(2008).
RN [5]
RP FUNCTION, INTERACTION WITH RMH-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27011106; DOI=10.1371/journal.pbio.1002412;
RA Jagut M., Hamminger P., Woglar A., Millonigg S., Paulin L., Mikl M.,
RA Dello Stritto M.R., Tang L., Habacher C., Tam A., Gallach M.,
RA von Haeseler A., Villeneuve A.M., Jantsch V.;
RT "Separable roles for a Caenorhabditis elegans RMI1 homolog in promoting and
RT antagonizing meiotic crossovers ensure faithful chromosome inheritance.";
RL PLoS Biol. 14:E1002412-E1002412(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27010650; DOI=10.1371/journal.pgen.1005872;
RA Hong Y., Sonneville R., Agostinho A., Meier B., Wang B., Blow J.J.,
RA Gartner A.;
RT "The SMC-5/6 complex and the HIM-6 (BLM) helicase synergistically promote
RT meiotic recombination intermediate processing and chromosome maturation
RT during Caenorhabditis elegans meiosis.";
RL PLoS Genet. 12:E1005872-E1005872(2016).
RN [7]
RP FUNCTION, IDENTIFICATION IN BTR COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=34252074; DOI=10.1371/journal.pgen.1009663;
RA Velkova M., Silva N., Dello Stritto M.R., Schleiffer A., Barraud P.,
RA Hartl M., Jantsch V.;
RT "Caenorhabditis elegans RMI2 functional homolog-2 (RMIF-2) and RMI1 (RMH-1)
RT have both overlapping and distinct meiotic functions within the BTR
RT complex.";
RL PLoS Genet. 17:e1009663-e1009663(2021).
CC -!- FUNCTION: Component of the BTR double Holliday Junction dissolution
CC complex, which is involved in homologous recombination during meiotic
CC double strand break in the germline (Probable). Stabilizes and
CC positively regulates the localization of the BTR double Holliday
CC Junction dissolution complex component rmh-1 at nuclear foci during
CC meiotic recombination (PubMed:27011106). Participates in DNA
CC replication and repair (By similarity). Exhibits a magnesium-dependent
CC ATP-dependent DNA-helicase activity that unwinds single- and double-
CC stranded DNA in a 3'-5' direction (By similarity). Negatively regulates
CC sister chromatid exchange (SCE) (PubMed:27010650).
CC {ECO:0000250|UniProtKB:Q9DEY9, ECO:0000269|PubMed:27010650,
CC ECO:0000269|PubMed:27011106, ECO:0000305|PubMed:34252074}.
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. Negatively regulates sister chromatid exchange (SCE)
CC (PubMed:27010650). Stimulates DNA 4-way junction branch migration and
CC DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA),
CC forked duplex DNA and DNA Holliday junction.
CC {ECO:0000250|UniProtKB:P54132, ECO:0000250|UniProtKB:Q9DEY9,
CC ECO:0000269|PubMed:27010650}.
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 (By similarity). Homodimer (via N-terminus) (By
CC similarity). Homotetramer (via N-terminus); dimer of dimers (By
CC similarity). Homohexamer (via N-terminus) (By similarity). Self-
CC association negatively regulates DNA unwinding amplitude and rate (By
CC similarity). Oligomer forms dissociate into monomer in presence of ATP
CC (By similarity). Component of the BTR double Holliday Junction
CC dissolution complex composed of at least him-6, top-3, rmh-1 and rmif-
CC 2, which is involved in double strand break repair in the germline
CC (Probable). May interact with rmh-1; the interaction is required for
CC mutual stability and localization at nuclear foci (PubMed:27011106).
CC Forms a complex composed of cdc-48.1, him-6 and crp-1; within the
CC complex, interacts with cdc-48.1 (PubMed:18458060).
CC {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:18458060,
CC ECO:0000269|PubMed:27011106, ECO:0000305|PubMed:34252074}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27011106,
CC ECO:0000269|PubMed:34252074}. Chromosome {ECO:0000269|PubMed:27011106}.
CC Note=Localizes on chromosomes during pachytene in meiotic prophase I in
CC oocytes. Co-localizes with rmh-1 at mid-pachytene and late-pachytene in
CC meiotic prophase I (PubMed:27011106). Localization at nuclear foci is
CC dependent on rmh-1 during meiotic recombination (PubMed:27011106).
CC {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
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 -!- DISRUPTION PHENOTYPE: Reduced viability, increased rad-51 foci in the
CC germline and an increase of meiotic crossover formation in the central
CC region of chromosomes (PubMed:27010650). Reduced number of rmh-1 foci
CC in the pachytene region (PubMed:27011106). In an smc-5 mutant
CC background, defects in diakinetic chiasmata formation, compromised
CC chromosome segregation and aberrant distribution of the condensin II
CC subunit hcp-6 in meiosis (PubMed:27010650).
CC {ECO:0000269|PubMed:27010650, ECO:0000269|PubMed:27011106}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AY095296; AAM26298.1; -; mRNA.
DR EMBL; BX284604; CAB05609.2; -; Genomic_DNA.
DR PIR; T24415; T24415.
DR RefSeq; NP_502390.2; NM_069989.5.
DR AlphaFoldDB; O18017; -.
DR SMR; O18017; -.
DR BioGRID; 43294; 9.
DR IntAct; O18017; 4.
DR MINT; O18017; -.
DR STRING; 6239.T04A11.6; -.
DR EPD; O18017; -.
DR PaxDb; O18017; -.
DR EnsemblMetazoa; T04A11.6.1; T04A11.6.1; WBGene00001865.
DR GeneID; 178201; -.
DR KEGG; cel:CELE_T04A11.6; -.
DR UCSC; T04A11.6.1; c. elegans.
DR CTD; 178201; -.
DR WormBase; T04A11.6; CE31724; WBGene00001865; him-6.
DR eggNOG; KOG0351; Eukaryota.
DR GeneTree; ENSGT00940000156800; -.
DR HOGENOM; CLU_001103_3_0_1; -.
DR InParanoid; O18017; -.
DR OMA; CLQWIRK; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; O18017; -.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR SignaLink; O18017; -.
DR PRO; PR:O18017; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001865; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IGI:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IGI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0032502; P:developmental process; IEA:UniProt.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:WormBase.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
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:0051321; P:meiotic cell cycle; IGI:WormBase.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:WormBase.
DR GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IGI:WormBase.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:WormBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:WormBase.
DR GO; GO:0071139; P:resolution of recombination intermediates; IMP:WormBase.
DR GO; GO:0010165; P:response to X-ray; IMP:WormBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; 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; 1.
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 ATP-binding; Chromosome; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Zinc.
FT CHAIN 1..988
FT /note="RecQ-like DNA helicase blm-1"
FT /id="PRO_0000205043"
FT REPEAT 121..129
FT /note="1"
FT /evidence="ECO:0000269|PubMed:10049920"
FT REPEAT 130..138
FT /note="2"
FT /evidence="ECO:0000269|PubMed:10049920"
FT DOMAIN 256..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 458..603
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 807..888
FT /note="HRDC"
FT /evidence="ECO:0000250|UniProtKB:P54132,
FT ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 46..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..138
FT /note="2 X 9 AA tandem repeats of [DE]-P-P-I-V-D-L-D-[ED]"
FT REGION 148..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..480
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 580..583
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 676..678
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 687..691
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 736..742
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT REGION 930..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 375..378
FT /note="DEAH box"
FT MOTIF 939..955
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9QY16"
FT COMPBIAS 90..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 272..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 633
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 297
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 388
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 501
FT /note="3' overhang DNA-binding; via amide nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 526
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 548
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
FT SITE 676
FT /note="3' overhang DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P54132"
SQ SEQUENCE 988 AA; 110659 MW; CB76494083F220A2 CRC64;
MIKNREIEVA PPRRTIQFGG YTFVEPDLNF KAPIFSCCGS IRDPSCEERE EEYIDNGHDE
EPPVEVNRIQ ESTSFDEPVS SPPRYRPSEN PGPSSSSYEP GHYSFNEYQQ FPSRPQKRLV
DPPIVDLDEE PPIVDLDDSF DNFHVGSTSE EVVSGDIAPE EEEEEGHDSF DDFESVPAQP
PSKNTLASLQ KSDSEIALNQ QRHDMHGRFR GFLQDDSEEF SDEVGLLGAD MNKELYDTLK
SKFGFNQFRH RQKQCILSTL MGHDTFVLMP TGAGKSLCYQ LPAVILPGVT VVVSPLRSLI
EDQKMKMKEL GIGCEALTAD LGAPAQEKIY AELGSGNPSI KLLYVTPEKI SASGRLNSVF
FDLHRRGLLA RFVIDEAHCV SQWGHDFRPD YTKLSSLREK YANPPVPIIA LTATATPKIV
TDARDHLKMQ NSKLFISSFV RDNLKYDLIP KAARSLINVV EKMKQLYPGK SGIVYCLSRK
ECETVQMMLT KAGLSAEVYH AGLNDNLRVS VQRSWIANKF DVICATIAFG MGIDKPDVRF
VIHYSLPKSI EGYYQETGRA GRDGMPSYCL MLYSYHDSIR LRRMIEEGNT TTGVRSMHLN
NVLQVVAYCE NVSVCRRKML VEHFGEVYDE QSCRNSKTPC DICERQRKNA EAIRLFDVST
DALSILKCLP RMQKATLKYI SELYRGALIK KSQEQAMRLG HTKLPFYSKG QGMSEQDALR
FVRKLVIEGY IHERLYSVPN QAAAVFAYAE LTEAGRDLAN GKKTAKVYLH IVTCERKRKN
AGLIELSNMN IVSEAQALKE RHMVKHGDVF TRCLQDLTHL ITAVAESSGL SGPYSIVSRE
GIEQIAALLP RTNSDLLRID SMTQIKVTKY GRLIMELLAT YWKQVDEREE EEMRNQLDKL
KSGEIVMGGF ATLQSDPGFP SVPYMKPLGG GGGCRGRGKK RAFSGFSSGR ATKKPRATAP
SARGKTSGRG GAKPATSLKR NMYPATSM
