HELQ_CAEEL
ID HELQ_CAEEL Reviewed; 923 AA.
AC H2KY86; Q65XX0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Helicase POLQ-like {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8TDG4};
GN Name=helq-1 {ECO:0000303|PubMed:9851916, ECO:0000312|WormBase:Y55B1AL.3a};
GN ORFNames=Y55B1AL.3 {ECO:0000312|WormBase:Y55B1AL.3a};
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 [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 [2]
RP FUNCTION.
RX PubMed=18472307; DOI=10.1016/j.dnarep.2008.03.021;
RA Muzzini D.M., Plevani P., Boulton S.J., Cassata G., Marini F.;
RT "Caenorhabditis elegans POLQ-1 and HEL-308 function in two distinct DNA
RT interstrand cross-link repair pathways.";
RL DNA Repair 7:941-950(2008).
RN [3]
RP FUNCTION.
RX PubMed=34880204; DOI=10.1038/s41467-021-27408-z;
RA Kamp J.A., Lemmens B.B.L.G., Romeijn R.J., Changoer S.C., van Schendel R.,
RA Tijsterman M.;
RT "Helicase Q promotes homology-driven DNA double-strand break repair and
RT prevents tandem duplications.";
RL Nat. Commun. 12:7126-7126(2021).
CC -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC homology-driven double-strand break (DSB) repair (PubMed:18472307,
CC PubMed:34880204). Involved in different DSB repair mechanisms that are
CC guided by annealing of extensive stretches of complementary bases at
CC break ends, such as microhomology-mediated end-joining (MMEJ), single-
CC strand annealing (SSA) or synthesis-dependent strand annealing (SDSA)
CC (PubMed:34880204). {ECO:0000269|PubMed:18472307,
CC ECO:0000269|PubMed:34880204}.
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:Q8TDG4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q8TDG4};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDG4}.
CC Chromosome {ECO:0000250|UniProtKB:Q8TDG4}. Note=Localizes to sites of
CC DNA damage. {ECO:0000250|UniProtKB:Q8TDG4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=H2KY86-1; Sequence=Displayed;
CC Name=b;
CC IsoId=H2KY86-2; Sequence=VSP_061492;
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD61810.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD61811.1; -; Genomic_DNA.
DR RefSeq; NP_001022911.1; NM_001027740.3.
DR RefSeq; NP_001022912.1; NM_001027741.2.
DR AlphaFoldDB; H2KY86; -.
DR SMR; H2KY86; -.
DR STRING; 6239.Y55B1AL.3a; -.
DR EPD; H2KY86; -.
DR PaxDb; H2KY86; -.
DR PeptideAtlas; H2KY86; -.
DR EnsemblMetazoa; Y55B1AL.3a.1; Y55B1AL.3a.1; WBGene00021905. [H2KY86-1]
DR EnsemblMetazoa; Y55B1AL.3b.1; Y55B1AL.3b.1; WBGene00021905. [H2KY86-2]
DR EnsemblMetazoa; Y55B1AL.3b.2; Y55B1AL.3b.2; WBGene00021905. [H2KY86-2]
DR EnsemblMetazoa; Y55B1AL.3b.3; Y55B1AL.3b.3; WBGene00021905. [H2KY86-2]
DR GeneID; 175210; -.
DR KEGG; cel:CELE_Y55B1AL.3; -.
DR CTD; 175210; -.
DR WormBase; Y55B1AL.3a; CE27019; WBGene00021905; helq-1.
DR WormBase; Y55B1AL.3b; CE37439; WBGene00021905; helq-1.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000157350; -.
DR HOGENOM; CLU_006553_1_0_1; -.
DR InParanoid; H2KY86; -.
DR OMA; MFLNANI; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; H2KY86; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00021905; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; H2KY86; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IPI:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:WormBase.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IDA:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IDA:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:WormBase.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025567; DUF4332.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF14229; DUF4332; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..923
FT /note="Helicase POLQ-like"
FT /id="PRO_0000455410"
FT DOMAIN 178..349
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 392..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 295..298
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..454
FT /note="Missing (in isoform b)"
FT /id="VSP_061492"
SQ SEQUENCE 923 AA; 102969 MW; DE32173B3E42F773 CRC64;
MNRTPIRRCK SAEIEEDPFS PIPKFSRLRT PRTSREYVCP LKSTSPQSPS SSTENEPPPV
SVTSPPARKR ALEESTVTPI QQKIGPPVLK RSSLSKLADG FRTAAYLNNE SENDDDPFGL
SFRNEQVLMS KCAPAPEKRP ETLTLDPSKC LPERDMEMYR KIKKLDKFYD WQQECLSDKR
LLDGENCILS LPTGAGKTLI AEVLMLREAI VRKRNAILVL PYVAIVQEKI SALAPFEDAF
GINIEEYASN KGRFPPIKRR KRVSVYVATI EKANMLINSL ITQGQLDRVG MVVVDELHMI
GDGGRGAILE QLLAKFLYKG TGQIVGMSAT LPNIDDLKFA LRAFVYSTNF RPVELTEFVK
IGQTMHQVSE NGDLNPAGDL PTNNLKSTDP DGICQLLAKL IPKNSAVIFC PNKKNCENVA
VLIAKTLPAH IRQAKRAESD AFLQSYLSDN DDERMDAVLK QCILSGVAYH HSGLTQDERK
CVEAAFMEGL IYVVCATSTL AAGVNLPVRR VIIKAPMVGR ERLGKAQYLQ MAGRAGRAGF
DTKGDCITII KAGEEERWFR EMLKSDIPRC MSSLSSEESM GSFILDCVVL KLAENIEEIM
TAVRYSLFYA QESPENIRKL VESSVKRLEE HYFITIEPLE QDVASEPSAQ ASSIPRVPGK
ISPSDLGNAV FNAGFDPDEA TRLHADLVSS LNQGVIFASH FHLLFIITPY EQVCNINWDL
FLLMYNALPS SERKLLAECG LEEKFILEAI ITRVDLTAGT PRMRLYIALM LQKIWNHEPM
YTVAERFGVE KGWLQATLQS SISQAASIAK FSEKITTMWP LRKLLPELVQ RLSEAAQPEL
LPLMTVDGIK KARAAILFKA GYKTVGMIAR ANPLKLVQEL GTIRMAQANS IIASARMVLR
DQVDEKMEEL DVWGVATDSF NYF
