HELQ_DROME
ID HELQ_DROME Reviewed; 1051 AA.
AC Q9VSE2; Q6NP41;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Helicase POLQ-like {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8TDG4};
DE AltName: Full=Mutagen-sensitive protein 301 {ECO:0000303|PubMed:16888338};
DE AltName: Full=Protein spindle-C {ECO:0000303|PubMed:9362456};
DE Short=Spindle-C {ECO:0000303|PubMed:9362456};
GN Name=mus301 {ECO:0000303|PubMed:16888338, ECO:0000312|FlyBase:FBgn0002899};
GN Synonyms=spnC {ECO:0000303|PubMed:9362456};
GN ORFNames=CG7972 {ECO:0000312|FlyBase:FBgn0002899};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=9362456; DOI=10.1242/dev.124.24.4927;
RA Gonzalez-Reyes A., Elliott H., St Johnston D.;
RT "Oocyte determination and the origin of polarity in Drosophila: the role of
RT the spindle genes.";
RL Development 124:4927-4937(1997).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-455; GLY-637;
RP MET-665 AND GLN-811.
RX PubMed=16888338; DOI=10.1534/genetics.106.058289;
RA McCaffrey R., St Johnston D., Gonzalez-Reyes A.;
RT "Drosophila mus301/spindle-C encodes a helicase with an essential role in
RT double-strand DNA break repair and meiotic progression.";
RL Genetics 174:1273-1285(2006).
CC -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC homology-driven double-strand break (DSB) repair (PubMed:16888338).
CC Involved in different DSB repair mechanisms that are guided by
CC annealing of extensive stretches of complementary bases at break ends,
CC such as microhomology-mediated end-joining (MMEJ), single-strand
CC annealing (SSA) or synthesis-dependent strand annealing (SDSA) (By
CC similarity). {ECO:0000250|UniProtKB:H2KY86,
CC ECO:0000269|PubMed:16888338}.
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 -!- DISRUPTION PHENOTYPE: Impaired meiosis, leading to maternal mutants
CC with eggshell defects (PubMed:9362456, PubMed:16888338). Mutant females
CC produce ventralized egg shells, with phenotypes ranging from fused
CC dorsal appendages to fully ventralized eggs with no dorsal appendages
CC (PubMed:16888338). Mutant flies are hypersensitive to chemical mutagens
CC (PubMed:16888338). {ECO:0000269|PubMed:16888338,
CC ECO:0000269|PubMed:9362456}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF50481.1; -; Genomic_DNA.
DR EMBL; BT011090; AAR82756.2; -; mRNA.
DR RefSeq; NP_648178.1; NM_139921.4.
DR AlphaFoldDB; Q9VSE2; -.
DR SMR; Q9VSE2; -.
DR IntAct; Q9VSE2; 4.
DR STRING; 7227.FBpp0076412; -.
DR PaxDb; Q9VSE2; -.
DR EnsemblMetazoa; FBtr0076689; FBpp0076412; FBgn0002899.
DR GeneID; 38905; -.
DR KEGG; dme:Dmel_CG7972; -.
DR UCSC; CG7972-RA; d. melanogaster.
DR CTD; 38905; -.
DR FlyBase; FBgn0002899; mus301.
DR VEuPathDB; VectorBase:FBgn0002899; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000157350; -.
DR HOGENOM; CLU_006553_0_0_1; -.
DR InParanoid; Q9VSE2; -.
DR OMA; MFLNANI; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; Q9VSE2; -.
DR BioGRID-ORCS; 38905; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38905; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0002899; Expressed in ovary and 16 other tissues.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IGI:FlyBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:FlyBase.
DR GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; TAS:FlyBase.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 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 1: Evidence at protein level;
KW ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1051
FT /note="Helicase POLQ-like"
FT /id="PRO_0000455411"
FT DOMAIN 274..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 497..689
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 391..394
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 455
FT /note="Y->D: In mus308-2255 mutant; mutant females produce
FT ventralized egg shells; when associated with H-811."
FT /evidence="ECO:0000269|PubMed:16888338"
FT MUTAGEN 637
FT /note="G->Q: In mus308-094 mutant; mutant females produce
FT ventralized egg shells."
FT /evidence="ECO:0000269|PubMed:16888338"
FT MUTAGEN 665
FT /note="M->K: In mus308-660 mutant; mutant females produce
FT ventralized egg shells."
FT /evidence="ECO:0000269|PubMed:16888338"
FT MUTAGEN 811
FT /note="Q->H: In mus308-2255 mutant; mutant females produce
FT ventralized egg shells; when associated with D-455."
FT /evidence="ECO:0000269|PubMed:16888338"
SQ SEQUENCE 1051 AA; 117332 MW; 15B051F526844D8A CRC64;
MANKHNLCKK RSLDLSEEST SESHAKRQCT ENLFWPEGED DDSFFSNAHL EDLLDGRKEE
LFGTQATTST NKMTQSGSDD GLGLFADTSF PSAQSVPPNS ASKPDEASAP TDKHQIDLAD
EENADKLFKK INLNDLSIAE MEDIFHGADD FSDPMVQNTQ LFLDAMTFKK PKTPEKLLAP
LKDDSMSFIS KSVIEGLVQG TQYVTCEELK NQSLLDPVNW ETQAFADFEK NNQDIDKFPS
KGEFYGLPDK VKKMILEHKG INSLYEWQDE CLNLPAIRQR KNLIYALPTS GGKTLVAEIL
MLRELLCRER NVLFILPYVS IVQEKVSAMS PFAIDLDFIV EEYTAGKGKC PPQPRRKRRS
LFIASIEKGA VLMDSLIDVQ RPHEIGLVVV DELHLIGEKG RGATLEAFLT KVMFLNANIQ
IVGMSATIGN LSEISSFLNA DVYTRGFRPV ELKEYIKCGP DLLEINSAGQ TLEEIFVPSR
SVEYNYSEAV KRADPDHLAG LISECAPEHC CLVFCPSRKN CENVALLLSR IVPKHKFFEH
RRSEKLDLMD ALDKMCGILS PVLAKTLPYG IAYHHSGLTT DERKYIETAY RFGVVTVICC
TSTLAAGVNL PAKRVIIRAP YVGQEFLTLC KYKQMVGRAG RAGLGEAGES ILIAQSKDNL
LVGQMLFSPM DKALSSLDQN EAVGLQSLIL SVVGLNLAEC RRDLNRLVNS TLLSVQAKSL
EVAVNEIVLR ILREMFKNKV LQLAEPQAKS KINSSDIITS QDVSQANRPA GDRRLLIGQS
TPFKLTNIGR AAFKAGIDYK RANAIHKELK QAQQQLILTN YLHLLYLVVC FNSNERGDEL
FPADASILFG VYTSLPLDSQ AMFKQLGFTE AHAARLFKTQ SVQGPLSLQL NRLYKVLILA
DILNLLPIPS VASKYNVERG TLQHLISQST AAASAIVRLC EELEEFWCYK PLFERILHKM
DRCGTFELEP LMELPAVKIN RARQLYAAGF QTIGDIARVR PSHLVQSLEH MPLRVATEIV
SAAKIILMKK LDHLEEETEN LKDCLKTSDK N
