ID   RECQ1_RAT               Reviewed;         621 AA.
AC   Q6AYJ1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000250|UniProtKB:P46063};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P46063};
DE   AltName: Full=DNA-dependent ATPase Q1;
DE   AltName: Full=RecQ protein-like 1;
GN   Name=Recql; Synonyms=Recql1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: DNA helicase that may play a role in the repair of DNA that
CC       is damaged by ultraviolet light or other mutagens. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that unwinds
CC       single- and double-stranded DNA in a 3'-5' direction.
CC       {ECO:0000250|UniProtKB:P46063}.
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:P46063};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57667, ChEBI:CHEBI:61404;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51909;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC   -!- SUBUNIT: Interacts with EXO1. Interacts with MLH1.
CC       {ECO:0000250|UniProtKB:P46063}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46063}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC079026; AAH79026.1; -; mRNA.
DR   RefSeq; NP_001012098.1; NM_001012098.1.
DR   RefSeq; XP_006237683.1; XM_006237621.2.
DR   RefSeq; XP_017448156.1; XM_017592667.1.
DR   AlphaFoldDB; Q6AYJ1; -.
DR   SMR; Q6AYJ1; -.
DR   STRING; 10116.ENSRNOP00000060671; -.
DR   iPTMnet; Q6AYJ1; -.
DR   PhosphoSitePlus; Q6AYJ1; -.
DR   PaxDb; Q6AYJ1; -.
DR   PRIDE; Q6AYJ1; -.
DR   Ensembl; ENSRNOT00000065576; ENSRNOP00000060671; ENSRNOG00000012602.
DR   GeneID; 312824; -.
DR   KEGG; rno:312824; -.
DR   UCSC; RGD:1311071; rat.
DR   CTD; 5965; -.
DR   RGD; 1311071; Recql.
DR   eggNOG; KOG0353; Eukaryota.
DR   GeneTree; ENSGT00940000157013; -.
DR   InParanoid; Q6AYJ1; -.
DR   OMA; FKLSTMV; -.
DR   OrthoDB; 445763at2759; -.
DR   PRO; PR:Q6AYJ1; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000012602; Expressed in testis and 20 other tissues.
DR   ExpressionAtlas; Q6AYJ1; baseline and differential.
DR   Genevisible; Q6AYJ1; RN.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; ISO:RGD.
DR   GO; GO:1990814; F:DNA/DNA annealing activity; ISO:RGD.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
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   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..621
FT                   /note="ATP-dependent DNA helicase Q1"
FT                   /id="PRO_0000205052"
FT   DOMAIN          100..275
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          296..451
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           219..222
FT                   /note="DEVH box"
FT   BINDING         113..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         514
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   MOD_RES         522
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   MOD_RES         597
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   MOD_RES         602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   621 AA;  69642 MW;  FA8F6B04ADA341C1 CRC64;
     MASIPALTDE LESVSSELHA VDIQIQELTE RQHELLQRKS VLTKRIKQCL EDSAAEASGD
     CDTSPAAWSK EDFPWSGKVK HVLRDVFKLQ KFRPLQLETV NATMARKDIF LVMPTGGGKS
     LCYQLPALCS DGFTLVICPL ISLMEDQLMV LQQLGISATM LNSSSSKEHV KCVHTEMMNK
     NSHLKLIYVT PEKIAKSKMF MSRLEKAYEA GRLTGVAVDE VHCCSQWGHD FRPDYKALGI
     LKRQFPNISL IGLTATATNH VLKDAQKILC VEKCLTFTAS FNRPNLYYEV RQKPSSAEDF
     IENIANLING RYKGKSGIIY CFSQKDSEQV TISLQKLGVR AGTYHANMEP EDRTKVHTQW
     SANELQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDW RADCILYYGF
     GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRALIAQ HFDEVWNADA CNKMCDNCCK
     DDSFEKKNIT EHCQALIKIL KQAEGLNEKL TPLKLIDAWM GKGAAKFRVA GVAVPALPRE
     DLEKIIVHAL LQQYLKEDYS FTAYATISYL KVGPRASLLS NEGHAVTMQV KRSTQSSVRA
     ASPEACEVDS KGKEKSSAVL C