GenomeNet

Database: UniProt
Entry: Q6AYJ1
LinkDB: Q6AYJ1
Original site: Q6AYJ1 
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   16-OCT-2019, entry version 117.
DE   RecName: Full=ATP-dependent DNA helicase Q1;
DE            EC=3.6.4.12;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: DNA helicase that may play a role in the repair of DNA
CC       that is damaged by ultraviolet light or other mutagens. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that
CC       unwinds single- and double-stranded DNA in a 3'-5' direction (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Interacts with EXO1 and MLH1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000305}.
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   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; KOG0351; Eukaryota.
DR   eggNOG; COG0514; LUCA.
DR   GeneTree; ENSGT00940000157013; -.
DR   HOGENOM; HOG000044388; -.
DR   InParanoid; Q6AYJ1; -.
DR   KO; K10899; -.
DR   OMA; IKLCYVT; -.
DR   OrthoDB; 445763at2759; -.
DR   PRO; PR:Q6AYJ1; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000012602; Expressed in 10 organ(s), highest expression level in testis.
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:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0036310; F:annealing helicase activity; 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: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   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; Complete proteome; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    621       ATP-dependent DNA helicase Q1.
FT                                /FTId=PRO_0000205052.
FT   DOMAIN      100    275       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      296    451       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     113    120       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       219    222       DEVH box.
FT   MOD_RES     514    514       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     522    522       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     597    597       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     602    602       Phosphoserine.
FT                                {ECO:0000244|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
//
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