RECQ1_PONAB
ID RECQ1_PONAB Reviewed; 649 AA.
AC Q5RF63;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857298; CAH89594.1; -; mRNA.
DR RefSeq; NP_001124706.1; NM_001131234.1.
DR AlphaFoldDB; Q5RF63; -.
DR SMR; Q5RF63; -.
DR STRING; 9601.ENSPPYP00000004971; -.
DR GeneID; 100171554; -.
DR KEGG; pon:100171554; -.
DR CTD; 5965; -.
DR eggNOG; KOG0353; Eukaryota.
DR InParanoid; Q5RF63; -.
DR Proteomes; UP000001595; Unplaced.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
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; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..649
FT /note="ATP-dependent DNA helicase Q1"
FT /id="PRO_0000205051"
FT DOMAIN 100..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 300..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 597..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..222
FT /note="DEVH box"
FT COMPBIAS 606..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q6AYJ1"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46063"
SQ SEQUENCE 649 AA; 73483 MW; B270A29E121ABA58 CRC64;
MASVSALTEE LDSITSELHA VEIQIQELTE RQEELIQKKK VLTKKIKQCL EDSDAGASNE
YDSSPAAWNK EDFPWSGKVK DVLQNVFKLQ KFRPLQLETI NVTMAGKEVF LVMPTGGGKG
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI
LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLRNLGIH AGAYHANLEP EDKTTVHRKW
SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF
GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRLLMAQ HFDEVWNSEA CNKMCDNCCK
DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE
DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRV
ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA
