ID A0A287BGJ9_PIG Unreviewed; 649 AA.
AC A0A287BGJ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN Name=RECQL {ECO:0000313|Ensembl:ENSSSCP00000055660.1,
GN ECO:0000313|VGNC:VGNC:92195};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000055660.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000055660.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000055660.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000055660.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR AlphaFoldDB; A0A287BGJ9; -.
DR PaxDb; 9823-ENSSSCP00000000610; -.
DR Ensembl; ENSSSCT00000059872.3; ENSSSCP00000055660.1; ENSSSCG00000000580.5.
DR VGNC; VGNC:92195; RECQL.
DR eggNOG; KOG0353; Eukaryota.
DR GeneTree; ENSGT00940000157013; -.
DR OMA; FKLSTMV; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000580; Expressed in tonsil and 44 other cell types or tissues.
DR ExpressionAtlas; A0A287BGJ9; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IEA:Ensembl.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0031297; P:replication fork processing; IEA:Ensembl.
DR CDD; cd18015; DEXHc_RecQ1; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 100..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 300..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 601..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..52
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 606..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 73877 MW; 7B17867E93B1FB93 CRC64;
MASISALSEE LDSITNELHA VDIQIQELLE RQQELIQKKK ILEKRIKQCS EDPDAGESSE
YDSSPASWNK EDFPWSGKVK EVLQNIFKLQ KFRPLQLETI NVTMSGKEVF LVMPTGGGKS
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
NSKLKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAIDE VHCCSQWGHD FRPDYKALGI
LKRQFPNTSL IGLTATATSH VLKDAQKILC VEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQKLGIH AGAYHANMEP EDKTTVHRRW
SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDT KADCILYYGF
GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRVLIAQ HFDEVWSPEE CNKMCDNCCK
DTSFERKNIT AYCRDLVKIL KQAEELNEKL TPLKLIDSWL GKGAAKLRVA GIAPPTLPRE
DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHVITMQV KRPTQSCFRI
ESPQSCHSEG ADKKREEKNS SNYQKSAHML QQSNCNKTIG AKKRKIDNA
//
