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Database: UniProt
Entry: A0A2R9B0Q1_PANPA
LinkDB: A0A2R9B0Q1_PANPA
Original site: A0A2R9B0Q1_PANPA 
ID   A0A2R9B0Q1_PANPA        Unreviewed;       998 AA.
AC   A0A2R9B0Q1;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   Name=RECQL5 {ECO:0000313|Ensembl:ENSPPAP00000022693.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000022693.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000022693.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000022693.1}
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   EMBL; AJFE02042220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02042221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9B0Q1; -.
DR   STRING; 9597.ENSPPAP00000022693; -.
DR   Ensembl; ENSPPAT00000045505.1; ENSPPAP00000022693.1; ENSPPAG00000034423.1.
DR   GeneTree; ENSGT00940000157800; -.
DR   Proteomes; UP000240080; Chromosome 17.
DR   Bgee; ENSPPAG00000034423; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR   GO; GO:0097550; C:transcription preinitiation complex; 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:0003678; F:DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR   GO; GO:0072757; P:cellular response to camptothecin; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0051304; P:chromosome separation; IEA:Ensembl.
DR   GO; GO:1990506; P:mitotic DNA-templated DNA replication; IEA:Ensembl.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0034244; P:negative regulation of transcription elongation by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
DR   CDD; cd18014; DEXHc_RecQ5; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 6.10.250.2460; -; 1.
DR   Gene3D; 6.10.250.3140; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; IPR010716; RECQ5.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF159; ATP-DEPENDENT DNA HELICASE Q5; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF06959; RecQ5; 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; PS00690; DEAH_ATP_HELICASE; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
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:UP000240080}.
FT   DOMAIN          39..213
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          241..403
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          613..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  109555 MW;  AF49109C109EEE0E CRC64;
     MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV CMPTGAGKSL
     CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL NSKLSARERK ELLADLEREK
     PQTKILYITP EMAASSSFQP TLNSLVSRHL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR
     SRLGHAPCVA LTATATPQVQ EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG
     NLKDFCLKAL GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL
     VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA GRDGKPSWCR
     LYYSRNDRDQ VSFLIRKEVA KLQVKRGNKA SDKATIMAFD ALVTFCEELG CRHAAIAKYF
     GDALPACAKG CDHCQNPTAV RRQLEALERS SSWSKTCIGP SQGNGFDPEL YEGGRKGYGG
     FSRYDEGSGG SGYEGRDEAH KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR
     RIPRLTVKAR EHCLRLLEEA LSSNHQSTRT TDEADLRAKA MELEHETFRN AKVANLYKAS
     VLKKVADIHR ASKDGQPYDM GGSAKSCNAQ AEPPEPNEYD IPPASHVYSL KPKRVGAGFP
     KGSCPFQTAT ELMETTRIGE QAPQPERGGE HEPPSRPCGL LDEDGSEPLP GPRGEVPGGS
     AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ QLLATAAHKD SQSIARFFCR RVESLALLAS
     APEAEGACPS CEGVQGPPMA PEKYTEEEDG AGGHSPAPPQ TEECLREREP PGPSAVITCP
     PRDQGTPEVQ PTPAKDTWKG KRPRSQQENP ESQPQKRPRP SAKPSVVAEV KGSISASEQG
     TLNPTAQDPF QLSAPGVSLK EAANVVVKCL TPFYKEGKFA SKELFKGFAR HLSHLLTQKT
     SPGRSVKEEA QNLIRHFFHG RARCESEADW HGLCGPQR
//
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