ID H2QIL6_PANTR Unreviewed; 670 AA.
AC H2QIL6; A0A2J8M209;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN Name=DDX18 {ECO:0000313|EMBL:JAA08506.1,
GN ECO:0000313|Ensembl:ENSPTRP00000021219.2,
GN ECO:0000313|VGNC:VGNC:10761};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000021219.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000021219.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA08506.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA08506.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA37197.1}, Skin {ECO:0000313|EMBL:JAA27869.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA16224.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000021219.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556,
CC ECO:0000256|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000256|ARBA:ARBA00024357}.
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DR EMBL; AC172375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01002832; JAA08506.1; -; mRNA.
DR EMBL; GABF01005921; JAA16224.1; -; mRNA.
DR EMBL; GABD01005231; JAA27869.1; -; mRNA.
DR EMBL; GABE01007542; JAA37197.1; -; mRNA.
DR RefSeq; XP_515753.2; XM_515753.6.
DR STRING; 9598.ENSPTRP00000021219; -.
DR PaxDb; 9598-ENSPTRP00000021219; -.
DR Ensembl; ENSPTRT00000023008.3; ENSPTRP00000021219.2; ENSPTRG00000012391.3.
DR GeneID; 459566; -.
DR KEGG; ptr:459566; -.
DR CTD; 8886; -.
DR VGNC; VGNC:10761; DDX18.
DR eggNOG; KOG0342; Eukaryota.
DR GeneTree; ENSGT00680000100037; -.
DR HOGENOM; CLU_003041_26_5_1; -.
DR OMA; LMEFHSQ; -.
DR OrthoDB; 149428at2759; -.
DR TreeFam; TF300471; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012391; Expressed in lung and 21 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR CDD; cd17942; DEADc_DDX18; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 210..385
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 399..569
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 27..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 75493 MW; 1D04AC82B2C64BAC CRC64;
MSHLPMKLLR KKIEKRNLKL RQRNLKLQGA SNLTLSETQN GDVSEETMGS RKVKKSKQKP
MNVGLSETQN GDVSQEAVEN VKVKKSPQKS SVLTNGEAAM QSSNSESKKK KKKKRKMVND
AEPDTKKAKT ENKGKSEEES AETPKETENN VDKPDNDEDE SEVPNLPLGL TGAFEDTSFA
SLCNLVNENT LKAIKEMGFT NMTEIQHKSI RPLLEGRDLL AAAKTGSGKT LAFLIPAVEL
IVKLRFMPRN GTGVLILSPT RELAMQTFGV LKELMTHHVH TYGLIMGGSN RSAEAQKLAN
GINIIVATPG RLLDHMQNTP GFMYKNLQCL VIDEADRILD VGFEEELKQI IKLLPTRRQT
MLFSATQTRK VEDLARISLK KEPLYVGVDD DKANATVDGL EQGYVVCPSE KRFLLLFTFL
KKNRKKKLMV FFSSCMSVKY HYELLNYIDL PVLAIHGKQK QNKRTTTFFQ FCNADSGTLL
CTDVAARGLD IPEVDWIVQY DPPDDPKEYI HRVGRTARGL NGRGHALLIL RPEELGFLRY
LKQSKVPLSE FDFSWSKISD IQSQLEKLIE KNYFLHKSAQ EAYKSYIRAY DSHSLKQIFN
VNNLNLPQVA LSFGFKVPPF VDLNVNSNEG KQKKRGGGGG FGYQKTKKVE KSKIFKHISK
KSSDSRQFSH
//
