DDX24_PONAB
ID DDX24_PONAB Reviewed; 859 AA.
AC Q5RDL2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP-dependent RNA helicase DDX24;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 24;
GN Name=DDX24;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase. {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; CR857893; CAH90145.1; -; mRNA.
DR RefSeq; NP_001125038.1; NM_001131566.1.
DR AlphaFoldDB; Q5RDL2; -.
DR STRING; 9601.ENSPPYP00000006931; -.
DR Ensembl; ENSPPYT00000007205; ENSPPYP00000006931; ENSPPYG00000006095.
DR GeneID; 100171919; -.
DR KEGG; pon:100171919; -.
DR CTD; 57062; -.
DR eggNOG; KOG0347; Eukaryota.
DR GeneTree; ENSGT00550000074847; -.
DR HOGENOM; CLU_003041_13_1_1; -.
DR InParanoid; Q5RDL2; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR TreeFam; TF105837; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005730; C:nucleolus; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..859
FT /note="ATP-dependent RNA helicase DDX24"
FT /id="PRO_0000291857"
FT DOMAIN 224..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 578..723
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 61..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..220
FT /note="Q motif"
FT MOTIF 471..474
FT /note="DEAD box"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 71
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 808
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR7"
SQ SEQUENCE 859 AA; 96419 MW; A951FBCE0C5324A6 CRC64;
MKLKDTKSRP KQSSYGKFQT KGIKVVGKWK EVKIDPNMFA DGQMDDLVCF EELTDYQLVS
PAKNPSSLFS KEAPKRKAQA VSEEEEEEEG ESSSPKKKIK LKKSKNVATE GTSTQKEFEV
KDPELEAQGD GMVCDDPEAG EMTSENLVQT APKKKKNKAK KGLEPSQSTA AKVPKKAKTW
IPEVHDQKAD VSAWKDLFVP RPVLRALSFL GFSAPTPIQV LTLAPAIRDK LDILGAAETG
SGKTLAFAIP MIHAVLQWQK RNAAPPPSNT EAPPGETRPE AGAETRSPGK AEAESDALPD
DTVIESEALP SDTAAEARAK TGGTVSDQAL LFGDDDAGEG PSSLIREKPV PKQNENEEEN
LDKEQTGNLK QELDDKSATC KTYPKRPLLG LVLTPTRELA VQVKQHIDAV ARFTGIKTAI
LVGGMSTQKQ QRMLNRRPEI VVATPGRLWE LIKEKHYHLR NLRQLRCLVV DEADRMVEKG
HFAELSQLLE MLNDSQYNPK RQTLVFSATL TLVHQAPARI LHKKHTKKMD KTAKLDLLMQ
KIGMRGKPKV IDLTRNEATV ETLTETKIHC ETDEKDFYLY YFLMQYPGRS LVFANSISCI
KRLSGLLKVL DIMPLTLHAC MHQKQRLRNL EQFARLEDCV LLATDVAARG LDIPKVQHVI
HYQVPRTSEI YVHRSGRTAR ATNEGLSLML IGPEDVINFK KIYKTLKKDE DIPLFPVQTK
YMDVVKERIR LARQIEKSEY RNFQACLHNS WIEQAAAALE IELEEDMYKG GKADQQEERR
RQKQMKVLKK ELRHLLSQPL FTESQKTKYP TQSGKPPLLV SAPSKSESAL SCLSKQRKKK
TKKPKEPQPE QPQPSTSAN
