ID H2LID7_ORYLA Unreviewed; 844 AA.
AC H2LID7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN Name=ddx24 {ECO:0000313|Ensembl:ENSORLP00000005760.3};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000005760.3, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000005760.3, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000005760.3,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000005760.3}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000005760.3};
RG Ensembl;
RL Submitted (JUL-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. DDX24/MAK5
CC subfamily. {ECO:0000256|ARBA:ARBA00038457}.
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DR RefSeq; XP_011483142.1; XM_011484840.1.
DR RefSeq; XP_011483149.1; XM_011484847.1.
DR AlphaFoldDB; H2LID7; -.
DR STRING; 8090.ENSORLP00000005760; -.
DR Ensembl; ENSORLT00000005761.3; ENSORLP00000005760.3; ENSORLG00000004581.3.
DR GeneID; 101158676; -.
DR KEGG; ola:101158676; -.
DR CTD; 57062; -.
DR eggNOG; KOG0347; Eukaryota.
DR GeneTree; ENSGT00550000074847; -.
DR HOGENOM; CLU_003041_13_1_1; -.
DR InParanoid; H2LID7; -.
DR OrthoDB; 56712at2759; -.
DR TreeFam; TF105837; -.
DR Proteomes; UP000001038; Chromosome 22.
DR Bgee; ENSORLG00000004581; Expressed in animal zygote and 14 other cell types or tissues.
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 CDD; cd17946; DEADc_DDX24; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24031:SF91; ATP-DEPENDENT RNA HELICASE DDX24; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 216..244
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 248..515
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 563..708
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 64..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 216..244
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 64..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 95238 MW; C67D5A56792D8B78 CRC64;
MKTKKVEAQN KNSSFRLKTR SIRAKGTWKA VEIDPSVFSE QGLEGLVCFE ELRDYRLIDS
EKAAAKQLQR EKKVAKKRKV AEEDEAGETP AEPAKKKAKK KKKGKKVAPK ESVGSESGDA
IGEDKAVDKE AGKDEISEDL CEQEHPPKRE KIRKKKLKNH SEKDPVTEEQ PKLDSPSETK
GLNKGQNKTK PIKKQTKNWT SAALCGSDDD KQSDVSAWKD LFVPSSVLKA LSSLGFESPT
PIQALALPPA IRDHMDVLGA AETGSGKTLA FGIPMIHAIL EWKRGTEQSL HDNIDKTPPK
VVSLYLPSVE ESAKSEDEST AVGNQEGSVE ASDEEDSSAE DGSEDQDEKT GSVCTVKNAE
RCVEEQLAGG RSRPLLGMVL TPTRELAVQV KHHIDAVTKF TDIKTAILVG GMAQQKQKRM
LKRCPEIIIA TPGRLWDLIK EKHPHLLNLR HLRCLVIDEA DRMVERGHFA ELESLLEMLN
TTHFNPKRQT FVFSATLTLT HSLPSRLLQK KKNLEKRSKL DILIEKVGIK SKPKVIDLTR
KEATVETLTE TQIHCQKDEK DFYLYYFLLQ YPGRTMVFAN SIDCIKRLNS LLVILECNPL
PLHANMHQKQ RLKNLERFAE RESGVLLTTD VAARGLDIPD VQHVIHYQVP RTSETYVHRS
GRTARATKEG LSLLLVGPDD MINLKKIYKT LEKDEESPMF PIETKCLEAI KERVNLARKI
EKIEFYNSRE KHHDSWFKQA AEALEVDLDD DLLLGGAKDE DEEREQQKKV KGMKRHLKHL
ISQPIFKHAM KTKYPTQMGK LPLAHMPHAT MESALTRVSN EKKNQKAKRG FSQPCKQRRG
KGKQ
//