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Database: UniProt
Entry: H2LID7_ORYLA
LinkDB: H2LID7_ORYLA
Original site: H2LID7_ORYLA 
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
//
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