ID H2Q4Q4_PANTR Unreviewed; 875 AA.
AC H2Q4Q4; A0A2J8L0L1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN Name=DDX10 {ECO:0000313|EMBL:JAA07783.1,
GN ECO:0000313|Ensembl:ENSPTRP00000007324.3,
GN ECO:0000313|VGNC:VGNC:11337};
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:ENSPTRP00000007324.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000007324.3, 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:JAA07783.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA07783.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA36477.1}, Skin {ECO:0000313|EMBL:JAA22582.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA18229.1};
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:ENSPTRP00000007324.3}
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|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.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; AACZ04006805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04006806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04006807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04006808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04006809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01003555; JAA07783.1; -; mRNA.
DR EMBL; GABF01003916; JAA18229.1; -; mRNA.
DR EMBL; GABD01010518; JAA22582.1; -; mRNA.
DR EMBL; GABE01008262; JAA36477.1; -; mRNA.
DR RefSeq; XP_009422398.1; XM_009424123.2.
DR STRING; 9598.ENSPTRP00000007324; -.
DR PaxDb; 9598-ENSPTRP00000007324; -.
DR Ensembl; ENSPTRT00000007936.4; ENSPTRP00000007324.3; ENSPTRG00000004256.4.
DR GeneID; 451534; -.
DR KEGG; ptr:451534; -.
DR CTD; 1662; -.
DR VGNC; VGNC:11337; DDX10.
DR eggNOG; KOG0343; Eukaryota.
DR GeneTree; ENSGT00550000074980; -.
DR HOGENOM; CLU_003041_26_1_1; -.
DR OMA; FLWRQKQ; -.
DR OrthoDB; 149428at2759; -.
DR TreeFam; TF315215; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004256; Expressed in fibroblast and 21 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; 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:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17941; DEADc_DDX10; 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; 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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF775; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
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:UP000002277};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 69..97
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 100..274
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 287..448
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..97
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 20..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 100823 MW; 330BF9D65D1EC1DE CRC64;
MGKTADSPGS GARPDPVRNF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER ESISRLMQNY
EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI GLALQGKDVL GAAKTGSGKT
LAFLVPVLEA LYRLQWTSTD GLGVLIISPT RELAYQTFEV LRKVGKNHDF SAGLIIGGKD
LKHEAERINN INILVCTPGR LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAVI
ENLPKKRQTL LFSATQTKSV KDLARLSLKN PEYVWVHEKA KYSTPATLEQ NYIVCELKQK
ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGV SILALHGRQQ QMRRMEVYNE
FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI HRAGRTARYK EDGEALLILL
PSEKAMVQQL LQKKVPVKEI KINPEKLIDV QKKLESILAQ DQDLKERAQR CFVSYVRSVY
LMKDKEVFDV SKLPIPEYAL SLGLAVAPRI RFLQKMQKQP TKELVMSQAD KVIEPRAPSL
TNDEVEEFRA YFNEKMSILQ KGGKRLEGTE HRQDNDTGNE EQEEEEDDEE EMEEKLAKAK
GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKD EKTLQKKEPS
KSSIKKKVTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW PQMQKSAIKD AEEDDDTGGI
NLDKAKERLQ EEDKFDKEEY RKKIKAKHRE KRLKEREARR EANKRQAKAK DEEEAFLDWS
DDDDDDDDGF DPSTLPDPDK YRSSEDSDSE DMENKISDTK KKQGMKKRSN SEVEDVGPTS
HNRKKAKWDT LEPLDTGLSL AEDEELVLHL LRSQS
//
