DDX10_DICDI
ID DDX10_DICDI Reviewed; 878 AA.
AC Q54Q94;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx10;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 10;
GN Name=ddx10; ORFNames=DDB_G0284017;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase which may be involved in
CC ribosome biogenesis. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000059; EAL65432.1; -; Genomic_DNA.
DR RefSeq; XP_638786.1; XM_633694.1.
DR AlphaFoldDB; Q54Q94; -.
DR SMR; Q54Q94; -.
DR STRING; 44689.DDB0234197; -.
DR PaxDb; Q54Q94; -.
DR PRIDE; Q54Q94; -.
DR EnsemblProtists; EAL65432; EAL65432; DDB_G0284017.
DR GeneID; 8624375; -.
DR KEGG; ddi:DDB_G0284017; -.
DR dictyBase; DDB_G0284017; ddx10.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q54Q94; -.
DR OMA; YDKMFER; -.
DR PhylomeDB; Q54Q94; -.
DR PRO; PR:Q54Q94; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 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 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..878
FT /note="Probable ATP-dependent RNA helicase ddx10"
FT /id="PRO_0000327412"
FT DOMAIN 172..346
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 372..521
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 141..169
FT /note="Q motif"
FT MOTIF 294..297
FT /note="DEAD box"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..649
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..850
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 878 AA; 100358 MW; 6C2C8B6AC14AF46F CRC64;
MNKDKSKQKP QKKENNNNNN KNNNNNNNKT ENNKTNKDFT KNKFDKDAKI DKVDNKKIFH
NRSSQKRIAK LKKIELQKKP LTLKLNEIKS IEQRLIDEAP QRGTNPLANI SSTTATTTTT
TATKNDKEKE KEYKIDYPSA TDFKDLPISQ LTLKALTESK FLKLTDIQRA SLPHTLCGRD
ILGAAKTGSG KTLSFILPIL ETLWRNRWGR DDGIGAIVLS PTRELAIQIF DVLKAVGKYH
TFSAGLIIGG RNVQQEKDKI NAMNILIATP GRLLQHMDET YGFDCSNLKI LVLDEADRIL
DLGFSKCLNS IVENLPRERQ TLLFSATQTK SIRDLARLSL QEPEYISVYE KDITTTPQNL
TQTLCVIPLE MKLNMLFSFI KTHLTSKIIV FFASCKQVRF AHETFKLLNP GTTLFPLHGK
MKQWTRLEVF EDFCKKKAGT LFATDIAARG LDFPAVEWVI QVDCPDDIET YIHRVGRTAR
NDAPGQSITI LLPSEKDGMV NLMEKQKMKF EILEPNPEKL VSIDSKLSSF LSEKTDLKYL
AQKSFVSYLR SVYRQSNKEI FKIQELNINE FSKSLGLLGT PNIQFGKASA DSKNKSFVVS
NIQKQLKDKK SKGEKDIDSS DDDDDDEERN KIGNSDDEDS EDDSDFQDDS DDDNKKVTKQ
QPKTNIEKLF DRKNANVMSE TYQKLRTKEE DEEDDSMFVV KRRDHDLDNL DIVKRLSRKE
NKEKNFINDP TKLKFQESTS VPKDGKLPTS YIEKVKSEVE KGDVQDKILL KERLKRKKLK
LQSKELRKQS GGGATGDDEE ESVAYFVPPG EKDPYENGEN DSDDESNDDD VWGQEYNSDD
DDDDEESESE EQPKPITKKR TLEDHEESAL KFLKKNRI
