DDX46_DICDI
ID DDX46_DICDI Reviewed; 1151 AA.
AC Q553B1; Q23909; Q869K2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent RNA helicase ddx46;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase helB1;
DE AltName: Full=DEAD box protein 46;
GN Name=helB1; Synonyms=ddx46, hel2A; ORFNames=DDB_G0275443;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 490-1066.
RC STRAIN=AX2;
RX PubMed=7695838; DOI=10.1515/bchm3.1994.375.11.759;
RA Mahal B., Nellen W.;
RT "Developmental regulation of DEAD box proteins and cloning of putative RNA
RT helicase genes from Dictyostelium discoideum.";
RL Biol. Chem. Hoppe-Seyler 375:759-763(1994).
CC -!- FUNCTION: ATP-dependent RNA helicase which may be involved spliceosome
CC assembly and in nuclear splicing. {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 {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. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69472.1; -; Genomic_DNA.
DR EMBL; X81823; CAA57417.1; -; mRNA.
DR RefSeq; XP_643509.1; XM_638417.1.
DR AlphaFoldDB; Q553B1; -.
DR SMR; Q553B1; -.
DR STRING; 44689.DDB0191329; -.
DR PaxDb; Q553B1; -.
DR PRIDE; Q553B1; -.
DR EnsemblProtists; EAL69472; EAL69472; DDB_G0275443.
DR GeneID; 8620090; -.
DR KEGG; ddi:DDB_G0275443; -.
DR dictyBase; DDB_G0275443; helB1.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_1_1; -.
DR InParanoid; Q553B1; -.
DR OMA; CGLGVQT; -.
DR PhylomeDB; Q553B1; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q553B1; -.
DR Proteomes; UP000002195; Chromosome 2.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1151
FT /note="ATP-dependent RNA helicase ddx46"
FT /id="PRO_0000327435"
FT DOMAIN 540..718
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 729..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 509..537
FT /note="Q motif"
FT MOTIF 666..669
FT /note="DEAD box"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1151 AA; 130685 MW; C88E8CB48AA71D02 CRC64;
MDEYDKKRRL EHGGSDRSRS SNDNRNSHGS SGNNYRDDRK DDRYYRDDRS HYNNNNNNNN
NNNNNNNNNN GNGYRDDRNY SSQNKYQNHH QQSPPQQQQQ QQNSSYVPSQ PPQQQTQTQQ
QPHIQAPPPA KPRKSRFDQA PETIPIQAPQ QPPMISNQPI FKQQPMYQQP MYQQKQQQPQ
PPIFQQQQKQ QQPPIFQHHQ PPPIYQQPPV YQQQQQQQQP VFQQQQQQRV ATEAIQFQQT
PQQLAIEQER LKQERENEKK IEQANLEEEM KKRREKVEQW RKQKLEQELK ASGSSNSGST
SSPPTTTTTT TKTTAATTTA TTSPLTIPSQ QQQTATTSPI KKKWSLEEEE ETAQPLVNTN
IEQKEIKLPP TANIPAAAAT TTSATINTTT IKQSIEEDDD IDPLDAYMEN LNKEANLNLK
KSKTSQMIDD DEKLEEESEG EDDGKDKTIK KGKKEMLHTD HTSIKYAEFQ KNFYIEVPVL
ANMTETEVLD FRSELGVKIT GKDCPKPIQS WAQAGLTEKV HLLLKKFQYE KPTSIQAQTI
PAIMNGRDLI GIARTGSGKT LAFLLPMFRH ILAQPKSAPG EGMIALIMSP TRELALQIHV
ECKKFSKVLG LRTACVYGGA SISEQIAELK RGADIVVCTP GRMIDILCAN NRRITNLRRV
TFLVLDEADR MFDMGFGPQI NCIVDSIRPD RQTIMFSATF PPKVENVAKK ILNKPLEIIA
GGRSIVSSDI EQFVEVRPTE TRFRRLIELL SIWYHKGQIL IFTNRQETTD NLYRQLSNSQ
YQCLSLHGSK DQTDRDETIS DFKNKVKTIL IATPLASRGL DIKDLNLVVN FDCPDHLEDY
VHRVGRTGRA GNRGTAYTFI TPDEERFSSS IIKALEQSGS KVPDELRKLN DTYEKKRKEG
KDVLLAPTGF TGRGHKFDAA EEDKKNIERK QQRKAYGIEE EEEEEDEDKE KAEKEKLAAA
SAEKEKQLLS EKEKLDPATT NTIVIPGVDG TIITPSSLLQ TDPSVPVGQQ AINQIFGISQ
VTSSEEAIKK LQLAAQLGMK GNIQKLNNQI TPLNQTHFIE ELEINDYSQQ ARWKVTHKDA
LLEITNFTNT TITTKGTFFP PNKIPAPGER KLYLYIEGPS DASVKNAKSD IKKILDEVQS
THQSTGKYSV F
