DHX8_DICDI
ID DHX8_DICDI Reviewed; 1160 AA.
AC Q54F05;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP-dependent RNA helicase dhx8;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 8;
GN Name=dhx8; Synonyms=prp22; ORFNames=DDB_G0291183;
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: Facilitates nuclear export of spliced mRNA by releasing the
CC RNA from the spliceosome. {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 -!- SUBUNIT: Identified in the spliceosome complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000175; EAL61875.1; -; Genomic_DNA.
DR RefSeq; XP_635385.1; XM_630293.1.
DR AlphaFoldDB; Q54F05; -.
DR SMR; Q54F05; -.
DR STRING; 44689.DDB0233399; -.
DR PaxDb; Q54F05; -.
DR EnsemblProtists; EAL61875; EAL61875; DDB_G0291183.
DR GeneID; 8628033; -.
DR KEGG; ddi:DDB_G0291183; -.
DR dictyBase; DDB_G0291183; dhx8.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_2_2_1; -.
DR InParanoid; Q54F05; -.
DR OMA; DPMVAPE; -.
DR PhylomeDB; Q54F05; -.
DR PRO; PR:Q54F05; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; ISS:dictyBase.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..1160
FT /note="ATP-dependent RNA helicase dhx8"
FT /id="PRO_0000330832"
FT DOMAIN 202..274
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 518..681
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 699..879
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 75..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 628..631
FT /note="DEAH box"
FT COMPBIAS 75..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 531..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1160 AA; 131707 MW; FE7E72B8D93617FA CRC64;
MDKLERIELE SQVCNELERF IGSGDKLLAE FVIGLADENP KLKDFNKAIS ENVPDFPESL
SSHLFNLIEK MKKKTTTTTN NNNNNNNNNT NTAKTTTTTT TTTTTTNNNN YKESEWEETK
LNSNSNNQKK NQFPGLSIPN KVEWDQGKIV DVPIDDEKTK EELKRKQQDM DREFEREQRE
KRDRDREQQN KRREIDKEPI LYKIYDGKVS SINDYGCFVT LEGIAGRRDG LVHISQILSG
RTKLNHPSDV VKRNQQVKVK ILSVASSKIS LSMKDVDQST GRDLNPQQNI QSIISTNSTN
NRSNPFKPNN NNNNSSNNNN NDDDDKYTTS KNRKRIASPD RWGYKQLIAS GILSVPEMPN
YDKEVGLVNH DEEQPEEDFD IERNEDEPQF LKGTRMNMQQ LSPIKIVKKP NGSLQRAAST
QTALSKERKE EKNQQRNEMM DSIPKDLSLP WHDPMPEAGE RHLAQEIRSI AGQGIDTEIP
EWKKVTQGSH IQYGKATSRS IKEQRESLPI FPLREAFLQA VSEHQLLVVI GETGSGKTTQ
MAQYLAEAGY GTRGKIGCTQ PRRVAAMSVS KRVAEEFGCQ LGQEVGYAIR FEDCTSPETI
IKFMTDGILL RECLLDPNLS AYSVIILDEA HERTISTDVL FGLLKQALQR RPELKVLITS
ATLEAEKFSK YFMNAQLFII PGRTFPVDIR YTKDPEADYL DASLITVMQI HLSEPPGDIL
LFLTGQEEID AACQILYERM KSLGSNVPDL IILPVYSALP SEMQTKIFEP APPGSRKVVI
ATNIAETSLT IDGIYYVIDP GFSKQKCFNP KNGMDSLVVA PISQAAARQR SGRAGRTGPG
KCYRLYTESA FKNEMLASSI PEIQRTNLGN TVLTMKAMGI NDLLNFDFMD PPPVQTLVSA
MEQLYSLGAL DEEGLLTRLG RKMAEFPLDP QLSKMLIASV DLGCSDEILT VVAMLSVQNV
FYRPKEKQAL ADQKKAKFFQ PEGDHLTLLN VYESWKNSKF SNPWCFENFV QARSLRRAQD
VRKQLITIMD RYKLDIISAG RNYTKIQKAI CSGFFANASK KDPNEGYKTL VEGQPVYIHP
SSTLFNRNPD WVIYHELVMT TKEYMREVCT IDPKWLVELA PKFFKTSDPN KISKRKRKEK
IEPLYDKYND PNAWRPSKRK
