ID F0ZCP8_DICPU Unreviewed; 815 AA.
AC F0ZCP8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=DICPUDRAFT_76134 {ECO:0000313|EMBL:EGC38307.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38307.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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. DDX10/DBP4
CC subfamily. {ECO:0000256|ARBA:ARBA00038084}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL870979; EGC38307.1; -; Genomic_DNA.
DR RefSeq; XP_003285168.1; XM_003285120.1.
DR AlphaFoldDB; F0ZCP8; -.
DR STRING; 5786.F0ZCP8; -.
DR EnsemblProtists; EGC38307; EGC38307; DICPUDRAFT_76134.
DR GeneID; 10502411; -.
DR KEGG; dpp:DICPUDRAFT_76134; -.
DR eggNOG; KOG0343; Eukaryota.
DR InParanoid; F0ZCP8; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR24031:SF54; 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.
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:UP000001064};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 140..314
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 340..489
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..785
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 93250 MW; 2D307F8497E9FA39 CRC64;
MDKNKQQNND ENIKKLTKNK YDSKKEKTDN SKIFHNRSSK KRIEKLKKIE HSKKPLTIKL
NEIEIIENRL KEEAPARGTN PLANSPSTNA TNATSSSSQE YKVDYPSATI FKDLPLSQLT
QKGLTESKFY KLTDIQRASL PHTLCGRDIL GAARTGSGKT LAFIIPVLET LWRNRWSRND
GIGAIVLSPT RELAIQIFDV LKSVGKHHTF SAGLLIGGRN VTQEKEKVNA MNILIATPGR
LLQHMDETYG FDCSNLKMLV LDEADRILDL GFSKSLNSIL ENLPKQRQTL LFSATQTKSV
RDLVRLSLNE PEYISVYEKD IITAPQNLTQ TICIIPLEMK LNMLYSFVKT HLTSKVIVFF
ASCKQIRFVY ETFRLLNPGT SLFQLHGKMK QWTRLEVFED FCKKKAGVLF ATDIAARGLD
FPEVEWVIQV DCPDDIETYI HRIGRTARNN ATGQAITILL PSEKEAMTAL LEKQKMKYEV
LEPNPEKLVS IDSQLSGFLS EKTELKYLAQ KSFVSYLRSV YRQSNKEIFN IEKLNIEDFS
KSLGLLGKPQ ISFGKSSADK NKSFIVADIQ KKLQDQKSKG EKDKDSDIDS DAELPEEGSD
GEIVITNNKR PLSNIEKTFL RKNANVFSEN YQKLRHKEDN EEDDEDFMTI KRKDHNVDTS
DVPEKLSRKD QKEKKYLNDP NKLKFQESTA LPTNGVLPTS YLEKIRSEVK QGDAEDKILQ
KERLKRRKLK LQSKELSQYK DGDEEESVAY FVPPGEDDPY ENSDDEEENS DNSEDESEEE
EEEEEKVKPQ ISNKKRTIED QEELALSILK KNRLN
//