DDX1_DICDI
ID DDX1_DICDI Reviewed; 765 AA.
AC Q55CP6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx1;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 1;
GN Name=ddx1; ORFNames=DDB_G0269966;
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: Acts as an ATP-dependent RNA helicase, able to unwind both
CC RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang
CC nuclease activity (By similarity). {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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72333.1; -; Genomic_DNA.
DR RefSeq; XP_646435.1; XM_641343.1.
DR AlphaFoldDB; Q55CP6; -.
DR STRING; 44689.DDB0233650; -.
DR PaxDb; Q55CP6; -.
DR EnsemblProtists; EAL72333; EAL72333; DDB_G0269966.
DR GeneID; 8617394; -.
DR KEGG; ddi:DDB_G0269966; -.
DR dictyBase; DDB_G0269966; ddx1.
DR eggNOG; KOG0349; Eukaryota.
DR HOGENOM; CLU_016321_0_0_1; -.
DR InParanoid; Q55CP6; -.
DR OMA; EYCIRAI; -.
DR PhylomeDB; Q55CP6; -.
DR PRO; PR:Q55CP6; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Exonuclease; Helicase; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome; RNA-binding.
FT CHAIN 1..765
FT /note="Probable ATP-dependent RNA helicase ddx1"
FT /id="PRO_0000327806"
FT DOMAIN 33..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 63..252
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 512..715
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 78..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT MOTIF 400..403
FT /note="DEAD box"
FT COMPBIAS 275..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 765 AA; 84828 MW; E3A85CAE937DBA0E CRC64;
MSAFEDLGVL PEIIKAIEEL DWLLPTPIQT EAIPLILGGG DVLAAAETGS GKTGAFALPI
LQITYETLNK KAEIPIIAPT NTSGEDGTSG GGGGGGGGDT IELDQIDRDK NMAVDGLICQ
SRSSDWCGIK ATKGISSGKF YYESIVRDEG LCRIGFALKK SSRNIGTDKF SWGYGGTGKK
SHESKFIDYG KPFGNNDVIG CYINFDEEII GFTKNGQDFG EAFTFNSKAG IFYPALVLKN
AEMEFNFGSK PMKHDLKGYK PINQAELLID QQTSTQIDNS KNNNNNNNKK GSGNNKKNKG
KDDDKMNDED NNNKQPRKTL SLIIEPTREL ADQAYSAILN FSKYLDSPKI QVSLCIGGEK
SNGGRNKIEG DIIIGTPGRL ESLVKEGSID LSSIKFFVLD EADQLIDDNL AIVNFIYNKL
PIGQNLQVLF FSATLHSTKV IKFCEQITKN PTWVDLKGRD FIPDLITHAY VKADPIKFES
LWRNSENPLR IRTDGVHASD VQQFGKLKEP EQKSEAIKLL KAQLLLKCIQ SFKMDQAIIF
ARTRLDCDHI HQFLKDAGGG NTSGLEGEFS STVLHGGDNI SRARKDNLEK FRNGDVRFLI
CTDVAARGID IRGLPYMINY TLPESFEDYI HRVGRVGRSD RIGLAISLVA YEQEKVWYHT
CRDKGKGCHN TKLTENGGCC IWYDEPQLFT AIQENIGPIE LDSDFQLPKD MKQLNFGGST
KLTGASADYK PHTEELRSRV LQLSQLEETI QIDYLTLPKR IIKLK
