ID Q55A06_DICDI Unreviewed; 973 AA.
AC Q55A06;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 2.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=DDB_G0272384 {ECO:0000313|EMBL:EAL71344.2};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL71344.2, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL71344.2, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL71344.2,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=12097910; DOI=10.1038/nature00847;
RG Dictyostelium Genome Sequencing Consortium;
RA Glockner 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., 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] {ECO:0000313|EMBL:EAL71344.2, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL71344.2,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner 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., 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., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., 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., 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., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL71344.2}.
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DR EMBL; AAFI02000008; EAL71344.2; -; Genomic_DNA.
DR RefSeq; XP_645178.2; XM_640086.2.
DR AlphaFoldDB; Q55A06; -.
DR SMR; Q55A06; -.
DR STRING; 44689.Q55A06; -.
DR PaxDb; 44689-DDB0233085; -.
DR EnsemblProtists; EAL71344; EAL71344; DDB_G0272384.
DR GeneID; 8618350; -.
DR KEGG; ddi:DDB_G0272384; -.
DR dictyBase; DDB_G0272384; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_305117_0_0_1; -.
DR InParanoid; Q55A06; -.
DR OMA; MQDQVHK; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; 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:0003678; F:DNA helicase activity; ISS:dictyBase.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF121; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000002195}.
FT DOMAIN 487..663
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 688..837
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 64..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 112003 MW; 55600C3BA512C91E CRC64;
MDNRPMNKLI SRSIFNKTNE RSTLSLFQSL NYYYKRDFTS EINKTNNNFD NCQNNEEGYN
VINNNKKNKN NSNNNNVEYN ENDNSNNNNN NNKNEINNNE IDFDWSMKAK KKIKKSVLTG
EDRLDKKTKD LKYLNSIGLL VKLKSTTISN NEISDNSNNN NLKDKENDEI ETIALIDEDN
EISTIKKKKK IKTNKNSYDD DNIDNESNDY TTTIIQNEDH NTFSSTTTTT RGSIKNKRNK
SLKKEEIQKQ HEENQDNNHD KISIEYDENE LKKTYNLDEN GDNIVEMSPA FKNNNLLIKK
SKNKKTKQSN IDIDNDNDNV DNYIDNDDDD ETIDKPKKSK SKSTTKSKKI NVKKQDDENE
EEEEDEDEEK EFKSIEISKL KKKKKEIKDG EYLNIKNVYK EWLESPIVIK LSNDDSCFTN
SKIKINPKSF TIKSDDDDDG NGNGNGNGND NDKNNLKLKR EWHELVETCN RDIFGNKEFR
NLQIEAINSI LHDRDTFVSL PTGGGKSLCF QIPSIVDHRG VTFVISPLLA LMQDQVHKLK
SLGIPAESIN SSGSQRENRD VLDQLLNGET CKLKLIYITP ERLAQSEFLH LLDQLYDQGR
LRRLVVDEAH CISEWGHSFR PKYRLISTFR DRFPSVPISA FTASATPNVE IDIKNSLKMV
NPITINSSFL RPNLLYQVRQ KQSDEESLLK DIYNFISFKY PNSTGIIYCA TVRECEIVAD
YLSERGLSSN FYHAKLSNTQ RSKLQKDWTN GEFKIVCTTI AFGMGIDKGD TRFVIHHSMP
QSMESYYQQT GRAGRDGKHS DCLLFYNKSD LMRFKHIISL NQPKDPFNAF SNYNGVGIGD
IGGEHLILDN DGNYISNYSS DESQYMDTIK NKIQQTSTKL EMLDSVASFC STQSKCRRVT
LLNYFGENSK SCGNMCDICI SNSNSNSNNR SKAKQNQIDY SERIYNRNSY SISSFKNKKK
KSHVSYDNDN DVD
//
