ID F1A4L2_DICPU Unreviewed; 1004 AA.
AC F1A4L2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Myb domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=DICPUDRAFT_4822 {ECO:0000313|EMBL:EGC28868.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC28868.1, 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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GL871528; EGC28868.1; -; Genomic_DNA.
DR RefSeq; XP_003294605.1; XM_003294557.1.
DR AlphaFoldDB; F1A4L2; -.
DR STRING; 5786.F1A4L2; -.
DR EnsemblProtists; EGC28868; EGC28868; DICPUDRAFT_4822.
DR GeneID; 10507063; -.
DR KEGG; dpp:DICPUDRAFT_4822; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; F1A4L2; -.
DR OMA; TAFYRKE; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 170..335
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 467..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 820..872
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGC28868.1"
FT NON_TER 1004
FT /evidence="ECO:0000313|EMBL:EGC28868.1"
SQ SEQUENCE 1004 AA; 117606 MW; C2AD3F1A436440D6 CRC64;
DDDEVEEDDD SIQAGLARKD ETEEEKKERL ESIRLEKERL KEIRAQQRKQ LKELQNNQMA
QLQEDKEKSA SARLKYLLER TEIFTHFVSN SQQTKKKETK SPTLSSQNGS ISATPTKRGH
ITEKAEDDEI MKGAIEEEEP HSFNFFTSSP PYIKSGTMRD YQVNGLNWLI QLYERGINGI
LADEMGLGKT LQTISLLGYL SEYKGIRGPH LIIAPKSTLS GWTKEFAKWC PFLRVVKFHG
SKEEREEIKR NSLIFKKFDV CITTYEVAIR EKAAFKKFSW RYIIIDEAHR IKNENSVLSK
GVRLFNSQFR LLITGTPLQN NLHELWSLLN FLLPDVFSSS EDFDKWFDLA NTENQQEVID
KLHKVLRPFL LRRLKSEVEK SLPPKKEIKL FVGLSSMQKD WYKRLLTKDI EAVMNPGSKG
QAARVRLLNI CMQLRKACNH PYLFDGAEEE PYTTGEHLIT NSGKMVLLDK LLKKLQERGS
RVLIFSQMAR MLDILEDYML YRNYRYARID GSTDSVSREN SIDNFNKPGS ELFAFLLTTR
AGGLGITLNT ADVVILFDSD WNPQMDLQAQ DRAHRIGQTK PVTVYRFVTE ASMEEKMVEK
AEMKLQLDAL VIQQGRLVEA NKNAKPEELL AMLRFGADDM FKSKSSTITD EDIDSILKKG
EEKTEQMNSK VKDLANNPIK FQSDGNLYEF DGVNYRNQHS SATFWADTLK RERKTVAVDE
DFSKMVTGQV RPSPMVKRER RFNKPKQPPL YDFQFYPPRL TQLYEKETEA YNRKVEWYDQ
KDKEKEKAGN NPTEIEDEEE PDFGDLNKEE QESKEKLLKS GFGDWTKTDF KSFIRGCELY
GRKAYQSIAE EIGTKTDKQV QQYSQVFWKR FEEVNEHEKH VLRIEKGEER ILRYKEQQES
LNHKISKYKN PWQQLKIQYG IKKNKTYNDD EDIFLVCMIH KLGYGAWEEL KEEIRKSPQF
RFDWLIQTRT PSELKQRCDQ LLKYIIKEHQ EEIEHQKELE KKKK
//
