ID A0A0N0U2P1_9HYME Unreviewed; 966 AA.
AC A0A0N0U2P1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Chromatin-remodeling complex ATPase chain Iswi {ECO:0000313|EMBL:KOX67578.1};
GN ORFNames=WN51_09186 {ECO:0000313|EMBL:KOX67578.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX67578.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX67578.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX67578.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX67578.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KQ436010; KOX67578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0U2P1; -.
DR STRING; 166423.A0A0N0U2P1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 3.
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; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 1.
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:UP000053105}.
FT DOMAIN 144..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 432..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 788..840
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 112163 MW; B6A7E84CBE9324B9 CRC64;
MSKPDENADT GDTGDNSNGS SAETTSSRGG DFETKLETDR SKRFDYLLKQ TEIFSDFMTN
NQKDKAGSPL KIKAGRPRKQ PIENQVKSDS GDHRHRKTEQ EEDEELLAES NASVAPTTRF
ESSPHYIKSG ELRDYQIRGL NWMISLYEHG INGILADEMG LGKTLQTISL LGYMKHFRNI
PGPHIVIVPK STLANWMNEF KKWCPTLRAV CLIGDAETRN TFIREVMMPG EWDVCVTSYE
MVIKEKSVFK KFNWRYMVID EAHRIKNEKS KLSEILREFK TANRLLLTGT PLQNNLHELW
SLLFNSSDDF DSWFNTNSFL GDNSLVERLH AVLRPFLLRR LKSEVEKGLK PKKEIKVYIG
LSKMQREWYT KVLMKDIDIV NGAGKIEKMR LQNILMQLRK CCNHPYLFDG AEPGPPYTTD
EHLVYNCGKM VILDKLLPKL QQQESRVLIF SQMTRMLDIL EDYCHWRGFQ YCRLDGNTAH
EDRQRQINEY NAPGSEKFIF MLSTRAGGLG INLATADVVI IYDSDWNPQM DLQAMDRAHR
IGQQKQVRVF RFITENTVEE KIVERAEVKL RLDKLVIQQG RLVDAKQTAL NKDEMLNMIR
HGANEVFASK DSAITDEDID TILQKGEART EEMKQKLESL GESSLRNFTV DAPTDSVYQF
EGEDYREKQK ILGIGNWIEP PKRERKANYA VDAYFREALR VSEPKAPKAP RPPKQPIVQD
FQFFPPRLFE LLDQEIYYFR QTVGYKVPKN PELGSDAARI QKEEQRKIDE AQPLTDEEVA
EKEKLLTQGF TNWTKRDFNQ FIKANEKYGR DDIENIAKEV EGKTPEEVME YSAVFWERCH
ELQDIDRVMA QIERGEAKIQ RRAGIKKALD AKMARYRAPF HQLRIAYGTN KGKNYTEEED
RFLVSLELQR RCNTLITLIE RENQELEERE RQERRKKGSS IGAKPASKRK QENLPAPQDK
PRKKKK
//
