ID A0A0T6AVN9_9SCAR Unreviewed; 1016 AA.
AC A0A0T6AVN9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=Helicase {ECO:0000313|EMBL:KRT79177.1};
GN ORFNames=AMK59_8193 {ECO:0000313|EMBL:KRT79177.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT79177.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT79177.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT79177.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT79177.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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:KRT79177.1}.
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DR EMBL; LJIG01022699; KRT79177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AVN9; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000051574; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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; 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 Helicase {ECO:0000313|EMBL:KRT79177.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT DOMAIN 142..307
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 437..588
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 793..845
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 118339 MW; CDA6BC24661E4DF5 CRC64;
MSTKTEEEGS EVVDTGENSN ESSSDTISSR GKGEDFETKL ETDRSKRFDF LLKQTEIFSH
FMTSHTSKSK DKPKSGRPKK VKSDEAAIAD HRHRKTEQEE DEELLAETNA KSKPTIRFEA
SPPYIKNGEM RDYQIRGLNW MISLYENGIN GILADEMGLG KTLQTISLLG FMKHYKNIQG
PHIVIVPKST LANWMNEFNK WCPTLRAVCL IGDQEARSAF IRDIMMPGEW DVCVTSYEMC
IKEKSVFKKF NWRYMVIDEA HRIKNEKSKL SEILREFKTT NRLLLTGTPL QNNLHELWAL
LNFLLPDVFN SADDFDAWFN TNQCLGDNAL VERLHAVLKP FLLRRLKSEV EKKLKPKKEV
KIYVGLSKMQ REWYTKVLMK DIDIVNGAGK IEKMRLQNIL MQLRKCTNHP YLFDGAEPGP
PYTTDEHLVY NCGKMVILDK LLPKLQEQDS RVLIFSQMTR MLDILEDYCH WRQYQYCRLD
GQTPHEDRQR QINEYNEDNS KKFIFMLSTR AGGLGINLAT ADIVIIYDSD WNPQMDLQAM
DRAHRIGQKK QVRVYRFITE NTVEEKIVER AEIKLRLDKL VIQQGRLVDS KSNALNKDEM
LSMIRHGANH VFASKDSDIT EEDIDTIVLK GEAKTAELNQ KYESLGESSL RNFTVDTPTE
SVYKFEGEDY REKQKAAGLS NWIEPPKRER KANYAVDAYF REALRVSEPK APKAPRPPKQ
PIVQDFQFFP PRLFELLDQE IYFYRKTLGY KVPKNPELGP EASKQQKEEQ RKIDESEPLT
EEEQQEKESL LTQGFTNWSK RDFNQFIKAN EKYGRDDIEN IAKEVEGKTS EEVMEYSAVF
WERCNELTDI DRIMAQIERG EAKIQRRASI KRALDAKMAR YRAPFHQLRI SYGTNKGKNY
MEDEDRFLVC MLHKLGFDRE NVYEELRAAI RASPQFRFDW FLKSRTAMEL QRRCNTLITL
IERENQELEE RERAERKKKA PKSGSLTGAP QSSTKSSQKR KNESGGGPTD KKKKKK
//