ID A0A183JEA4_9TREM Unreviewed; 1014 AA.
AC A0A183JEA4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Global transcription activator SNF2L1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCUD_LOCUS1017 {ECO:0000313|EMBL:VDO65072.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000101601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0000101601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO65072.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDO65072.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAK01000768; VDO65072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183JEA4; -.
DR STRING; 6186.A0A183JEA4; -.
DR WBParaSite; SCUD_0000101601-mRNA-1; SCUD_0000101601-mRNA-1; SCUD_0000101601.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000279833}.
FT DOMAIN 120..285
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 415..566
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 777..829
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 42..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 117268 MW; BEDB2FE9D352D54B CRC64;
MDPAQEHNSG IHTNNVQGAL RQLDLLVEKA ELYAQVKLIG SGTKDLSSPS RIKQEQPISS
PTSHSFGDHR HRRTEKEEDE ELLTETKHSS SGIQRFEASP WYVKGGEMRD YQIRGLNWMI
QLHHSSINGI LADEMGLGKT LQTISLLGYI KHCRHKHGPH MVIVPKSTLS NWMNEFARWV
PSLRTVSLIG NHEERSQKIQ EEILKKEWDV IVTSYEMCIK EKAVLKKFHF IYLIIDEAHR
IKNEKSKLSE IVRDFRSQNR LLITGTPLQN NLHELWALLN FLMPDLFSSS EMFDDMFKTG
NDQEESLVQR LHAVLKPFLL RRIKADVEKR LPPKKECKIY IGLSKMQRDL YTKILMKDID
VVNSVGNKVD RLRLLNILMQ LRKCCNHPYL FDGLEPGPPY TTDRHLVDNC GKLMLLDKLL
PKLKEQGSRV LLFCQMTRMM DILEDYCLWR GHEYFRLDGS TPHEERQISI DEYNRPGSTK
FLFMLSTRAG GLGINLATAD VVIIYDSDWN PQVDLQAMDR AHRIGQTKTV RVFRLITEHT
VEERIIMRAE MKLKLDNLVI QQGRLVEQKS NQLQKGDVLD MIRHGANYIF RSKDSDFKDE
DIDIILARGE QKTAEMNEKL AQLGESNLRS LKFDTADENG APTSAYIFEG EDYREKQCRT
SLLDGWIEPP KRERKANYAV DAYFREALRV SEPKAPKPPR PPKQPNVQDF QFFPPRLFEL
LDKEIYAFRK SIGYKVPRNP DAGPDGERDR LDEQARIDEA EPLTEEELAE KEELLTQGFT
NWSKRDFQQF IKANEKHGRD DLEAISVDVE GKTPDEVKRY ARVFWTRCNE LQDVDKHMAQ
IERGEAKIQR RAAVKRALDL KMARYRAPFH QLRIQYGTNK GKNYVEEEDR FLICMLHKLG
FDRDNVYDDL RLAVRLAPQF RFDWFLRSRT AMELQRRCST LITLIEREIC DLEDRTKQRS
GAGANNLPLT PANSGPSNTS TVSNQKRKST AAGGINSDST AEISGNAKKK KVTA
//