ID A0A158PBN4_ANGCA Unreviewed; 981 AA.
AC A0A158PBN4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Global transcription activator SNF2L1 {ECO:0000313|WBParaSite:ACAC_0001122401-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001122401-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0001122401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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 AlphaFoldDB; A0A158PBN4; -.
DR STRING; 6313.A0A158PBN4; -.
DR WBParaSite; ACAC_0001122401-mRNA-1; ACAC_0001122401-mRNA-1; ACAC_0001122401.
DR Proteomes; UP000035642; 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:UP000035642}.
FT DOMAIN 140..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 426..577
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 782..835
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 71..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 114283 MW; 4A3561BCE0F7745B CRC64;
VFCSLHSSSD DEYCSSSYYS NVDVSHFFLS EDSLESKFEA DSFKRFELLL KKTENFSHCL
SAGDVAAYKA GSPQKKKRGR HAKAGVDGDH RHRKTEQEED EEMAEAARKE DDIMVFDKNP
FYIQNGELRD YQIRGLNWLI SLQHNGINGI LADEMGLGKT LQTISLLGYM KHYKNMAGPH
LVIVPKSTLK NWMNEFAKWC PSITTCCVIG DEKERNEVIH NVILPQKFDV CCTTYEMVLK
VKTQLKKLVW KYIIIDEAHR IKNEKSKLSE VVREIKSKNR LLITGTPLQN NLHELWSLLN
FLLPDMFSSS EDFDSWFTDG SMQGNVLQPF LLRRIKSDVE KGLLPKKEVK IYVGLSKMQR
EWYTKVLMKD IDVINGAGKV EKARLMNILM HLRKAANHPY LFDGAEPGPP YTTDQHLVDN
SGKMVVLDKL LLKLKQQGSR VLIFSQFSRI LDLLEDYCWW KQYQYCRLDG NTAHVDRQEA
IDAYNAPNSE KFIFMLTTRA GGLGINLATA DVVIIYDSDW NPQSDLQAMD RAHRIGQKKQ
VRVFRLITEN TVDERIIERA EVKLRLDSIV IQQGRIAEAQ KTLGKDDMIN MIRHGAELVF
ASKDSTITDE DIDTILERAE LKTAELNAKM EELGETSLRN LTFDNSKSVY NFEGENWKDK
QNEGMGQFWI EPPKRERKAN YQVDAYFREA MRQGQPVEKQ SRAPRPKQPA VFDFQFYPPR
LMELLDRETY HYRKTIGYKA EKPKECGPKE AEKRQKEEQR LIDTAEPLTE EEQIEKNELL
THGLANWSKR DFTAFIRANE KFGRNDIDNI ANEMIETKSR DEVEYYAKTF WERFEELQDH
EKILAQIEKG EARIQRRQSV KRALDAKIAK YKAPFHQLRI AYGTNKGKTY TEEEDRFLVC
ELHRLGFDKE TVYEELRQSV RMAPQFRFDW FIKSRTAMEL QRRCNTLITL IEKEMGETEV
KHRTRKDAKD KPNIGRPKTN K
//