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Database: UniProt
Entry: A0A158PBN4_ANGCA
LinkDB: A0A158PBN4_ANGCA
Original site: A0A158PBN4_ANGCA 
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
//
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