ID A0A0V0SLY6_9BILA Unreviewed; 1035 AA.
AC A0A0V0SLY6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=Putative global transcription activator SNF2L1 {ECO:0000313|EMBL:KRX27737.1};
GN Name=Smarca1 {ECO:0000313|EMBL:KRX27737.1};
GN ORFNames=T07_12857 {ECO:0000313|EMBL:KRX27737.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27737.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX27737.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX27737.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRX27737.1}.
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DR EMBL; JYDL01000002; KRX27737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0SLY6; -.
DR Proteomes; UP000054630; 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:UP000054630}.
FT DOMAIN 168..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 456..607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 814..865
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 120148 MW; 6949CE3275E027BD CRC64;
MVSEDDMEVD DGPPMLDRED YSEPSSSRRQ SESEEEDYLD VKSSKIAKVA RPDTGDHYDQ
VLNDQAKRFE YLLKQTEVYS HFVSSGALTE GKKLGSPLKI KEKKDGKVIP KVSAVGDHRH
RKTEKEEDEE LLEEERHNAN IFCFAQSPWY IKGGEMRDYQ IRGLNWMIAL LENGINGILA
DEMGLGKTLQ TISFIGYLKH YKNMPSPHLV ICPKSTLPNW VNEFNRWCPS IIVVQLIGNQ
ETRDAIINEK LMPGKWDVCV TSYEMAIREK CVLRKFNWRY IVIDEAHRIK NEKSKLSEIV
RQFRSSHRLL LTGTPLQNNL HELWALLNFL LPDVFNSSDD FDAWFNTSSC FGDTGLVERL
HTVLKPFLLR RLKSEVEKAL PPKKELKIYI GLYTKILMKD IDIVNGAGKL EKARLLNILM
QLRKCCNHPY LFDGAEPGPP FTTDQHLVDN CGKMVLVDKL LPKLKEQGSR VLIFSQMSRM
LDILEDYCLW KQYPYCRLDG QTPHQERQAS IDAFNAPNSE KFIFMLTTRA GGLGINLATA
DIVILYDSDW NPQMDLQAMD RAHRIGQKKT VRVFRLITEN TVEERIVERA EIKLRLDTVV
IQQGRLAETQ KSLGKDEMLT MIRHGADHVF AGKESEITEE DIDCILARSE EKNEALKRRL
EELGESSLRN FTLDTQEASS VYQFEGKDYR GKQRKALGYW IEPPKRERKA NYQIDAYFRD
ALRPHVEPKA PKAPRPPKQP QIQDFHFYPP RLLHLCEREV YYYRKTIGYK VPLMQDLPPE
KALKRQEDEQ KKIDEAVPLT EEELAEKEQL LHCGFSNWSR REFNQFIKAN EKYGRNDVEN
IAQEVDGKSP DEVREFYKVF WARCCELADI DRVLGQIERG EARIQKRLSV KRALELKIAR
YRAPFHQLRV QYGTNKGKNY TEEEDRFLVC MLHEIGFGKE NLYEELRQAI RVAPQFRFDW
FLKSRTAMEL QRRCNTLISL IEKEMHDVEQ NDKSSGGGRN RNNCKSGRSG SSAATPEKRK
ADVQDGKRSS RRSKA
//