ID A0A0V1I476_9BILA Unreviewed; 1043 AA.
AC A0A0V1I476;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 41.
DE SubName: Full=Putative global transcription activator SNF2L1 {ECO:0000313|EMBL:KRZ17649.1};
DE Flags: Fragment;
GN Name=Smarca1 {ECO:0000313|EMBL:KRZ17649.1};
GN ORFNames=T11_18430 {ECO:0000313|EMBL:KRZ17649.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ17649.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ17649.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ17649.1};
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:KRZ17649.1}.
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DR EMBL; JYDP01000006; KRZ17649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I476; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:TreeGrafter.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0034728; P:nucleosome organization; IEA:TreeGrafter.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.300:FF:000082; ISWI chromatin remodeling complex ATPase ISW1; 1.
DR FunFam; 1.10.10.60:FF:000022; ISWI chromatin-remodeling complex ATPase CHR11 isoform A; 1.
DR FunFam; 1.10.10.60:FF:000049; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member; 1.
DR FunFam; 1.10.1040.30:FF:000001; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member; 1.
DR FunFam; 1.20.5.1190:FF:000002; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member; 1.
DR FunFam; 3.40.50.10810:FF:000101; SWI/SNF-related, matrix-associated, actin-dependent regulator of; 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-like.
DR InterPro; IPR009057; Homeodomain-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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A MEMBER 5; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 168..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 463..614
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 821..872
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1020
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1043
FT /evidence="ECO:0000313|EMBL:KRZ17649.1"
SQ SEQUENCE 1043 AA; 121305 MW; BDF6F58935DA4B74 CRC64;
MVSEDDMEVD DGPPMLDRED YSEPSSSRRQ SESEEEDYLD VKDSKIAKVA RRDTGDHYEQ
VLNDQAKRFE YLLKQTEVYS HFVSSGALTE GKKLGSPLKI KEKKDGKVVP KVSAVGDHRH
RKTEKEEDEE LLEEERHKAN IFCFAQSPWY IKGGEMRDYQ IRGLNWMIAL LENGINGILA
DEMGLGKTLQ TISFIGYLKH YKNMSSPHLV ICPKSTLPNW VNEFNRWCPS IIVVQLIGDQ
ETRDAIINEK LMPGKWDVCV TSYEMAIREK CVLRKFNWRY IVIDEAHRIK NEKSKLSEIV
RQFRSSHRLL LTGTPLQNNL HELWALLNFL LPDVFNSSDD FDAWFNTSSC FGDTGLVERL
HTVLKPFLLR RLKSEVEKAL PPKKELKIYI GLSKLQRDWY TKILMKDIDI VNGAGKLEKA
RLLNILMQLR KCCNHPYLFD GAEPGPPFTT DQHLVDNCGK MVLVDKLLPK LKKQGSRVLI
FSQMSRMLDI LEDYCLWKQY PYCRLDGQTP HQERQASIDA FNAPNSEKFI FMLTTRAGGL
GINLATADIV ILYDSDWNPQ MDLQAMDRAH RIGQKKTVRV FRLITENTVE ERIVERAEIK
LRLDTVVIQQ GRLAETQKSL GKDEMLTMIR HGADHVFAGK ESEITEEDID CILARSEEKN
EALKRRLEEL GESSLRNFTL DTQEASSVYQ FEGKDYRGKQ RKALGYWIEP PKRERKANYQ
IDAYFRDALR PHVEPKAPKA PRPPKQPQIQ DFHFYPPRLL HLCEREVYYY RKTIGYKVPL
MQDLPPEEAL KRQEDEQRKI DEAVPLTEEE LAEKEQLLHC GFSNWSRREF NQFIKANEKY
GRNDVENIAQ EVDGKSPDEV REFYKVFWAR CCELADIDRV LGQIERGEAR IQKRLSVKRA
LESKIARYRA PFHQLRVQYG TNKGKNYTEE EDRFLVCMLH EIGFGKENLY EELRQAIRVA
PQFRFDWFLK SRTAMELQRR CNTLISLIEK EMHDVEQNDK NSGGGRNRNS SCKSGRSGSS
ATTPDKRKSD VQDGKRSSRR SKT
//
