ID A0A0V1A2V1_9BILA Unreviewed; 1042 AA.
AC A0A0V1A2V1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative global transcription activator SNF2L1 {ECO:0000313|EMBL:KRY18665.1};
GN Name=Smarca1 {ECO:0000313|EMBL:KRY18665.1};
GN ORFNames=T12_12653 {ECO:0000313|EMBL:KRY18665.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18665.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY18665.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18665.1};
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 -!- 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:KRY18665.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDQ01000044; KRY18665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A2V1; -.
DR Proteomes; UP000054783; 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; 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 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:UP000054783}.
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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1042
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 1002..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 121067 MW; 0571AF719444A1F5 CRC64;
MVSEDDMEVD DGPPMLDRED YSEPSSSRRQ SESEEEDYLD VKSSKIAKVA RPDTGDHYDQ
VLNDQAKRFE YLLKQTEVYS HFVSSGALTE GKKLGSPLKI KEKKDGKVIP KVSAVGDHRH
RKTEKEEDEE LLEEERHNAN IFCFAQSPWY IKGGEMRDYQ IRGLNWMIAL LENGINGILA
DEMGLGKTLQ TISFIGYLKH YKNMPSPHLV 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 KRQEDEQKKI DEAVPLTEEE LAEKEQLLHC GFSNWSRREF NQFIKANEKY
GRNDVENIAQ EVDGKSPDEV REFYKVFWAR CCELADIDRV LGQIERGEAR IQKRLSVKRA
LESKIARYRA PFHQLRVQYG TNKGKNYTEE EDRFLVCMLH EIGFGKENLY EELRQAIRVA
PQFRFDWFLK SRTAMELQRR CNTLISLIEK EMHDVEQNDK SSGGGRNRNN CKSGRSGSSA
ATPEKRKTDV QDGKRSSRRS KA
//
