ID A0A504YVC4_FASGI Unreviewed; 1016 AA.
AC A0A504YVC4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=SWI:SNF matrix associated {ECO:0000313|EMBL:TPP65404.1};
GN ORFNames=FGIG_02731 {ECO:0000313|EMBL:TPP65404.1};
OS Fasciola gigantica (Giant liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=46835 {ECO:0000313|EMBL:TPP65404.1, ECO:0000313|Proteomes:UP000316759};
RN [1] {ECO:0000313|EMBL:TPP65404.1, ECO:0000313|Proteomes:UP000316759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uganda_cow_1 {ECO:0000313|EMBL:TPP65404.1};
RA Choi Y.-J.;
RT "Annotation for the trematode Fasciola gigantica.";
RL Submitted (APR-2019) 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:TPP65404.1}.
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; SUNJ01003232; TPP65404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A504YVC4; -.
DR STRING; 46835.A0A504YVC4; -.
DR Proteomes; UP000316759; 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:UP000316759}.
FT DOMAIN 115..280
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 414..565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 775..827
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 47..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 117201 MW; 796E74E7809492B9 CRC64;
MSDGETAEPI PVATRQLEDL IAKAEIYSKI KLAGGETAKA VTSPLKAAPE LLIQSPTHDQ
GPDHRHRRTE REEDEELLSE TKHTPSSVQR FESSPFFVKG GEMRDYQVRG LNWMIQLHQD
NINGILADEM GLGKTLQTIS MLGYMKHCRQ KSGPSLIIVP KSTLSNWMNE IKRWVPTLRP
VALIGMQEER NQVIRDEIVG KEWDVLVTSY EICIREKAVL RKFHYIYLII DEAHRIKNEK
SKLSDIVRQF RSQNRLLITG TPLQNNLHEL WALLNFLMPD LFASSELFDD MFKTNSEQEQ
NLIQRLHAVL KPFLLRRIKA DVEKRLPPKK EIKIYIGLSK MQRDLYTKIL MKDIDLVNSM
INVNANRADR VRLLNILMQL RKCCNHPYLF DGLEPGPPYT TDMHLIENCG KMVLLDKLLA
RLKEQGSRVL IFSQMTRLLD ILEDYCLWRG HDYFRLDGST RHEDRQVYID EYNRPGSTKF
IFMLSTRAGG LGINLATADV VIIYDSDWNP QVDLQAMDRA HRIGQTKTVR VFRLITENTV
EERIIMRAEM KLRLDNLVIQ QGRLVEQKAN QLQKGEVLDM IKFGANYIFR TKDSDFKDED
IDIILARGEQ RTAEMNEKLA KLGESSLRSL KFDTPEELGP ATSAYYFEGE DYREKHRGTA
LEGWIEPPKR ERKANYAVDA YFREALRVSE PKAPKPPRPP KQPNVQDFQF FPPRLFELLD
KEIYAFRKSI GYKVPRNPDA GPDAERERLE QQLRIDEAEP LTEEEVVEKE DLLSQGFTNW
SKRDFQQFIK ANEKHGRDDL EAISMDVEGK TPEEVKRYAR VFWTRCNELQ DVDKHMAQIE
RGEAKIQRRA AIKRALDLKM ARYRAPFHQL RIQYGANKGK NYVEEEDRFL ICMLHKLGFD
RDNVYDDLRL AVRLAPQFRF DWFLRSRTAM ELQRRCSTLI TLIEREICDM DDRTKQQRGG
GPGTNNQTGG PATANDGSGT NSGSGGTAAS AQKRKATEGG GAVEPNGKKR KTAAVN
//
