ID A0A7I8VN25_9ANNE Unreviewed; 1018 AA.
AC A0A7I8VN25;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE SubName: Full=DgyrCDS6439 {ECO:0000313|EMBL:CAD5117688.1};
GN ORFNames=DGYR_LOCUS6190 {ECO:0000313|EMBL:CAD5117688.1};
OS Dimorphilus gyrociliatus.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Polychaeta incertae sedis; Dinophilidae; Dimorphilus.
OX NCBI_TaxID=2664684 {ECO:0000313|EMBL:CAD5117688.1, ECO:0000313|Proteomes:UP000549394};
RN [1] {ECO:0000313|EMBL:CAD5117688.1, ECO:0000313|Proteomes:UP000549394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hejnol A.;
RL Submitted (AUG-2020) 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:CAD5117688.1}.
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DR EMBL; CAJFCJ010000007; CAD5117688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7I8VN25; -.
DR EnsemblMetazoa; DGYR_LOCUS6190_t1; CAD5117688.1; DGYR_LOCUS6190.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000549394; 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:UP000549394};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 152..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 450..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 807..859
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 117939 MW; 4DF62ADA95D6C875 CRC64;
MSDSDGDSSA TSSSEEQNGR PLPKPRSDTD YHAKIKSDAT KRFDFLLKQT EFFAHFMATG
SPTTTKPTSP LKMRLEQVAQ QAEETSTRTR TTSSSDDHRH RRTEKEEDEE LLSVAAKTNT
QSGKVTRFED SPSFIEGGKM RDYQVRGLNW LISLYENGIN GILADEMGLG KTLQTISLLG
YMKHYRNVAS PHLIIAPKST LSNWMNEIKR WCPSMTAVCL IGNQEQRSAI IRDTLLPATE
WNICVTSYEM ILRERAVLKR FNWRYLVIDE AHRIKNEKSK LSEMVREFRS TNRLLLTGTP
LQNNLHELWS LLNFLLPDVF NSSDDFDAWF NTNSIQSADQ QLVHRLHSVL RPFMLRRIKL
DVEHALLPKK ETKIYIGLAK MQREWYTRIL MKDIDIVNGA TGRSDKMRLL NILMQLRKCT
NHPYLFDGAE PGPPYTTDKH IVDNSGKMIL LDKLLPKLKE QDSRVLIFSQ MTRLLDILED
YCCWRGYNYC RLDGQTSHDI RQQQIDEYNA PNSSKFIFML STRAGGLGIN LATADVVILY
DSDWNPQADL QAMDRAHRIG QKKQVRVFRL ITENTVDERI CERAEMKLKL DSIVIQQGRL
VDGAGNKLGK DDMLNMIRHG AQHVFSSKDS EITDEDIDSL LERGEKKTKE LAEKLKDMGE
GNLRSLTFDT EDNYTIYEFE GEDYRAKQKV QSWIEPPKRE RKANYAVDAY FRDALRVTSA
EPKAPKAPRP PKQPIVHDFQ FFPPRLFELL DKEIYYFRKT VGYRAAKNPD LPSAEAERER
RDEQRRIDES EPLTEDEVGE KDELLKQGFT HWSRRDFHQF IKANEKYGRD DLDSISKEVD
GKTSEQVMDY STVFWSRCTE LHDVEKIMAQ IERGEAKIAR KHAVKKALDS KMEQYKAPFH
QLRLHYGTNK GKNYTEEEDR FLICTLHKLG LEKDYVYDEL RMCIRNAPQF RFDWFLKSRT
SSELQRRCNT LISLIEREHM DSQPSDGKRK AGSAAGLPAK KAKHEDSPAP AKSKSRRR
//
