ID A0A0C2GI70_9BILA Unreviewed; 862 AA.
AC A0A0C2GI70;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Protein, SNF2 family {ECO:0000313|EMBL:KIH58574.1};
GN ORFNames=ANCDUO_11218 {ECO:0000313|EMBL:KIH58574.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH58574.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH58574.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH58574.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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; KN732969; KIH58574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GI70; -.
DR Proteomes; UP000054047; 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; 1.
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:UP000054047}.
FT DOMAIN 38..196
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 326..477
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 682..735
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 841..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 100843 MW; D4443149FBA85D13 CRC64;
MVEAAEKEDS ITIFDKSPFY IQNGELRDYQ IRGLNWLISL YHNGINGILA DEMTISLLGY
MKHYKNMGSP HLVIVPKSTL KNWMNEFAKW CPSMTTCCII GDEQERNQVI RDVILPQKFD
VCCTTYEMVL KVKTQLKKLV WKYIIIDEAH RIKNEKSKLS EVVREIKSKN RLLITGTPLQ
NNLHELWALL NFLLPDMFSS SEDFDSWFTD GSMQGNTDII SRLHKVLQPF LLRRIKSDVE
KSLLPKKEVK IYVGLSKMQR EWYTKVLMKD IDVINGAGKV EKARLMNILM HLRKAANHPY
LFDGAEPGPP YTTDQHIVDN SGKMVVLDKL LKKLKEQGSR VLIFSQFSRI LDLLEDYCWW
RQYQYCRLDG NTAHVDRQEA IDAFNAENSE KFIFMLTTRA GGLGINLATA DVVVIFDSDW
NPQSDLQAMD RAHRIGQKKQ VRVFRLITEN TVDERIIERA EVKLRLDSIV IQQGRIAEAQ
KTLGKDDMIN MIRHGAELVF ASKDSTITDE DIDTILQRAE VKTAELNAKM EEMGESNLRN
LTFDNSKSVY NFEGENWKGK QNDGMGHFWI EPPKRERKAN YQVDAYFREA MRQGQPVEKQ
SRAPRPKQPA VFDFQFYPPR LMELLDRETY HYRKTIGYKA EKPKECGPKE AEKRQKEEQR
LIDTAQPLTE EEQQEKNDLL TQGLANWSKR DFTAFVRANE KYGRHDIENI ANEMIETKSR
DEVEYYAKIF WERFEELQDH EKILGQIEKG EARIQRRQSV KRALDAKIAK YKAPFHQLRI
AYGTNKGKTY TEEEDRFLVC ELHRLGFDKE TVYEELRQSV RMAPQFRFDW FIKSRTAMKP
AAQHHRGLRQ GRNWDDQNPA NK
//