ID A0A158QNV9_HAEPC Unreviewed; 967 AA.
AC A0A158QNV9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VDO42550.1, ECO:0000313|WBParaSite:HPLM_0001131401-mRNA-1};
GN ORFNames=HPLM_LOCUS11306 {ECO:0000313|EMBL:VDO42550.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001131401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001131401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO42550.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO42550.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAF01017530; VDO42550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158QNV9; -.
DR STRING; 6290.A0A158QNV9; -.
DR WBParaSite; HPLM_0001131401-mRNA-1; HPLM_0001131401-mRNA-1; HPLM_0001131401.
DR OMA; VHDYQFF; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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:UP000268014}.
FT DOMAIN 154..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 449..600
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 804..857
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 112509 MW; 9556D18E1864A7C7 CRC64;
MATEDITNEE ERMDISEMTP EADAVDEVKV EQEENEEGEM EAEEGEDSLE SKFEADSFKR
FELLLKKTEN FSHCLSAGDV AAYKGSPVKK KRGRVAKTGV DGDHRHRKTE QEEDEEMAEA
AVREDTAMVF DKNPFYIQNG ELRDYQIRGL NWLISLQHNG INGILADEMG LGKTLQTIAL
LGYMKHYKNM ASPHLVIVPK STLKNWMNEF AKWCPSLSTC CVIGDEKERN DVIHNTILPQ
KFDVCCTTYE MVLKVKTQLK KLVWKYIIID EAHRIKNEKS KLSEVVREIK SKNRLLITGT
PLQNNLHELW ALLNFLLPDM FSSSEDFDSW FTDGSMQGNA DIISRLHKVL QPFLLRRIKS
DVEKSLLPKK EVKIYVGLSK MQREWYTKVL MKDIDVINGA GKVEKARLMN ILMHLRKAAN
HPYLFDGAEP GPPYTTDQHL VDNSGKMVVL DKLLVKLKQQ GSRVLIFSQF SRILDLLEDY
CWWRQYQYCR LDGNTAHVDR QESIDAFNAP NSEKFIFMLT TRAGGLGINL ATADVVIIFD
SDWNPQSDLQ AMDRAHRIGQ KKQVRVFRLI TENTVDERII ERAEVKLRLD SIVIQQGRIA
EAQKTLGKDD MINMIRHGAE LVFATKDSTI TDDDIDVILE RAEVKTAELN AKMEELGESN
LRNLTFDNKS VYNFEGENWK GKQSEGMGHF WIEPPKRERK ANYQVDAYFR EAMRQGQPVE
KQSRAPRPKQ PAVFDFQFYP PRLMELLDRE TYHYRKTIGY KAEKPRECGP KEADKRQKEE
QHLIDTAEPL TEEEQQEKND LLTQGLANWS KRDFTAFVRA NEKYGRHDID NIANEMMETK
SRDEVEYYAK IFWERFEELQ DHEKILAQIE KGEARIQRRQ SVKRALDAKI AKYKAPFHQL
RIAYGTNKGK TYTEEEDRFL VCELHRLGFD KETVYEELRQ SIRMAPQFRF DWFIKSRTAM
VIHCQCY
//