ID D2VNB4_NAEGR Unreviewed; 745 AA.
AC D2VNB4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Helicase-like protein {ECO:0000313|EMBL:EFC41624.1};
GN ORFNames=NAEGRDRAFT_80631 {ECO:0000313|EMBL:EFC41624.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC41624.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC41624.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738884; EFC41624.1; -; Genomic_DNA.
DR RefSeq; XP_002674368.1; XM_002674322.1.
DR AlphaFoldDB; D2VNB4; -.
DR STRING; 5762.D2VNB4; -.
DR EnsemblProtists; EFC41624; EFC41624; NAEGRDRAFT_80631.
DR GeneID; 8851259; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_80631; -.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; D2VNB4; -.
DR OMA; ELMLPRK; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF923; PASG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Helicase {ECO:0000313|EMBL:EFC41624.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 211..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 524..675
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 85619 MW; 974EDF5C88B9082C CRC64;
MLSSNNVGSS SSGDEKSSLK KHTMHHHREE IDSSSALTET LDIEVVDEEH EKDLVKEEES
VAELIKDENV DEEKIDGDLP DQEEVEDESS APKAVKENFD KLNELLQKTE TYSRFIHEHV
VGEEEDDVKE EEQEEEEASE GEEEESNGKR KRKGRKATTT DESAQKKLKS VFSKSKTLQT
ANQAALKYSQ PKYLSGTTLR DYQLKGVNWL ISLYENGVNG ILADEMGLGK TIQTIGLFCH
LYEKGIKGPF LVVAPLSTVS NWVNEIDKWA PDIGCVLYHG NKDDRAIIRA KNFSKVKKGQ
IAVVVSSYEI VMRDKKFLAN KFNWKYIVVD EAHRLKNFNC RLTRELKTYS SENRLLLTGT
PLQNNLSELW SLLNFLLPSI FDDLSAFNKW FDFTKKEKND YITNEKTQLI SKLHNILRPF
LLRRLKSDVD IGIPKKREFL IYTHMTDMQK EYYNAVKSKD LLPIFKDQKR ANSTTLLNLL
MQMRKICNHP FLLREFETKD SESESASNKR FLKECTQNSG KFGLLVKMLE NLKKNGHKVL
IFSLMTRFLD VLEDYLECRG DMKYCRIDGS IAQTEREQKI KEFNQDEDVF CFLLSTRAGG
LGINLTAADT VIIYDSDWNP QIDLQAQDRC HRIGQKRSVR IFRLLTLGTV EKKVLQTATK
KLKLERLIIH KGNFKGNTQQ QSKMTITAQN LMEILDDTQV NNDSKHDEGI NDDILDRLIN
ERGDDSTLPA AGVGYEEAHI FQQDF
//
