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Database: UniProt
Entry: D2VMD7_NAEGR
LinkDB: D2VMD7_NAEGR
Original site: D2VMD7_NAEGR 
ID   D2VMD7_NAEGR            Unreviewed;       793 AA.
AC   D2VMD7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=NAEGRDRAFT_50744 {ECO:0000313|EMBL:EFC41970.1};
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:EFC41970.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC41970.1,
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC       subfamily. {ECO:0000256|ARBA:ARBA00009334}.
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DR   EMBL; GG738882; EFC41970.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2VMD7; -.
DR   STRING; 5762.D2VMD7; -.
DR   EnsemblProtists; EFC41970; EFC41970; NAEGRDRAFT_50744.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_50744; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   InParanoid; D2VMD7; -.
DR   OrthoDB; 5473705at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025197; DUF4116.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF57; ATP-DEPENDENT RNA HELICASE DDX1; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13475; DUF4116; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          429..604
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   793 AA;  93430 MW;  51E1FDE8A72EE8A2 CRC64;
     MLDREQLVFN VDVAFIVQSF LNDSDRRNCE QVSINFHRAC NTLERLEFRD RLQNVELNLI
     REKFDKSSIA SSPKRVFSSA EEVFNEDIEM EIEAFERKHI KIPFHLKEYL RMSVHLDPYL
     ILDILKEYVF MHPLTVLCPL SDWIVIREGE EYLIGEFSNS SGRESFIFTL NQKQNGKCSI
     FMTITKNNNF GYDQIISYTT KKRVEIGTLK RWFNNYGFGW FVNRNIFHYS FHNSLQRNHL
     DLFQISRNTT SSFNSQHIYN LIKNYKFVFP GALMEKYSID LLREGLITLK QLKENLRKDP
     RIIDMAVRCN GLNLEFVGKE YHRNEEMVRK AISQNGLALK FASKSVRMNK DIVEMAYRQN
     KYALKYSLLS PKEDSKTISD RFLKYFSFNQ DPNCEIETLF PNNDYLLRCI YGFGLEYFSQ
     YQVDMIKRCQ REDNTAQNIL FQAPSVGKTL ASLIVALERI QKFKSILGSG IHCLILCPNR
     ELVIKVARLF SSLLMWNDIN IITAHGGHIE KLYFYNYETY MPCTPMEVDF SRKTETSPNP
     SILIGTPGRL ALDDLRSGMF ELNKVHTIIY EEADTLLSGE YDSLTHIMRE IEEYNPNCKL
     MNIVLCQTLT ERMYFKMNTT FNQNLEYFYK EEKFAFLKPL SLLRGFIDHE IVSVEDLSDT
     EVHNLKLDLL KKNGDEIPLL VAFGNRRSIE RYIDGNQSIL ISILHSDMEQ RDRELVWKEA
     NELTCQVLST TDINSNAMLL TREIHTVFQF DFPSSEEIFI KRIRYALFRE NKMKVITFVN
     SKKQERRILK WLR
//
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