ID D2VXZ0_NAEGR Unreviewed; 1385 AA.
AC D2VXZ0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=DEXH-box helicase {ECO:0000313|EMBL:EFC38323.1};
GN ORFNames=NAEGRDRAFT_59568 {ECO:0000313|EMBL:EFC38323.1};
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:EFC38323.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC38323.1,
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; GG738909; EFC38323.1; -; Genomic_DNA.
DR RefSeq; XP_002671067.1; XM_002671021.1.
DR STRING; 5762.D2VXZ0; -.
DR EnsemblProtists; EFC38323; EFC38323; NAEGRDRAFT_59568.
DR GeneID; 8863517; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_59568; -.
DR eggNOG; KOG1000; Eukaryota.
DR InParanoid; D2VXZ0; -.
DR OrthoDB; 318617at2759; -.
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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18010; DEXHc_HARP_SMARCAL1; 1.
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 InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF06839; zf-GRF; 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.
DR PROSITE; PS51999; ZF_GRF; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EFC38323.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 12..55
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 126..166
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 346..521
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 648..826
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 57..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 878..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 156064 MW; 51BBFF7E747AC2DC CRC64;
MSDSHAPDLI QCKCGALAQL RVTKKGDNMG REYWACARNF GDRERCNFFK WSDNGVKPKP
SNNNFNNNNN NTPNRFIPPP SSFVNNSASS SSSSTFVQAS SSTIGSNNTN NNNNTNNDDD
IGAPLCPKHQ ITCVQKRVVK EGNNKGKLFW CCNIEHGCYF EWCKEGTKVA DYLLNPEIQN
RPLYSSTYSS KNTLGVHYPI SLQLVGSNIL QQAMKQQKDR HETLVFNNAN YDCVLVTFPK
LGFIMDKLLR SLKELFDNKI TKLNDLEYLF PLDQHETLRT FLLDVKIDGA SIQVQDFPEI
VKLIINNYPQ IDISKTDQLC NELDLAHKFP KQVWTKLRPF QKQGISFAVK REGRVLLGDE
MGVGKTLQGL STMYYFKQDW PLLIICPSSL KHNWGKEIEE WFITSERGHT DITMEKIKII
SHGKQIPDNY INIVSYTMAA NMLESQPCNN DGGGGGAILN GIKFNCIICD ESHYLKNSST
KRSSHIVPFL KQAKRLVMIT GTPALSRPVE VYPQLNLLLD DKFTFTRSAF TYRYCDAKET
QFGLDDKGSS NVLELNYLLS RTVMIRRRKE TVLSELPEKQ RQRVLLSVKP SDLKQLEFSA
ERMKRAIEKM KTAITSEEHN QSNFDKNSEI FRMYTMTGKA KLPAVKEYIQ DMIENTGDLK
FLVFAYHKEV MDGIEECVAL ELAKFYNLKG QKKKSKDLQK KMRGDYYIRI DGSTDSNRRQ
NLVNTFRTNG HCRVAILSIK AAGVGYTMTP CSTVLFAELY WTPSDLRQAE DRVHRMGQTN
AVSIKYLLGK DTFDEYLWPL LQKKLEVVGK SVDGESHVDR NVDQVIFDRT NTYDDNDNDE
DEYNEEDGSY AGGASSAYYQ DMKERDYLDE DEEEEYYEEL EKKKQKLKSS PSVKERESPK
LSQSNRSNSN TTNRGSNSRS VGSSSSTQSH HANEEDIRKV VPPPNSTATD FLKGFLCTKN
GKLPPNIILM RDDNNNSNTK IFNTSSSTQK KEYTYNKSFR DTNNNTKNNN TKKRHLDDEE
EEDDMKVNSD DDDDDITFGT PKKNNSSITQ KTSPFFSKLK SSSLLPNTSN LKQKLPNNNS
SSSSSSSNNI TTISNESNSG LNDDFMQDEQ EEKVNSSSFL NLSNAFKRTQ SDSIQSTKFV
TPSKFILPNN KTLPPKLLST SSQIPSIPSP VGNTNTNNTT TNITNNTSPP PNFNLSKTSP
PPSTPPNHNN NNNRLTNITP ENKPSELEQL LAKFSFQGSA SISPFAKRTP PTKSKTTTTT
TINNTINNTP LSISNNNNIN NIGSSSSNVN STTSLSTPKF IPPTFKSPIT TINRPSSSNS
SHSSAAVSSF TQHKSPPTFL PPKKPSIEPE PKKLKLDSIT PKTENNSLDI DDSDFILDDI
LPDIL
//
