ID D2V2V4_NAEGR Unreviewed; 1648 AA.
AC D2V2V4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49126.1};
GN ORFNames=NAEGRDRAFT_46260 {ECO:0000313|EMBL:EFC49126.1};
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:EFC49126.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49126.1,
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; GG738849; EFC49126.1; -; Genomic_DNA.
DR RefSeq; XP_002681870.1; XM_002681824.1.
DR STRING; 5762.D2V2V4; -.
DR EnsemblProtists; EFC49126; EFC49126; NAEGRDRAFT_46260.
DR GeneID; 8855116; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_46260; -.
DR eggNOG; KOG0950; Eukaryota.
DR InParanoid; D2V2V4; -.
DR OrthoDB; 208079at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd18026; DEXHc_POLQ-like; 1.
DR CDD; cd08638; DNA_pol_A_theta; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.20; -; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR046931; HTH_61.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048960; POLQ-like_helical.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF20470; HTH_61; 1.
DR Pfam; PF21099; POLQ_helical; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 200..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 417..624
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1648 AA; 188604 MW; 21D9BD09072CC8AB CRC64;
MISNNNHNKN KSQPTNVVAA TPLPKTLKNV SNPSSASSVS TTTPKSTGEA SVDFWPPFSQ
SSRSSMSVGS PSTPEDEYYF NIDEDLELSD ISDIEVEQLE NLDDDELNIG EESENTLDDE
LDISGIVNLL DEADSNNTIP SSDKTFSNTS NLLNTSLKAT HTEDDMNDPT SLYHYIPYQI
ADNYKHKSLY PWQVALLENN QILDGGKNII YSSPTSGGKT LVSEIIMVRR LTRNKSKVVF
MLPFKAIIEE KVADLNEKFK NVGWKANPYH SEAVKLIDTA SFNDDDERVM VCTFERGNSI
LNGLIRTGKI DEIGTIIIDE LHSITEPDRG YILELILTKI IYLKPKIQII AMSATLPNVD
KLASFLNAYL FVTDYRPVPL SEYMVHDSKV FDTNCNLVRN LTPYTVSKKL PDGFNISILS
LIDTEFATII FCSSKLKCKL FAKFIAEENQ PQHIPEHLVQ QRQELLTNLK LSTTGLDPDL
NFSMGRGVGF HHSSLTMEEK KLVELAFRNG MIKILLCTTT LATGVNLPAR RVIISSLTMG
RDDLSIVNYK QAAGRAGRAG IDVKGESYLI VPSLESGSKL LSSKFTPMKS CLNEKHISRA
LLENISTGII RTAHDIVSYL KCTFLSKCIP EKELRSIGIN SKVFLEKNGF IRWINGKDSF
DCKPLGFATQ IANICPYLSL KFYQTIKNEL KNFYLEDDLG MIYILASFSE NSLFHTDYND
TFSKVAEKIV NIAIKRREFS EFVNNKIRDI NELRGYILSV GNRSSHQREL SETIYTLRKT
FILYDIILEY PIKNIAETYF GDSDARGSVQ NVQKDAASKA SVLSSFCKYA ALPSFFSEAF
KEIKERLVSG VRQELVPLVQ IPFVGSSRAR LLFSAGLRTI AQVADETPES IENILVKGSQ
NTTESRTKAN LIVEGAKAIV EEKLLPLEWI FGPQDEDTFL FQNSSPKKRG KKRCNAFDDN
QAEHKKKKED SVIELKLGDN QLFDEFLERW NNSKVFSFCF EFGIKKKQDN PTTFIKNRDV
YTVKGLSICF NEVFEDYLTF EKRCETKIDP NIPCKCYFIH LDDYRSKIVK RMLQDKRKPK
LTFGFKKQQT RLLQAWDLIV KDPVLDPMIG DWVQHPDDSD NEKTLEEIYL KYFPSDSFLF
TPKNDKFVIV KTASQCWPIM TAVMVSIINL ELRQMFEFEM SFSKVLSTME HNGIRFNYHW
IKHNTKLIDA KLDEITRDLN SLQILDGKKI DVSNNDHVAL LLFDKLKLKG TERKTNKEIL
EKLKKLYPDK SYIMKQISEY RYLLNIKTHH IQNMPNDIKY CPDTQEYRIF ASQMQTTSAT
GRLSVKNPNL QNIPNDIDIK DPFSQKSIIT LSIRSAFIPR NGYVMVSIDY KNIELRILAH
LSQDRTLSDI LSNTERDIFE EIARNFWNFR PEEPVPLSHR SLVKQIIYGI SYCMGSETLS
GKMFNSENED FMLRPGEDRI EAAERYKQNF FEKYQGLKQY KDFVENHLVE KHYVETSYSR
KRFIHDICSD DSSKRAAARR AALNTVSQGS ASDIMKIVML GIYSFMRHFN KKEERAYMLL
QIHDELLFEV REDSLSTFIY CTKNIMQNTD KKLLVPLPVK VQIGDSWGTL KDYPSSIPLT
NEEKDEIRNL SVCLGFDWKE KLGVTDNF
//
