ID A0A0D9QSL0_PLAFR Unreviewed; 565 AA.
AC A0A0D9QSL0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Nucleoside-diphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK88_00409 {ECO:0000313|EMBL:KJP89953.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP89953.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP89953.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ001647; KJP89953.1; -; Genomic_DNA.
DR RefSeq; XP_012333483.1; XM_012478060.1.
DR AlphaFoldDB; A0A0D9QSL0; -.
DR EnsemblProtists; KJP89953; KJP89953; AK88_00409.
DR GeneID; 24265723; -.
DR VEuPathDB; PlasmoDB:AK88_00409; -.
DR OMA; NLFNYKH; -.
DR OrthoDB; 261519at2759; -.
DR Proteomes; UP000054561; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF128; PUTATIVE-RELATED; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..565
FT /note="Nucleoside-diphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002344221"
FT REGION 205..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 246..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 565 AA; 64826 MW; 9939919BF55FAB51 CRC64;
MKNGRGVSNK PFRLLALVCA MIMCLGMSAS AKETIDGNHL YKSVVIDAGS TGTRVHIYNY
KIVYEKKGIN IHIPSISYRT TPGVVYLLNN YFANDEKIAF HEYFKNIKEF LYEHVKVNER
SSTPIMIRAS GGFRLLSITE SENYINFVKQ YFLNNFSDFL LIDELLIKVL SGKEEAILSF
VSIYALLEKF NPSPVTFTNL DKASGSTTSE VLTGKDSQEE KLSKESNGKT SNNGENDIIG
VLELGGATAQ VVIKFPLSKM NEDIKNLFNY KHREEKVKKS VIEENYKNKN VVKIHLFDED
IYLYCKSYLV LGRQNAMKTY LHYIIHQHNR EEQVDDQGFT GGEKNAPAGV DVKKDTRDKN
KFIPAACFPK DFKFYVNNLY ETSIEEEMHE YDGKTEMSEH DYVAVGTGNI DLCRLQVQSI
LNYAQIDDLP FKMKRFIKLY GIENFHHFAM DILNLPESFN PISLNSNMYL EKAKEICPLT
IDEIVKVVRP EANIEKAQTS CFGLIFLYEF MRYILKIDEP IAFQSTNYIN KISITWTVAV
LLMELPPHLN TIKKQTQEPY LNDEL
//
