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Database: UniProt
Entry: D2VXT3_NAEGR
LinkDB: D2VXT3_NAEGR
Original site: D2VXT3_NAEGR 
ID   D2VXT3_NAEGR            Unreviewed;       736 AA.
AC   D2VXT3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Adenylate kinase {ECO:0000313|EMBL:EFC38346.1};
GN   ORFNames=NAEGRDRAFT_59535 {ECO:0000313|EMBL:EFC38346.1};
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:EFC38346.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC38346.1,
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220}.
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DR   EMBL; GG738908; EFC38346.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2VXT3; -.
DR   STRING; 5762.D2VXT3; -.
DR   EnsemblProtists; EFC38346; EFC38346; NAEGRDRAFT_59535.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_59535; -.
DR   eggNOG; KOG3078; Eukaryota.
DR   InParanoid; D2VXT3; -.
DR   OMA; VEDFRWT; -.
DR   OrthoDB; 5472436at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01351; adk; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFC38346.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   736 AA;  86139 MW;  22DABF4886BE863A CRC64;
     MSSIRSIYLL STNPLKLPEY VRNFDRYGVR VVIRDPKDFD TDQKKLEFLQ QNTSAICFIC
     DQMDLFKKGT SERAKLEHLE LVESSTELTV WQLNKEKDAL VKKVFKNVQY GFIDLSRKKP
     NLLRKTVFGW DDVFVNLYSG KSNLDQIESG GSKISSRDMA ISEYIKERFY YSKRKDLNFT
     PQNITERTID FRKSVLTYFE GHNLYNNEST RKYKITNVWK TVVNDGLVFK SSKNRRENNY
     FSTLLNPALP LVSKRDPIHE TTFQMHDCGH FCILELIYTG YESTELQKLV YIAFRMISEA
     VTMMMADVLF IHALKMQGIE FVPFFVEDYK WNANNYQNME TRKEEIKKWW DSVEHVRHYT
     PEIRFLTIDE FIAHMENYTP SELTSLHTDE IVDIVFETVW QEMVKPVFEK DTIEVLPEER
     RNFNTFVRYM CGQLAIFSAF ETPESSIYRD GILKFIKEKA KTKTMTIDEI ENAETFFGAY
     VDLLAQKNMI TYDDASTYKE IYPMFEPCYV FYDENKSYYD SLSNVYKRLF KIPHRIIIMG
     LPGCGKGTQS KLIAEKYGLV HISTGDLVRE VISKQTELGK KCEAIINTGG LLPDELINPI
     FLDRILKEDC KTKGWILDGY PRTTSNLEFV RANRLNVTGV IFLTLDDDTA IERQCGRITD
     PLTGAIYHSK FLPPTEEIRE RLVKRATDNE EKAKIRVKVY HDEMDQAFDW FPEEISHKID
     ATPSPEEVFE AIKKLL
//
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