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
//