ID A0A0S4JLR6_BODSA Unreviewed; 258 AA.
AC A0A0S4JLR6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
GN ORFNames=BSAL_32780 {ECO:0000313|EMBL:CUG91577.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG91577.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; CYKH01001941; CUG91577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4JLR6; -.
DR VEuPathDB; TriTrypDB:BSAL_32780; -.
DR OMA; QCETIKE; -.
DR OrthoDB; 168147at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR CDD; cd22981; DD_TbAK-like; 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; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ SEQUENCE 258 AA; 28269 MW; 8C9EDDF5ADDD509F CRC64;
MATGNLSEDA VAYLQEHKVE ALFESLLHDL LIGLPDKPLD HLLGLLRKLP TPKIVIAGPP
AGGKGTQCQK IVERFGVVHI STGDILRDHT QRGTEFGKKA SEYMSKGMLV PDDLIISLVK
DRLSQDDVFQ RGWLLDGFPR TRSQAISLQT AGIIPNALIV LDVSDSVVVN RIAGRRTDPA
TGAVYHTTAN PPPAGLHVIQ RADDTEEAIT VRLRLFHANL HEVLACYRSI SVHINGEQDK
DVVAAEVIEQ LEHRIVLV
//
