ID A0A0S4TF38_CRYHO Unreviewed; 179 AA. AC A0A0S4TF38; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 22-FEB-2023, entry version 19. DE RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000256|HAMAP-Rule:MF_03173}; DE Short=AK6 {ECO:0000256|HAMAP-Rule:MF_03173}; DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03173}; DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000256|HAMAP-Rule:MF_03173}; DE Short=AK/ATPase {ECO:0000256|HAMAP-Rule:MF_03173}; GN ORFNames=CHUDEA3_3270 {ECO:0000313|EMBL:CUV05269.1}; OS Cryptosporidium hominis. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium. OX NCBI_TaxID=237895 {ECO:0000313|EMBL:CUV05269.1}; RN [1] {ECO:0000313|EMBL:CUV05269.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A., RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D., RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C., RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V., RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A., RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L., RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H., RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that CC catalyzes the reversible transfer of the terminal phosphate group CC between nucleoside triphosphates and monophosphates. Has also ATPase CC activity. {ECO:0000256|HAMAP-Rule:MF_03173}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC Evidence={ECO:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP- CC Rule:MF_03173}; CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03173}. 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; LN877949; CUV05269.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0S4TF38; -. DR VEuPathDB; CryptoDB:Chro.30373; -. DR VEuPathDB; CryptoDB:ChTU502y2012_401g0055; -. DR VEuPathDB; CryptoDB:CHUDEA3_3270; -. DR VEuPathDB; CryptoDB:GY17_00002555; -. DR OrthoDB; 5472563at2759; -. DR Proteomes; UP000199752; Chromosome 3. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00009; AAA; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1. DR PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1. DR Pfam; PF13238; AAA_18; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03173}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}. FT REGION 38..61 FT /note="NMPbind" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT REGION 118..128 FT /note="LID" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 17..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 44 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" SQ SEQUENCE 179 AA; 21025 MW; 34EE6DC5DF66221A CRC64; MLGKGRKPNI LIIGTPGTGK TSLSKKLEKK LEGYKRIELS KAIKKHRLYS EWDDKMGASI FDENLVRRYL KNQLDKYNSK NVGIILDFHS VNFIKRKWFD IVFCLNSETH VLFDRLEKRG YSQDKIKENV ECEIFKVIRF DATEIFDEEQ IIDLQSNDIC EQRSNIKFIL NKISSIENS //