ID A0A0S4TF38_CRYHO Unreviewed; 179 AA. AC A0A0S4TF38; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 11-DEC-2019, entry version 11. 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; Alveolata; Apicomplexa; Conoidasida; Coccidia; Eucoccidiorida; OC Eimeriorina; Cryptosporidiidae; Cryptosporidium. OX NCBI_TaxID=237895 {ECO:0000313|EMBL:CUV05269.1, ECO:0000313|Proteomes:UP000199752}; RN [1] {ECO:0000313|Proteomes:UP000199752} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Alzate J.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|HAMAP-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 OrthoDB; 1488235at2759; -. 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:ATPase activity; IEA:UniProtKB-UniRule. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12595:SF0; PTHR12595:SF0; 1. DR SUPFAM; SSF52540; SSF52540; 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 NP_BIND 17..22 FT /note="ATP" FT /evidence="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 44 FT /note="AMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 89 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 115 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 119 FT /note="ATP" 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 //