ID A0A0S4TF38_CRYHO Unreviewed; 179 AA. AC A0A0S4TF38; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 18-JAN-2017, entry version 4. 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; OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium. OX NCBI_TaxID=237895 {ECO:0000313|EMBL:CUV05269.1}; RN [1] {ECO:0000313|EMBL:CUV05269.1} RP NUCLEOTIDE SEQUENCE. 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., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase CC that catalyzes the reversible transfer of the terminal phosphate CC group between nucleoside triphosphates and monophosphates. Has CC also ATPase activity. {ECO:0000256|HAMAP-Rule:MF_03173}. CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {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 GO; GO:0005634; C:nucleus; IEA:UniProtKB-HAMAP. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. 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 ATP. {ECO:0000256|HAMAP-Rule:MF_03173}. FT REGION 38 61 NMPbind. {ECO:0000256|HAMAP-Rule: FT MF_03173}. FT REGION 118 128 LID. {ECO:0000256|HAMAP-Rule:MF_03173}. FT BINDING 44 44 AMP. {ECO:0000256|HAMAP-Rule:MF_03173}. FT BINDING 89 89 ATP. {ECO:0000256|HAMAP-Rule:MF_03173}. FT BINDING 115 115 ATP. {ECO:0000256|HAMAP-Rule:MF_03173}. FT BINDING 119 119 ATP. {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 //