ID A0A0S4TF38_CRYHO Unreviewed; 179 AA. AC A0A0S4TF38; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 24-JUL-2024, entry version 22. 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. Involved in the late cytoplasmic maturation steps of the 40S CC ribosomal particles, specifically 18S rRNA maturation. While NMP CC activity is not required for ribosome maturation, ATPase activity is. CC Associates transiently with small ribosomal subunit protein uS11. ATP CC hydrolysis breaks the interaction with uS11. May temporarily remove CC uS11 from the ribosome to enable a conformational change of the CC ribosomal RNA that is needed for the final maturation step of the small CC ribosomal subunit. Its NMP activity may have a role in nuclear energy CC homeostasis. {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 -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03173}; CC -!- SUBUNIT: Interacts with small ribosomal subunit protein uS11. Not a CC structural component of 43S pre-ribosomes, but transiently interacts CC with them by binding to uS11. {ECO:0000256|HAMAP-Rule:MF_03173}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173}. CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03173}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03173}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03173}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03173}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}; KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP- KW Rule:MF_03173}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_03173}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW 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 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173" FT BINDING 22 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 //