ID Q5DAB1_SCHJA Unreviewed; 174 AA.
AC Q5DAB1;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 22-FEB-2023, entry version 71.
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 Name=Taf9 {ECO:0000313|EMBL:CAX72244.1};
GN ORFNames=EWB00_008108 {ECO:0000313|EMBL:TNN06910.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:AAW27245.1};
RN [1] {ECO:0000313|EMBL:AAW27245.1}
RP NUCLEOTIDE SEQUENCE.
RA Han Z.;
RT "The full-length cDNA sequences of Schistosoma japonicum genes.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW27245.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA Liu F., Lu J., Hu W., Wang S.Y., Cui S.J., Chi M., Yan Q., Wang X.R.,
RA Song H.D., Xu X.N., Wang J.J., Zhang X.L., Zhang X., Wang Z.Q., Xue C.L.,
RA Brindley P.J., McManus D.P., Yang P.Y., Feng Z., Chen Z., Han Z.G.;
RT "New perspectives on host-parasite interplay by comparative transcriptomic
RT and proteomic analyses of Schistosoma japonicum.";
RL PLoS Pathog. 2:268-281(2006).
RN [3] {ECO:0000313|EMBL:CAX72244.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72244.1};
RX DOI=10.1038/nature08140;
RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT "The Schistosoma japonicum genome reveals features of host-parasite
RT interplay.";
RL Nature 460:345-351(2009).
RN [4] {ECO:0000313|EMBL:CAX72244.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX72244.1};
RA Gang L.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:TNN06910.1, ECO:0000313|Proteomes:UP000311919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuSjv2 {ECO:0000313|EMBL:TNN06910.1};
RC TISSUE=Worms {ECO:0000313|EMBL:TNN06910.1};
RA Hu W., Luo F., Yin M., Mo X., Sun C., Wu Q., Zhu B., Xiang M., Wang J.,
RA Wang Y., Zhang T., Xu B., Zheng H., Feng Z.;
RT "An improved genome assembly of the fluke Schistosoma japonicum.";
RL Submitted (MAR-2019) 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. May have a role in
CC nuclear energy homeostasis. Has also ATPase activity.
CC {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 -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03173}.
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DR EMBL; AY815513; AAW27245.1; -; mRNA.
DR EMBL; FN316513; CAX72244.1; -; mRNA.
DR EMBL; SKCS01000446; TNN06910.1; -; Genomic_DNA.
DR EMBL; SKCS01000446; TNN06912.1; -; Genomic_DNA.
DR EMBL; SKCS01000446; TNN06913.1; -; Genomic_DNA.
DR EMBL; SKCS01000446; TNN06914.1; -; Genomic_DNA.
DR EMBL; SKCS01000446; TNN06916.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5DAB1; -.
DR Proteomes; UP000311919; Unassembled WGS sequence.
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:0016310; P:phosphorylation; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03173, ECO:0000313|EMBL:TNN06910.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW Reference proteome {ECO:0000313|Proteomes:UP000311919};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 36..59
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 111..121
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 16..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 174 AA; 19779 MW; 0A8D2188461086A4 CRC64;
MPAGTLPNIL ITGTPGTGKT TVSKEVSERS SLNYISINEV AKEGELYDGY DEANECYILD
EDRIVDELED AMSSGGQIID YHSCEFFPER WFDAVFVLRT DNTILYPRLT SRDYSSKKVS
DLIHCEIVQV ILDEARESYN TDIVHELINN TPEDLESNVS QICGWIKQWR AEKS
//
