ID A7AUU0_BABBO Unreviewed; 172 AA.
AC A7AUU0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=BBOV_II007510 {ECO:0000313|EMBL:EDO06701.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO06701.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO06701.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO06701.1};
RX PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA Nene V.M.;
RT "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT hemoprotozoa.";
RL PLoS Pathog. 3:1401-1413(2007).
RN [2] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT invertebrate hosts.";
RL Data Brief 33:106533-106533(2020).
RN [3] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33069745;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Comparative analysis of gene expression between Babesia bovis blood stages
RT and kinetes allowed by improved genome annotation.";
RL Int. J. Parasitol. 51:123-136(2021).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDO06701.1}.
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DR EMBL; AAXT01000003; EDO06701.1; -; Genomic_DNA.
DR RefSeq; XP_001610269.1; XM_001610219.1.
DR AlphaFoldDB; A7AUU0; -.
DR STRING; 5865.A7AUU0; -.
DR EnsemblProtists; EDO06701; EDO06701; BBOV_II007510.
DR GeneID; 5478503; -.
DR KEGG; bbo:BBOV_II007510; -.
DR VEuPathDB; PiroplasmaDB:BBOV_II007510; -.
DR eggNOG; KOG3347; Eukaryota.
DR InParanoid; A7AUU0; -.
DR OMA; HHSCERF; -.
DR Proteomes; UP000002173; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000002173};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 35..58
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 41
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 172 AA; 19312 MW; 2EF06A3A5C82002B CRC64;
MRERGCNILV TGTPGVGKTR LCNHVASELG LTYVNVAELI RDEQLHSGWD SELDCSIYDE
RKLRKALKQR ELSRGGFILE FHSVDGIREG DIDHVLVLSA EIEILSKRLS DRGYGDKKID
CNIEAEIFKV CLQDAVDHFG EDKVVELPSN TESDFLGAVE HVRTLVNMAT LR
//
