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Database: UniProt
Entry: A0A1X1BLB0_9APIC
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ID   A0A1X1BLB0_9APIC        Unreviewed;       168 AA.
AC   A0A1X1BLB0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
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=BXIN_1630 {ECO:0000313|EMBL:ORM40889.1}, BXIN_1788
GN   {ECO:0000313|EMBL:ORM40982.1};
OS   Babesia sp. Xinjiang.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=462227 {ECO:0000313|EMBL:ORM40889.1, ECO:0000313|Proteomes:UP000193856};
RN   [1] {ECO:0000313|EMBL:ORM40889.1, ECO:0000313|Proteomes:UP000193856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinjiang {ECO:0000313|EMBL:ORM40889.1,
RC   ECO:0000313|Proteomes:UP000193856};
RX   PubMed=27784333; DOI=10.1186/s13071-016-1846-1;
RA   Guan G., Korhonen P.K., Young N.D., Koehler A.V., Wang T., Li Y., Liu Z.,
RA   Luo J., Yin H., Gasser R.B.;
RT   "Genomic resources for a unique, low-virulence Babesia taxon from China.";
RL   Parasit. Vectors 9:564-564(2016).
RN   [2] {ECO:0000313|EMBL:ORM40889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Xinjiang {ECO:0000313|EMBL:ORM40889.1};
RA   Guan G.G., Korhonen P.K., Yin H.Y., Young N.Y., Gasser R.B.;
RL   Submitted (JUL-2016) 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|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: 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:ORM40889.1}.
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DR   EMBL; MBFZ01000037; ORM40889.1; -; Genomic_DNA.
DR   EMBL; MBFZ01000037; ORM40982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1BLB0; -.
DR   VEuPathDB; PiroplasmaDB:BXIN_1630; -.
DR   VEuPathDB; PiroplasmaDB:BXIN_1788; -.
DR   OrthoDB; 5472563at2759; -.
DR   Proteomes; UP000193856; 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, ECO:0000313|EMBL:ORM40889.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193856};
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         15..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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   168 AA;  18889 MW;  F8970FA6E9145066 CRC64;
     MRKNGVNILV TGTPGVGKTT LCKRVVDDVG LKYLNIADLI KAEKLHSEWD DELDCSIYDE
     KLLKKALAKK ELNSGGYLLD FHSVEGIDED DIDHVIVLTV EIENLSQRLT DRSYSDKKID
     ANIEAEIFKV CLQDAVDLFG EERVTELPNN TEEESLCALE HIKKLVKA
//
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