ID A0A0W8DGR2_PHYNI Unreviewed; 161 AA.
AC A0A0W8DGR2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 27.
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=AM587_10017192 {ECO:0000313|EMBL:KUF64516.1}, AM588_10009089
GN {ECO:0000313|EMBL:KUF95476.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF95476.1, ECO:0000313|Proteomes:UP000054636};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUF64516.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, Race 1
RC {ECO:0000313|EMBL:KUF95476.1}, and race 1
RC {ECO:0000313|Proteomes:UP000054636};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-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. {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:KUF95476.1}.
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DR EMBL; LNFO01006129; KUF64516.1; -; Genomic_DNA.
DR EMBL; LNFP01000223; KUF95476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8DGR2; -.
DR STRING; 4790.A0A0W8DGR2; -.
DR EnsemblProtists; KUF64516; KUF64516; AM587_10017192.
DR EnsemblProtists; KUF95476; KUF95476; AM588_10009089.
DR OMA; QCEIFGT; -.
DR OrthoDB; 5472563at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; 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:KUF64516.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 96..106
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 27
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 161 AA; 18563 MW; F4719D46638E06C1 CRC64;
MTRGPNILVT GTPGTGKTSM CQQLAVKERG LHNGRDEEFD CFVLDEDKVC DEMEDMMAEG
GKVVDFHTCD FFPERWFDLV VVLRVDNTTL FDRLQKRGYS EKKVAENVEC EIMEVVLQEA
RESYAPEIVQ ELPSRTVEDM ESNIERVLTW VQHWMAQHTG N
//
