ID A0A162PH49_PHYB8 Unreviewed; 186 AA.
AC A0A162PH49;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=PHYBLDRAFT_113332 {ECO:0000313|EMBL:OAD72777.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD72777.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-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. May be involved in rRNA maturation and transcription
CC regulation. {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 -!- 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}.
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DR EMBL; KV440982; OAD72777.1; -; Genomic_DNA.
DR RefSeq; XP_018290817.1; XM_018428339.1.
DR AlphaFoldDB; A0A162PH49; -.
DR STRING; 763407.A0A162PH49; -.
DR GeneID; 28989245; -.
DR VEuPathDB; FungiDB:PHYBL_113332; -.
DR InParanoid; A0A162PH49; -.
DR OrthoDB; 5472563at2759; -.
DR Proteomes; UP000077315; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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|HAMAP-Rule:MF_03173};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03173};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03173};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_03173};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_03173};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_03173};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..71
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 123..133
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 28..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 54
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 186 AA; 21262 MW; B66FE175D19CF962 CRC64;
MSASDSDDQP IEIPDRPIPN ILVTGTPGTG KTTTSELIAQ VTGLQHVNVG AIVKAKQLHE
GYLEEFDTHV LDEDKLIDEL EDTMTEGGKI VDFHTCEIFP ERWFDLVIVL RADTATLYDR
MEKRGYNKRK IEENMECEIM QIVLENAHES YEPEIVVELQ SNTVDDMESN VERVKQWLDA
YRARHA
//
