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Database: UniProt
Entry: A0A0B0MWL5_GOSAR
LinkDB: A0A0B0MWL5_GOSAR
Original site: A0A0B0MWL5_GOSAR 
ID   A0A0B0MWL5_GOSAR        Unreviewed;       177 AA.
AC   A0A0B0MWL5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-SEP-2023, entry version 37.
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=F383_28174 {ECO:0000313|EMBL:KHG03291.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG03291.1, ECO:0000313|Proteomes:UP000032142};
RN   [1] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) 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:KHG03291.1}.
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DR   EMBL; JRRC01342005; KHG03291.1; -; Genomic_DNA.
DR   RefSeq; XP_017626402.1; XM_017770913.1.
DR   AlphaFoldDB; A0A0B0MWL5; -.
DR   SMR; A0A0B0MWL5; -.
DR   GeneID; 108469850; -.
DR   KEGG; gab:108469850; -.
DR   OMA; QCEIFGT; -.
DR   OrthoDB; 5472563at2759; -.
DR   Proteomes; UP000032142; 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:KHG03291.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   REGION          40..63
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   REGION          115..125
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         20..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         46
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         86
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"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ   SEQUENCE   177 AA;  19945 MW;  8565E701DAD0F39C CRC64;
     MAADGNKRKR PNILVTGTPG TGKTTTSSAL AEATNLRHIN IGDLVKEKNL HDGWDDDLQC
     HVINEDLVCD ELEDVMEEGG NIVDYHGCDF FPERWFDLVV VLQTDNTVLY DRLSKRGYEG
     AKLSNNIECE IFQVLLEEAK ESYSEDIVKA LKSNNIDDIT RNVSSLTDWI RSWPPTS
//
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