ID C0NE83_AJECG Unreviewed; 624 AA.
AC C0NE83;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=HCBG_02176 {ECO:0000313|EMBL:EEH10531.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH10531.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03173}.
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DR EMBL; GG663364; EEH10531.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NE83; -.
DR STRING; 447093.C0NE83; -.
DR VEuPathDB; FungiDB:I7I50_00249; -.
DR HOGENOM; CLU_013053_1_0_1; -.
DR InParanoid; C0NE83; -.
DR OrthoDB; 5491084at2759; -.
DR Proteomes; UP000001631; 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; 3.90.70.130; -; 1.
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 InterPro; IPR012462; UfSP1/2_DUB_cat.
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 Pfam; PF07910; Peptidase_C78; 2.
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:UP000001631};
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 DOMAIN 216..322
FT /note="UfSP1/2/DUB catalytic"
FT /evidence="ECO:0000259|Pfam:PF07910"
FT DOMAIN 323..391
FT /note="UfSP1/2/DUB catalytic"
FT /evidence="ECO:0000259|Pfam:PF07910"
FT REGION 98..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..504
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 557..567
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT COMPBIAS 98..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 624 AA; 70233 MW; 23AD697C6EBA703A CRC64;
MAQGGMEIDI LPCPFWPVAN DDDPLSGYVD CPHGCGEIIS TAELSSHLDL HIAEEMAFED
ASGGVVSKCE SEGEEIDANT DYIHDDIESR FSTKLPKELR NRDNILQPKS SRKGSHRDSK
AALGPSEKKK RKSKRGSRDA AGSFLRRLGR SELGPYAHEK QMPSWLRNML EEGAKVTVSN
QIQTDGTLRR VEHVANEMSN LIPVLARLCE LDETVEQVFL CHPTVRHVFK MPKEGGFCGY
RNIQMLVSHI QDTRADGYEQ FPGRLPTILR LQDLIEQAWD LGFNSNAQIE TGGIKGTRKY
IGTSEAQALF LSLGVKCEAG AFGHSLTIVG FEIRKSGSPN LLVFDPMFKT SPAIERLIGN
IRARPQDPRC LIKAYRRGPG YLHKYKEFEI LKCIDGNLPL TKISDKLRPN SFILFSFQHR
NISRTFLVLL PFLHLTLSSA ARTRKTKMRT LPNIIITGTP GVGKTVHCEQ LAQDTGLRHL
SINQVVKEHN CHEGYDDTFQ SYIVDDDKLL DAIEKDVPKG GYLIDWHACD LFPKSWIDLV
VVIRCNSTSI LYDRLAARGY SELKLQENLD VEIFDVLLQE ARESYDEEIV VELTSENDED
IESNCARIEA WIDSWKKARV ESSG
//
