ID C6HG89_AJECH Unreviewed; 964 AA.
AC C6HG89;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=HCDG_05429 {ECO:0000313|EMBL:EER40840.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER40840.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
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.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-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; GG692425; EER40840.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HG89; -.
DR STRING; 544712.C6HG89; -.
DR VEuPathDB; FungiDB:HCDG_05429; -.
DR eggNOG; KOG3347; Eukaryota.
DR HOGENOM; CLU_013053_1_0_1; -.
DR OMA; PFCPFSD; -.
DR Proteomes; UP000002624; 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; -; 2.
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:UP000002624};
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 574..680
FT /note="UfSP1/2/DUB catalytic"
FT /evidence="ECO:0000259|Pfam:PF07910"
FT DOMAIN 681..749
FT /note="UfSP1/2/DUB catalytic"
FT /evidence="ECO:0000259|Pfam:PF07910"
FT REGION 451..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..844
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 897..907
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT COMPBIAS 451..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 827
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 867
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 894
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 964 AA; 109138 MW; 069E32FA1BC7F204 CRC64;
MSLENEPLFF RPYNALIQPP EIDTLTDYYP EFDESPFRNA ENLSWYLNQY FQNCTLPNQD
LNPPGSSYID FGSFKFGKLM DVFKHPRWQV QAAWNIAHAT VPHMKVLMYS GIIGNRDELF
RGELLAIIDV MCRRLNTKSL RPHIIAPVLL FSVVGMHHIR VLEAYFNGKE LVLVLCLVVI
LCKGHESLEA ARLESYSPAS PAPFTASVRS NLSLQNLNTL TTVSLYDPAD QQIRWNLVKS
PPVLIWSFER KRSHAKPDMT SIKLSRANNQ EPICCHRFQN PPPFTCRCRN VCSCNRFSKS
LFLMAQGGME IDILPCPFCE FSDSDPYFLT QHVELCHPEN GTSPFSAIEE PCASAQDLNH
SNTYKKDSPV DYTGHVANDD DPLSGYVDCP HGCGEIISTA ELSSHLDLHI AEEMAFEDAS
GGVVSKCESE GEEIDANTDY IHDDIESRFS TKLPKELRNR DNILQPKSSR KGSHRDSKAA
LGPSEKKKRK SKRKSHDAAG SFLRRLGRSE LGPYAHEKQM PSWLRNMLEE GAKVTVSNQI
QTDGTLRRVE HVANETSNLI PVLARLCELD ETVEQVFLCH PTVRHVFKMP KEGGFCGYRN
IQMLVSHIQD TRADGYEQFP GRLPTILRLQ DLIEQAWDLG FNSNAQIETG GIKGTRKYIG
TSEAQALLFS LGIKCEAGAF GHSLTIVGFE IRKSGSSNLL VFDPMFKTSP AIERLIGNSR
ARLQDPRCLI KAYRRGPGYL HKHKEFEILK YRTNYAQTHR NISRTFLVLL PFLHLTLSSA
ARTRKTKMRT LPNIIITGTP GVGKTVHCEQ LAQDTGLRHL SINQVVKEHN CHEGYDDTFQ
SYIVDDDKLL DAIEKDVPKG GYLIDWHACD LFPKSWIDLV VVIRCNSTSI LYDRLAARGY
SELKLQENLD VEIFDVLLQE ARESYDEEIV VELTSENDED IESNCARIEA WIDSWKKARV
ESSG
//
