ID H0XXB2_OTOGA Unreviewed; 172 AA.
AC H0XXB2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Adenylate kinase isoenzyme 6 {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=Coilin-interacting nuclear ATPase protein {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 Name=AK6 {ECO:0000256|HAMAP-Rule:MF_03173,
GN ECO:0000313|Ensembl:ENSOGAP00000020755.1};
GN Synonyms=CINAP {ECO:0000256|HAMAP-Rule:MF_03173};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000020755.1, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000020755.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. May have a role in
CC nuclear energy homeostasis. Has also ATPase activity. May be involved
CC in regulation of Cajal body (CB) formation. {ECO:0000256|HAMAP-
CC 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 -!- SUBUNIT: Monomer and homodimer. Interacts with COIL (via C-terminus).
CC {ECO:0000256|HAMAP-Rule:MF_03173}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000256|HAMAP-
CC Rule:MF_03173}. Nucleus, Cajal body {ECO:0000256|HAMAP-Rule:MF_03173}.
CC Note=Displays widespread diffuse nucleoplasmic distribution but not
CC detected in nucleoli. Detected in Cajal bodies but not in all cells.
CC {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; AAQR03039740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03039746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003785934.1; XM_003785886.2.
DR AlphaFoldDB; H0XXB2; -.
DR STRING; 30611.ENSOGAP00000020755; -.
DR Ensembl; ENSOGAT00000033352.1; ENSOGAP00000020755.1; ENSOGAG00000027736.1.
DR GeneID; 100952269; -.
DR KEGG; oga:100952269; -.
DR CTD; 102157402; -.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00390000015930; -.
DR HOGENOM; CLU_079096_3_3_1; -.
DR InParanoid; H0XXB2; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 5472563at2759; -.
DR TreeFam; TF313388; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 33..56
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 108..118
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 13..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 172 AA; 19912 MW; 7E0263C564D803CD CRC64;
MLLPNILLTG TPGVGKTTLG KELASRSGLK YINVGDLAKE GQLYDGYDEE YECPMLDEDR
VVDELDNQMT EGGVIVDYHG CDFFPERWFH VVFVLRTNTS ELYKRLETRG YNEKKLKDNI
ECEIFQVLYE EATASYKEEI VHQLPSNNPA ELENNIDFIL KWIEQWVQVH NS
//
