ID M3X272_FELCA Unreviewed; 172 AA.
AC M3X272;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 65.
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:ENSFCAP00000020719.2,
GN ECO:0000313|VGNC:VGNC:67575};
GN Synonyms=CINAP {ECO:0000256|HAMAP-Rule:MF_03173};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000020719.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000020719.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020719.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000020719.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020719.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000020719.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020719.2};
RG Ensembl;
RL Submitted (SEP-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}.
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DR EMBL; AANG04002524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006927836.2; XM_006927774.3.
DR AlphaFoldDB; M3X272; -.
DR PaxDb; 9685-ENSFCAP00000020719; -.
DR Ensembl; ENSFCAT00000028701.4; ENSFCAP00000020719.2; ENSFCAG00000031227.4.
DR GeneID; 109491348; -.
DR KEGG; fca:109491348; -.
DR CTD; 102157402; -.
DR VGNC; VGNC:67575; AK6.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00940000155097; -.
DR HOGENOM; CLU_079096_3_3_1; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 5472563at2759; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000031227; Expressed in testis and 9 other cell types or tissues.
DR GO; GO:0015030; C:Cajal body; 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 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 PRINTS; PR01100; SHIKIMTKNASE.
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:UP000011712};
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"
FT BINDING 148..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 172 AA; 19929 MW; F26513F1685C8EDE CRC64;
MLLPNILLTG TPGVGKTTLG KELASRSGLK YINVGDLARE GQLYDGYDEE YDCPILDEDR
VVDELENQMS EGGVIVDYHG CDFFPERWFH IVFVLRADNS VLYKRLETRG YNEKKLKDNI
QCEIFQVLYE EALASYKEEI VHQLPSNKPE DLEDNINQIL KWIEQWIKDH SS
//
