ID   KAD6_RABIT              Reviewed;         172 AA.
AC   Q9TTU2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Adenylate kinase isoenzyme 6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE            Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03173};
DE   AltName: Full=Coilin-interacting nuclear ATPase protein {ECO:0000255|HAMAP-Rule:MF_03173};
DE   AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE            Short=AK/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
GN   Name=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
GN   Synonyms=CINAP {ECO:0000255|HAMAP-Rule:MF_03173};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RX   PubMed=11062043; DOI=10.1006/viro.2000.0604;
RA   Hou X., Foley S., Cueto M., Robinson M.A.;
RT   "The human T-cell leukemia virus type I (HTLV-I) X region encoded protein
RT   p13(II) interacts with cellular proteins.";
RL   Virology 277:127-135(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_03173};
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with COIL (via C-terminus).
CC       {ECO:0000255|HAMAP-Rule:MF_03173}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03173}. Nucleus, Cajal body {ECO:0000255|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:0000255|HAMAP-Rule:MF_03173}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03173}.
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DR   EMBL; AF195950; AAF09498.1; -; mRNA.
DR   RefSeq; XP_008260533.1; XM_008262311.2.
DR   AlphaFoldDB; Q9TTU2; -.
DR   SMR; Q9TTU2; -.
DR   STRING; 9986.ENSOCUP00000023998; -.
DR   GeneID; 103349645; -.
DR   KEGG; ocu:103349645; -.
DR   CTD; 102157402; -.
DR   eggNOG; KOG3347; Eukaryota.
DR   InParanoid; Q9TTU2; -.
DR   OrthoDB; 1488235at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
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; -; 1.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12595; PTHR12595; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transferase.
FT   CHAIN           1..172
FT                   /note="Adenylate kinase isoenzyme 6"
FT                   /id="PRO_0000153898"
FT   REGION          33..56
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   REGION          108..118
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         39
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT   BINDING         148..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
SQ   SEQUENCE   172 AA;  20079 MW;  D3CED96756590873 CRC64;
     MRLPNILLTG TPGVGKTTLG KELASRSGLK YVNVGDLARE GELYDGFDEE YNCPILDEDR
     VIDELDTQMR DGGVIVDYHG CDFFPERWFH IVFVLRTETS VLYKRLETRG YSEKKLNDNI
     QCEIFQVLYE EAMESYKEEI VHQLPSNKPE ELEENISQIL KWIEQWIKDH NS