ID   J9HNF6_9SPIT            Unreviewed;       874 AA.
AC   J9HNF6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 41.
DE   SubName: Full=ADK domain containing protein {ECO:0000313|EMBL:EJY65344.1};
GN   ORFNames=OXYTRI_14502 {ECO:0000313|EMBL:EJY65344.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY65344.1};
RN   [1] {ECO:0000313|EMBL:EJY65344.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY65344.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJY65344.1}.
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DR   EMBL; AMCR01021508; EJY65344.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9HNF6; -.
DR   EnsemblProtists; EJY65344; EJY65344; OXYTRI_14502.
DR   OrthoDB; 178992at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd22967; DD_AK7; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR047499; DD_AK7.
DR   InterPro; IPR007858; Dpy-30_motif.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF105; ADENYLATE KINASE 7; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF13207; AAA_17; 1.
DR   Pfam; PF05186; Dpy-30; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          126..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          774..806
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        126..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  102423 MW;  C00CAF464213AD3D CRC64;
     MAKRIFINNI NSFVSQAIFN ELRNDITEDG EKSEDGNVIF GTYIDKDSSE KPEGINKMLK
     RSKPRLTMKY LSECDLLVYD LHAGNPRDVD LALQALKKHN FEEEKVLILI SSLMVWNKTP
     NKMKEIKEGK EGDEQDQENP DGLDEQPKDQ EDPVSKKNDD EDDDVSRGNK SNIDEDEEGQ
     QLEEQEPVKA PEPKPKVFVH LPFTEEDFMT RIPSAEYEEI KRIEDEILEF KKENVKTFVI
     ASGIMYGKGE SIFNNHFKKA WLQNPEKLPF IGEGKNLVPT IHVTDLARMV KKVYETKPEK
     NYIFAIDNTR RPTQKKLIQA ISSGIGTGGI ESFDFPETAR KLHPKKTPLQ LDLDWRIPLT
     LNLKLKPSAL FVSQNEEEEP VEFEWHCKEG LKHNINRVKE EFQKERGLKP FKIFITGPPA
     AGKSFFGKQL AEHYNVPHIH VGKMLEDIEK WDQERENAIL KKREIRRLKK EAEEKERLRI
     IQEVAEQKRQ AQLARGDDPD DPDKEDQKVE DKPIDENSQP QPDNEIADNE DEEKKQPELE
     DVESESDADW NEIDIKKMLK EFKTQNPGQR FPDELMNEAV RWRLNQNDCQ NRGYVLDGYP
     YSFEQAKGVF FITPKRPEKK IVIGEDGEPI PQEDEIDEEE MRRLLRPQFQ KSIYPDSVIL
     LRGTYGQVQQ NINKLSSEEL QKTHWMPVDL DRRITKYTDL NSINNFQQAI QGAQVALPTI
     RFFQENKTEI FELDCDGEKF EMFESMRIYI ERDGRPYNYL SSLDELNHKR EEQLKVEEYE
     MNEKKRKEDE AQNLSAKERI DELEKLADKR WIEIKKHMQD LEQCDKLNMR QFLMKYIIPV
     LTEGMIEVCK VGPIDPVDYL AEYIFKRSQE FRGQ
//