ID   I7M2R5_TETTS            Unreviewed;      1014 AA.
AC   I7M2R5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Adenylate kinase {ECO:0000313|EMBL:EAS01156.2};
GN   ORFNames=TTHERM_00317200 {ECO:0000313|EMBL:EAS01156.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS01156.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220}.
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DR   EMBL; GG662605; EAS01156.2; -; Genomic_DNA.
DR   RefSeq; XP_001021401.2; XM_001021401.2.
DR   AlphaFoldDB; I7M2R5; -.
DR   STRING; 312017.I7M2R5; -.
DR   GeneID; 7833398; -.
DR   KEGG; tet:TTHERM_00317200; -.
DR   eggNOG; KOG3079; Eukaryota.
DR   InParanoid; I7M2R5; -.
DR   OrthoDB; 178521at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF220; ADENYLATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAS01156.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          200..253
FT                   /note="ATPase AAA-type core"
FT                   /evidence="ECO:0000259|Pfam:PF00004"
FT   REGION          846..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          964..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..997
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1014
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1014 AA;  118960 MW;  DC95C81097E0F48D CRC64;
     MSVTLNYEIS YLNPKIVFVS GGPGSGKGTQ CERLVRDYHF EHISVGDLVR DEIKRGTPEG
     QKFKDASAKG ELVPDHLVVA LIIKAIKSRK SFRFLIDGFP RNVEQAKMFE MKFKEIDYIL
     NFEVPDEILT SRLMGRGASS GRADDNPEAI ATRLRVFHNE TQPVLDFYNH FGKVKTMDGS
     KSVDEVYKQV QEQIKPNLIF MYGPPCVGKT ETARRLSEKI KYHFVNLEAF DKQHQVKSET
     DRINKLINYL QDAPHNNFII DSFFNSKNDA EVFLKHFSLP FRIFYYDSPK DEVMNNIQKY
     ILDEKERKRQ KDLYEQFIKC RGGILSLIQN QPYFVKVNSV DTIPNIIKFI LNNIRPLVIS
     AFTYNNTDLA LDYCDQLEKQ RDFIYLDVSE QCQSEIERGT NLGAKMNAFE QSGKEIPPKF
     QVELLQKILF ANPKQRRFII TKFPERNNQF EHFERELFPI DYLITFYMPQ QQVKYYHDNS
     PLLQFFAKGK YIHIDRLALD IVDAYINERS NYGFVLGPQA SGKSSIAKYV ASKFGYTLID
     WEQTFEFLKT KLGGEEGPLD ELTYEQVEKY FAETLNPAKN PSKTLFDGWP SVYNFAQFQQ
     FIKKLGLPSL GIDLQINKDI YVRRYKIKNE MDPEAEMSEE DQQKIDDLLA NASQYTQLIS
     QTAESNFGFT LYKLDVNHSL ESTTRYLNNI FFKRVYVVND YTTHHQQEVK EEQKLVFLNF
     CAKTNTTFVD VQEIIKLNYW QKTYNLHDQV QSEYAMRWTD QQPTFPSNYS PKLIIQAISN
     YLKTLKIPSR DILLYGYPSG DTPAERSSNE RFYPRASDEI YNIEKEVGPV RMVLVLTDNR
     LTWQISDEAR KLDPPPEKPK KAADEEGQEE EPPAEEEEEG KPKFNIFDYE WTTTNGLPKT
     IPQWYNKLKK TQKKHYSIKY NGSLNTYDKL LEYLRLINEE NPENKAEQEY RKVNLFVQLR
     YDEVPEHEEN EVEPPREQYK HIVPEEPKLI LPEEEFPEEQ QEKVEQQEEE EEDN
//