ID   GDT9_DICDI              Reviewed;        1577 AA.
AC   Q5VJL3; Q1ZXI4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable serine/threonine-protein kinase gdt9;
DE            EC=2.7.11.1;
DE   AltName: Full=Growth-differentiation transition protein 9;
DE   AltName: Full=Protein kinase Dusty;
DE   Flags: Precursor;
GN   Name=gdt9; ORFNames=DDB_G0278879;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Huang C.-H.;
RT   "Organization of slime mold dusty protein kinase gene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GDT family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC       superfamily. TKL Ser/Thr protein kinase family. {ECO:0000305}.
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DR   EMBL; AY429682; AAS55398.1; -; mRNA.
DR   EMBL; AY429683; AAS55399.1; -; Genomic_DNA.
DR   EMBL; AAFI02000024; EAS66889.1; -; Genomic_DNA.
DR   RefSeq; XP_001134573.1; XM_001134573.1.
DR   AlphaFoldDB; Q5VJL3; -.
DR   SMR; Q5VJL3; -.
DR   STRING; 44689.DDB0232936; -.
DR   PaxDb; Q5VJL3; -.
DR   EnsemblProtists; EAS66889; EAS66889; DDB_G0278879.
DR   GeneID; 8621755; -.
DR   KEGG; ddi:DDB_G0278879; -.
DR   dictyBase; DDB_G0278879; gdt9.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_251247_0_0_1; -.
DR   InParanoid; Q5VJL3; -.
DR   OMA; CHKEEND; -.
DR   PhylomeDB; Q5VJL3; -.
DR   PRO; PR:Q5VJL3; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0050793; P:regulation of developmental process; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR026237; STKINASEGDT.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR02079; STKINASEGDT.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..1577
FT                   /note="Probable serine/threonine-protein kinase gdt9"
FT                   /id="PRO_0000323586"
FT   TOPO_DOM        17..966
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        967..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        988..1577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1290..1573
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          998..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1436
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         1296..1304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1317
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        283
FT                   /note="N -> K (in Ref. 1; AAS55398/AAS55399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1274..1275
FT                   /note="CV -> WG (in Ref. 1; AAS55398/AAS55399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1552
FT                   /note="I -> R (in Ref. 1; AAS55398/AAS55399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1559
FT                   /note="L -> R (in Ref. 1; AAS55398/AAS55399)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1577 AA;  175900 MW;  8473361205CCE7ED CRC64;
     MKTFLLIFLL ICVCKGITNI TTPSIYFDLK KINRFQDYLN NGITPSINLT FHDFYYPDVC
     VNTIKNIDGS TNFVKSSFLN APTNFANLYI TKGSKMTVKP NQILGAFINI LCIEGSLEVP
     VGVFPFFIGA LVILPGGNFK SESSFRFMNL VNSKIDPLNF FPGILTLGGS LSILGPKSIK
     YSANRLGDFQ FQLLELIDPN SFNSDYKANI YSESFVTGQQ CDFVSITNGY TLTVGGCQGV
     PSTDVNIYIF FATVDYDCTF IDSDSEVPAS IYISGDTNVH IENFFLNSLG KTTNANYNDT
     ILIFSPTDDT NVTDIIIGTN QRYRNSLFVE FSNNVTLRNN FIRESIESRS PLMFFASSPI
     LEGNLVVSNS GSSVIAQFGT EFIQSTNNSY FLEPPTQPVI PNDNNMDYGT EGNGIYSLSP
     IVSFTTDVFV GQLISINFNF IANRSLVTGF NYDCFAPCYP GSPIISNLVQ HSVDFNIIKP
     TFSYSHGNTT SSTTTSSTTT NTNSHFLLNV NDNGNEPSSY YSFNQLSIAS EAIKVNLPIG
     TLGIGNLFAT NNFKIDGALE RLDILNSIFN LPPPISNNFS QSGILLSTTT SMLNSYVFVS
     IGSEPTRIES QIYGSTITPY YYNNIETLDL FQIQSIFPSV QYQIIKNSTI NITINITTTT
     TTTTTPTTNN VVCSFTSIVN QQSSVTNEIS INETLIQMDP ILNNCVFPLS IDQEGSLKLR
     VTIKNQNSTL ENQYYYIIDF PEITIFQSFQ FYTGIKFIDV QSSSSSSQQT SSFSPTTTTF
     LNLLSTTENS NGFLNGCQIS NQCTLSNNVK YVSSLPNVTN SPDFQLFQSG ITPIIPYDPV
     VINLGIEKNK TFQFQLFFTF YQPIDQYSSP LSIFIQSEPY LLLDPLIDAP NFKNFTFFYD
     NLNQDSIEIS FISRGDIYLT SMAIYSLDLV SYESSDSSSS SSNSSSSTGN GIGDIVNNED
     NHKKLVIALS VSIPVAALLV ILCFGIFICY NNNKKNKNET KGKDIETNTD KKDDENENEN
     CKFQFKDEFL TNPNEINIQL KKLMINKSST LPPQSTISID TSPSSENTTF TESLTPKKSA
     TVNGEIDFSR NSTNESTVSN SSSENNSDNN NNNNNKCKKE KLSSFPTIPG TNLTNIPLNL
     VGRKSRNPED KYRTNNDILV CLQESHYFKP DDPSIPIEFS ESVLDFGRGS KCLIDETYIY
     TISVKNKSTT DYNILLILPI DNNTGTISTD TQYFQINAGE SKPISFSISL NCTTKYFEKI
     GVSIEELNYH TFICVHMESE LSTRLDFSEL DFDEICGQGT YGMVYKGKWR SQVVAIKMMR
     VGTVNCDEVY REMDIMGKIR HQNVISFIGC VVSLEHLCIV TEFSPIGSLG DLIHGDNNQK
     KSNTNTITNT ITNTNTNTNT STSTSTKLTV KQKLRIAIDI ARGCQFLHQC GIIHRDLKPD
     NVLVFDINHN APVCAKISDF GTSKETNEFS NKNTNCVGTP IYMSNEILEK KTYDNSTDVY
     SFAVLFYEMM IEEVPFSEID EKWEIPSKVI SGWRPTKGLN SLDRDIKNLI NICWAPHSLP
     SFDEIVFSLV KIFKRFN