GDT8_DICDI
ID GDT8_DICDI Reviewed; 1326 AA.
AC Q55CY9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable serine/threonine-protein kinase gdt8;
DE EC=2.7.11.1;
DE AltName: Full=Growth-differentiation transition protein 8;
DE Flags: Precursor;
GN Name=gdt8; ORFNames=DDB_G0270668;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
RN [2]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=15236669; DOI=10.1186/1471-213x-4-8;
RA Chibalina M.V., Anjard C., Insall R.H.;
RT "Gdt2 regulates the transition of Dictyostelium cells from growth to
RT differentiation.";
RL BMC Dev. Biol. 4:8-8(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000005; EAL72684.1; -; Genomic_DNA.
DR RefSeq; XP_646342.1; XM_641250.1.
DR AlphaFoldDB; Q55CY9; -.
DR SMR; Q55CY9; -.
DR STRING; 44689.DDB0220636; -.
DR PaxDb; Q55CY9; -.
DR EnsemblProtists; EAL72684; EAL72684; DDB_G0270668.
DR GeneID; 8617297; -.
DR KEGG; ddi:DDB_G0270668; -.
DR dictyBase; DDB_G0270668; gdt8.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_251247_0_0_1; -.
DR InParanoid; Q55CY9; -.
DR PhylomeDB; Q55CY9; -.
DR PRO; PR:Q55CY9; -.
DR Proteomes; UP000002195; Chromosome 1.
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 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 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1326
FT /note="Probable serine/threonine-protein kinase gdt8"
FT /id="PRO_0000323585"
FT TOPO_DOM 23..782
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..1326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1036..1292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 419..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1042..1050
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1065
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1326 AA; 150109 MW; C8F07D060C277261 CRC64;
MINKILIKLI TIIIFCFSFL FAEEDLIRTP PGYYNLTRHK RYPHITEYQS SQDTDLYYPD
VCRNALRNDI IPGVDEFFPF LFPGFNSDGP NSIYIQKNSS LLFKSESLGT TYNFVAVCVE
GSFTVKGSMF FTINSLIILP GGRFESEAGI EFYDENDPLH IYNNPDFPKD PFGFFPGILV
LGGTISVVAK ESLVYRADRI SNSSIEISPP FSPMNKINQT IRIFTELYPL GFYCSFSSDL
ERKILSLLDC LPISENDKII RVLIEVDRDQ NVSPTNILKK GKTTKGSIYI TGDSNVYFKN
MFFKNLGFTT NEPYNDTKLI FSPNDPNQVT DIIMGTNQRF RSSLYIEFSK NVTIDGCAFF
EDNLTRSPLV LFDSNVIISN SLISSKSGSN IIAQYGTESI QSSNNSYILV KIDTASLDVD
QNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN MDYGNQGNGI YSISPNINSN
GDSFFGQQYA FNYYFISKNS VNSNQDNSSL LNSKPIELII IDSSFNPTNS NGSLNKYLLN
INSDGNKTIS TYLVCNSIIE YYSGWLMDNL NSNQQISFEG NLFQNGCNKV DGNCTISQNS
KYSTDLPKVA NQTKFDEIVQ LDKLFSNGIT SINPNEKVII STKINSKIHY YQIQLFFTHL
PIDDQPTPLS IYIENQPVFL LEPIKSTFPT FNNFTFKFEN KNSLDKINIA FTTRGDIYLT
SMATYSSIVV EPPTETPTET PTETPTETPT DTPTQTPTQT PILTSKPITQ ISVDRNENLE
LKIALPICLS LALLIGIIIM ICIFKKVQSN SKLKKDDDEN EMATIKEGNK SIIVSQPPTV
IEEKPQDNSK PDDQKLIERD QQINNPILKI REYPSLKDIE LSNEETKSPQ YGSLNSFSTL
QFSRQYDYGS EEFPFQFNKQ VLEFNLNGRK CMNDEVINDS LMIHNKSEIT YLVNIIFPQN
IETGCVSILN VEIFNESFEL LPHCTTEVKF SLTLTCTTKF LENFAVLVEA QGSKCHTFLS
VHVESETSLK LDYKEIKTEQ LIASYLPSKV YVFKGYYRDL AVAVKKFAIS DNSKSFEKIK
NEVQILSKVN NINVVRYIGS AQNISHVCIV TEYAKEGSLG SLIHDSKIKL SFIQKVKFML
DAAKGFTFLH ASEIVHGDIK PDNLLVFSKE ISGVCVKICD FGNSEELGEK ESKSKPDSTM
NYLPNEVFDG EGYQKSADVY AFGVSLYEVM VEKIPFHEIC YNDIPNRVQD GFRPTADLDT
IDDDIRKIIE CCWIKEKSKR PSFSEISLHL EIKFSKLLHQ MNESEESTSN HNTNSKTKED
KDLDEN
