GDT4_DICDI
ID GDT4_DICDI Reviewed; 1620 AA.
AC Q55DU7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable serine/threonine-protein kinase gdt4;
DE EC=2.7.11.1;
DE AltName: Full=Growth-differentiation transition protein 4;
DE Flags: Precursor;
GN Name=gdt4; ORFNames=DDB_G0270550;
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}.
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DR EMBL; AAFI02000005; EAL72625.2; -; Genomic_DNA.
DR RefSeq; XP_646034.2; XM_640942.2.
DR AlphaFoldDB; Q55DU7; -.
DR SMR; Q55DU7; -.
DR STRING; 44689.DDB0220632; -.
DR PaxDb; Q55DU7; -.
DR PRIDE; Q55DU7; -.
DR EnsemblProtists; EAL72625; EAL72625; DDB_G0270550.
DR GeneID; 8616981; -.
DR KEGG; ddi:DDB_G0270550; -.
DR dictyBase; DDB_G0270550; gdt4.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_251247_0_0_1; -.
DR InParanoid; Q55DU7; -.
DR OMA; SSICAKI; -.
DR PhylomeDB; Q55DU7; -.
DR PRO; PR:Q55DU7; -.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1620
FT /note="Probable serine/threonine-protein kinase gdt4"
FT /id="PRO_0000323581"
FT TOPO_DOM 20..891
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..1620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1349..1604
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1355..1363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1620 AA; 183863 MW; 4983E4766A716640 CRC64;
MKLEQRIFFL ICLVINSFSN CSLLVAPDGY YNIYRENKIE NILNLKPNGN KSQDSYYPDV
CSKAVKNKEG VKSFILSSFP LSTKEYANVI VTKGSHMTLG DGEYHQIFNI NRFLNIVCVE
GSLVFSTKDV VYMSALVILP GGNFECIDCT IKFRDLYPTN SLIDPFGFLP GIITLGGSLS
LLGKQKTVYS AVLIDENILE VQDISSLDIF NGYSLFIFSE SFPLGKASTF TFNSNQIKVL
EIKIPKTDKS IRVFFYSRFS TFSTSTTASI HITGNSNVHI ENFYIDSFGR TTNDQYSDTE
LIFSQDDPNL ITGFINGSNQ RFRSSLYIEH SNNVTIKNSV ILENRGETRS PLIFFGSNVN
ISGNIISSKS GSSLIAQYGT ENIQSTNNYY SLSLPLLKSL NSTLDSMDYG NEGNGIFSIS
PKINSINDIF NGQIIAINHI ILSDRSSITG FDKDCYSPCY NDSIRVSSKV QHSVEFKITG
STFISSSNYS ESSFLFRISE TGSKQSSFYK IINSNLSYPI SVLLENNAFI LDNVYGFGNF
TINGLIKRLD IINSTLDPSV TSSISLSNFS KAISIQNSFM DYRSFQKQNN QIYGSIITPY
LYYFENTMNL IKVSKMYPNV NHQILAGTVL NMGIEIIIIA PLFGKMDCIF EDESGIQTIP
FNKSSNSCVL PYLFKNEGSF NVRVTLSLTK SLDNIIFQVY FPMVTVFNIY SFYSGWAMID
SNIEKEIIID GNIFKKGCQQ QVLGNCTIST NSKLITGLPS VTESDKLNRL FSSGITSINP
YEPVTITIPI DKESKKNQIQ LFFTHQPIDI ETSLLSIYVE NQPIFLLEPL QSNLDSTFKN
LTFHYENSKS LEKIKITFIT RGDIYLTSTA IYSSTNQPIY NEVIGINEQL NILAIVLPIT
ISLFAAASIL AGYLVIKKYK KPNMYYNRNT NGNIGMKVFS TKFKRRPKKV IPLSIPLSTN
RITKKSLQSL DSMAENPVIL LSIPELEKAN EPEFNPEKTF LQESELLDLP TPKVEPEEPR
INIVPLPRFP TVYKKEDNDK LLKELNITGP ITSENIESFF EVDVGLPSLI IKNESEIILQ
EIDYIETGEI QEMEGSFLED KSTDTTVIVT KSDGLPKFFQ TKVFSKRFND ISKFDNDFFD
LKEYIVEHQE ESFEIPFMTS EDEVDETKIN IIDFLLSPKS NKVALNMYLK SFQNRNHKLC
YGKYGSNKNS ILVIEGTSYY YDCTDVRLPI STPRSNLNFG ITDGNKCIVD RKYRERLQYI
NVYSEPFRIY TLFPDSNDNV TITTSECCKE IDPFGSLDVD IFVTLKTTTK FNEKVTIRYE
TDDKELAFST FVYLNLESQV SSKIDFDEIV LEKYLSEGSF GVVYSAIWRS SSVAVKLFKH
HYSKDEIDKE TSILSKIKHP NIVSFIGSLN FLNTYGIVID YHPRGSLNYY TRNQNIKLSM
VQNIRISLDI SRACSFLHKN GIIHRDLKPD NVLIVSFDPD SSICAKISDF GTCREINGKH
ELNSKAGTTR YMSPEILEGL PYTYSTDVYS FAILFFELLS GRVPFREIPK REIPRFVRLG
TRPRLDQDVF ADNDISLILL ACWNPNPRGR PTFDTLIDLL EKLLKKYKER AKRNKKNQNQ
