FNKB_DICDI
ID FNKB_DICDI Reviewed; 530 AA.
AC Q55FV4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable serine/threonine-protein kinase fnkB {ECO:0000250|UniProtKB:Q8T126};
DE EC=2.7.11.1;
DE AltName: Full=FNIP repeat-containing protein B {ECO:0000312|dictyBase:DDB_G0267934};
GN Name=fnkB {ECO:0000312|EMBL:EAL73420.1};
GN Synonyms=FNIPK-B {ECO:0000250|UniProtKB:Q8T126}; ORFNames=DDB_G0267934;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL73420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL73420.1};
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; AAFI02000003; EAL73420.1; -; Genomic_DNA.
DR RefSeq; XP_647429.1; XM_642337.1.
DR AlphaFoldDB; Q55FV4; -.
DR SMR; Q55FV4; -.
DR STRING; 44689.DDB0229295; -.
DR PaxDb; Q55FV4; -.
DR PRIDE; Q55FV4; -.
DR EnsemblProtists; EAL73420; EAL73420; DDB_G0267934.
DR GeneID; 8616236; -.
DR KEGG; ddi:DDB_G0267934; -.
DR dictyBase; DDB_G0267934; fnkB.
DR eggNOG; KOG4645; Eukaryota.
DR HOGENOM; CLU_514305_0_0_1; -.
DR InParanoid; Q55FV4; -.
DR OMA; SENWEIL; -.
DR PhylomeDB; Q55FV4; -.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q55FV4; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR008615; FNIP.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF05725; FNIP; 1.
DR Pfam; PF00069; Pkinase; 1.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..530
FT /note="Probable serine/threonine-protein kinase fnkB"
FT /id="PRO_0000379438"
FT DOMAIN 11..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 530 AA; 60726 MW; 10BE37745B79C8D1 CRC64;
MNSYIYKEED WEIVETLKSN VFKVNNKNNI VLNGNSFKTC ILKIIINKDK NVWKEGQVLE
KLKNIDSIVK CYGWCCNKHT TYIFIEYING YTLEEYVLKN HPIPEKELSE IIEDLIKSLA
SIHEIGVIHR DLKLENVMFD KESNKWKLID FGLSFSFSPS NDGSKCYTQC GSIGYIPPEI
KLGGQCGRKS DIWIFGCLVI KMLGGELEET EIQIDGASFN NNNNKPNIWI PKIPPHASKF
LQNFIQKCFF EEEVLRFDSI TLIDHPFLSL FKSKGNMLYL IQRGHKRWMD ITQKKKGIKI
EGKTFTFEDN DNKEPFGPGI VPDGTVELIF KKTFNQRLIP GSIPSTVQIL DFGVDGDSFF
NQEMDDDLFL DCDLKSLTLG NAFTHTLPYF GSLCYLSLGR NRNALQNLPP TLETLKYYGE
VQTDLNIKSI PHVKNLLIPF NNHSIIIDTI PPTVKYLAWG KLKDLEAIET LKNLPPSVND
LTFSCPPDVF DKIQRKHIPD SISIIIINQH VIELKNSDNS ETYLKDNIVC
