FNKE_DICDI
ID FNKE_DICDI Reviewed; 1321 AA.
AC Q552Z2; Q869K5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable serine/threonine-protein kinase fnkE {ECO:0000250|UniProtKB:Q8T126};
DE EC=2.7.11.1;
DE AltName: Full=FNIP repeat-containing protein E {ECO:0000312|dictyBase:DDB_G0275879};
GN Name=fnkE {ECO:0000312|EMBL:EAL69690.1};
GN Synonyms=FNIPK-E {ECO:0000312|dictyBase:DDB_G0275879};
GN ORFNames=DDB_G0275879;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL69690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69690.1};
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000312|EMBL:EAL69690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69690.1};
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; AAFI02000013; EAL69690.1; -; Genomic_DNA.
DR RefSeq; XP_643528.1; XM_638436.1.
DR AlphaFoldDB; Q552Z2; -.
DR SMR; Q552Z2; -.
DR STRING; 44689.DDB0229870; -.
DR PaxDb; Q552Z2; -.
DR PRIDE; Q552Z2; -.
DR EnsemblProtists; EAL69690; EAL69690; DDB_G0275879.
DR GeneID; 8620110; -.
DR KEGG; ddi:DDB_G0275879; -.
DR dictyBase; DDB_G0275879; fnkE.
DR eggNOG; KOG0198; Eukaryota.
DR eggNOG; KOG4645; Eukaryota.
DR HOGENOM; CLU_259886_0_0_1; -.
DR InParanoid; Q552Z2; -.
DR OMA; YNQLFTP; -.
DR PhylomeDB; Q552Z2; -.
DR PRO; PR:Q552Z2; -.
DR Proteomes; UP000002195; Chromosome 2.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR008615; FNIP.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF05725; FNIP; 8.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
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..1321
FT /note="Probable serine/threonine-protein kinase fnkE"
FT /id="PRO_0000379937"
FT REPEAT 108..149
FT /note="FNIP 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..191
FT /note="FNIP 2"
FT /evidence="ECO:0000255"
FT REPEAT 192..233
FT /note="FNIP 3"
FT /evidence="ECO:0000255"
FT REPEAT 255..296
FT /note="FNIP 4"
FT /evidence="ECO:0000255"
FT DOMAIN 295..595
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 654..696
FT /note="FNIP 5"
FT /evidence="ECO:0000255"
FT REPEAT 741..783
FT /note="FNIP 6"
FT /evidence="ECO:0000255"
FT DOMAIN 860..1128
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1160..1202
FT /note="FNIP 7"
FT /evidence="ECO:0000255"
FT REPEAT 1224..1268
FT /note="FNIP 8"
FT /evidence="ECO:0000255"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523"
FT ACT_SITE 990
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523"
FT BINDING 301..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 866..874
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 895
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1321 AA; 150518 MW; 6530FD1E919BF01A CRC64;
MQKIKEGYRR RHDYIIPKFI SFQSGYLDFS FYQVSLKNVK YLDLSSYYQL HAPRRFRKIV
EYLNLSYGQL LTLGTLPKYV MSLDLSSYNQ LFTPGRLPIR VSLDLSSYNQ LFTPGRLPDT
VDYLKLSSYN QLFTPGTLPN HMVYLNLSSY NQPLTPGTLP NKVKYLVLSS YNQLLTPGTL
PNNVKYVDLS SYNKLLTPET LPNKVKYLVL SSYDQLLTPG TLPNNVKCVD LSSYDKLLTP
GTLPNNVKYV DLSSYNKLLT PRTLPNNVEC LVLSSYNQLL TPGILPNYVK YLDISSYNQL
LTPGTLSNNV EYLDLSSYNQ VLAPKTIPNN VKCLDCPSYK QSLISETFPN RVGDLELSDH
PKHVNDNWEI IKPQKNISEN KVYYTTKHKN AKIIDVLNIC KCSLKLYGYV KDRNNEFNIY
FEYIDKAIPL SRLLEKLNKK EQFIVATEII KSIKSIHEMG IIHFDIKCQN ILILYDENEK
MLPTDFIKII GFDHSTLDSE VNSNIIGVTE THMAPEIKLK NGKLGYKSDI WSLGCTLIEI
VGGNLKLLDI NGIPLIPDHL SNLFKNTIQH CLQINPNARF NANELYNYVI KDSIMEPIEP
IYLPNQCTNL PLFNEVIVPS GFFGIKYLEL QAYNQPIDSI FIFNGVEYLI LQSFNHPLGP
GILPESIKYL KLPSFNHPLK EGSIPRSVIH LVFNKFNQFS LDEINLILPK FLDFGDAFDI
EKYGILIPED SILTLRTGFT FNQPINQRYI PSSVTDLQLY NYNLKILPHS IPRSIIMLTL
GSNFTHFESL SNLPSSIINL TFGFKNNFKI AELKKYIPSH ITSININGKI VNFKKSSPLN
TFNQSTDNIL NNNEHFKEDW EIISTLGSGN FGKVFKARKI NGIINGSKVS LCAIKKIEKK
DKLKIKLSTE VEILNKLKDN EHSMKYYGYG YDEDDNLFIY TEYIEGSTSI SDLIKKKPNN
RFEEEEIKSL MIKIVKALSK IHESGVIHRD IKSDHIILAQ DKNNETIVKF IDFGLSKQIE
KNSKYYSFVG TDSHMAPEVK LQNGKAGSKS DIFCIGCTMI EMAGLNLCHS ERDDKGIPSI
PTHLSNSFKN IIQNCLKFDT NARHSVESLI ITLSNIQIEG DSVFEKYLSP NLKKLELKTN
EPILLGSIGN EINYLSLPIY NQMITPGALP PSVQYLLFNK LNQYLECDSI PESVKYLDLG
NEFDIEKNGI NLSNESILVL RCGFNFTQPV SQRLLPYSVT DLQLYNYNIN LKRNSIPTLV
TSLTLGSNFT NIESLSFLPE NVNSLAIGIK DEDEKLTKEI EKIIQTKKSI TSFKINGIQR
N
