FNKA_DICDI
ID FNKA_DICDI Reviewed; 793 AA.
AC Q869L4; Q553F7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase fnkA {ECO:0000250|UniProtKB:Q8T126};
DE EC=2.7.11.1;
DE AltName: Full=FNIP repeat-containing protein A {ECO:0000312|dictyBase:DDB_G0275561};
GN Name=fnkA {ECO:0000312|EMBL:EAL69531.1};
GN Synonyms=FNIPK-A {ECO:0000250|UniProtKB:Q8T126}; ORFNames=DDB_G0275561;
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=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:EAL69531.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69531.1};
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; EAL69531.1; -; Genomic_DNA.
DR RefSeq; XP_643456.1; XM_638364.1.
DR AlphaFoldDB; Q869L4; -.
DR SMR; Q869L4; -.
DR STRING; 44689.DDB0216322; -.
DR PaxDb; Q869L4; -.
DR PRIDE; Q869L4; -.
DR EnsemblProtists; EAL69531; EAL69531; DDB_G0275561.
DR GeneID; 8620041; -.
DR KEGG; ddi:DDB_G0275561; -.
DR dictyBase; DDB_G0275561; fnkA.
DR eggNOG; KOG4645; Eukaryota.
DR HOGENOM; CLU_354285_0_0_1; -.
DR InParanoid; Q869L4; -.
DR OMA; QEWEINT; -.
DR PhylomeDB; Q869L4; -.
DR PRO; PR:Q869L4; -.
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 InterPro; IPR008615; FNIP.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF05725; FNIP; 6.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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..793
FT /note="Probable serine/threonine-protein kinase fnkA"
FT /id="PRO_0000379437"
FT DOMAIN 11..358
FT /note="Protein kinase"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 403..444
FT /note="FNIP 1"
FT /evidence="ECO:0000255"
FT REPEAT 470..514
FT /note="FNIP 2"
FT /evidence="ECO:0000255"
FT REPEAT 515..557
FT /note="FNIP 3"
FT /evidence="ECO:0000255"
FT REPEAT 558..601
FT /note="FNIP 4"
FT /evidence="ECO:0000255"
FT REPEAT 691..733
FT /note="FNIP 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 138
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:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 793 AA; 88327 MW; 96A3C60032D8BB38 CRC64;
MKKLVHKESQ WEILSQLGTG AFGRVVKAKK INCDGTGIII DICAIKIIKK SVFTKNEIEI
LKQLDHPLIV KYYGYGVGEI DDNIYIYMEY IDGYPVSSIL RKQPKNQFPE DIISKIVIDL
ALILSYIHDN ERKIIHRDLK CDNIMLVNDN THSCDVNGNC SRNGGGSAKS ANQSFFTEDC
VCNVNGSGTD ENCKSCKLKS KPIREIQGSC ESCGSDLEQD SSSSSSSSSS TINNGQSSTC
RLINCIYSVS KKIKLIDFGL SKGCDGDSKY YSLVGTSTHM PPEVALRNNT ACRKSDIWSL
GCTIIEMAGG NLFEKDIHGK PKIPDHLSAS CKNFIQRCLT IDPNHRDDII NLISHNFIDR
NRINEEIKED ISKSKIQFDD EFNEIISPGD LDSVNEVVFG FDFNQTIIPG TMNSVKKIEF
GGSFNKELLI DSLPSATSIT FGARFNNGNK PFAIGAIPST CKSITFGWTY NQPFYPGILP
NSLKKLIFQE GGDFNRILEV GSLPSSITTL ILGDYDQKIE KGVLPSSLTI LELGGEFNQP
LEGSIPDSVT SLTLGYRFNK ALTENCIPPN CKFLKFGSNF NKDLSPGILP SSIETLILGY
CFNKELVEGS LPLSITTLIY EHRDNQKKVS YDYKEVTNLS KDLEENEIIP LTPESLPESI
TKLTIGKNQN HVIEFNCLPP DLQCLKYHGG FIRPLIPRDL PSSITSVKLY NYNYEIKKTS
IPKSVTSLQL GSRHNKFTQI QSLSNFHPNM RDLKIYINDD DIDIYNLKDI IPQTITSLII
NGDNIDLPIG IEN
