PAKF_DICDI
ID PAKF_DICDI Reviewed; 1176 AA.
AC Q869T7; Q554V7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serine/threonine-protein kinase pakF {ECO:0000250|UniProtKB:Q869N2};
DE EC=2.7.11.1;
GN Name=pakF {ECO:0000312|EMBL:EAL70097.1}; ORFNames=DDB_G0274409;
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:EAL70097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL70097.1};
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. STE20 subfamily. {ECO:0000250|UniProtKB:Q869N2}.
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DR EMBL; AAFI02000012; EAL70097.1; -; Genomic_DNA.
DR RefSeq; XP_644216.1; XM_639124.1.
DR AlphaFoldDB; Q869T7; -.
DR SMR; Q869T7; -.
DR PaxDb; Q869T7; -.
DR EnsemblProtists; EAL70097; EAL70097; DDB_G0274409.
DR GeneID; 8619645; -.
DR KEGG; ddi:DDB_G0274409; -.
DR dictyBase; DDB_G0274409; pakF.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_273573_0_0_1; -.
DR InParanoid; Q869T7; -.
DR OMA; DDYQERH; -.
DR PRO; PR:Q869T7; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
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; PF00069; Pkinase; 1.
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; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1176
FT /note="Serine/threonine-protein kinase pakF"
FT /id="PRO_0000363942"
FT DOMAIN 370..383
FT /note="CRIB"
FT /evidence="ECO:0000255"
FT DOMAIN 394..646
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..133
FT /evidence="ECO:0000255"
FT COILED 812..873
FT /evidence="ECO:0000255"
FT COMPBIAS 1..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..872
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 514
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 400..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1176 AA; 128726 MW; 5EDC80D65F8F3445 CRC64;
MSNLKLSNNN NGNQKESSSF FQKVMKSPST QNLLNSFSSN NSNNNLSNSG SNEVKDTTTN
SPSQLPPNYT PPPPPHQIRN SSSIEGGEFS LLNNENSDNN NNNNNNNNNN NNNNNNNNNN
NNNNNEQLAR TESSVSIISS SSSGSNSGQP NLQRHSSNIS TDDSNTTTET YSMSPNQTLN
SNIDSSEQQH QDLSSSVNNN NNNNNNNNNN NNNNNNNNNN NNNNNNTHES RKLTRKIAQF
ISSPKLLQSS ISQLPSTPTQ QNVEIQTTNG GSSETSPNGL ISPRPSNDQP LKEKKKKKFL
KTPEIFKHHH HHKESSLSSS TTTPSTTSSL TSSPSSSSLA ISSPNTTAAT TTNKKSHKKT
KSTFDINTEI SVPYNVIHKM HVDFDLKWTG HNDFILDEKL GDGAYGSVYK GTHKDLGFTL
AIKVIEMKES ESVSLQNEIN ILKNCKSPNI VSYFGSLQTE SHIWILLDFC ALGSIRDIIE
STEKTLNEAQ ISFVVKNTLK GLIYLHSQNI IHRDVKAANV LLSEGCDVKI ADFGVSEKLN
GALDQSKEMI GTPLWMAPEV ILKKNYDYKA DIWSLGITII EMADGLPPHI DLPPMRAMKM
VPNWPPPTFA EPKKWSPLLN DFLARCLVKD PEKRASPIDL LCHPFLKKDR GPDVLSDLVN
QLFKIKKKKI DDLKKQQKHQ TSQSSSSSSP QSPNATVNGG DIGSDGLSTS IISPIPSSPS
DELDNCNNSL KLATSSKGML SFKGNYTTCR DFQEEEEDSK HLNNNQDEQD DEQDDEDDDD
ENEDDEDVDP FSTTIFHGKK KGSGNGNGGV TSDQDDEEED EEEDDEEEEE EEEDDDEINE
DEEISATGTM VVRKKKNKST KKSNKKKNKK NNLSTIGKSG SGNNLLHVAP NKPLPITPPF
SISMTNEFKQ LETKLFTYID SSNQKIVNDI KNEIKQLESS IINKININLQ QQLSPILLAL
EEIKQNQHTT SQPKQMQSKL SATNLNEKKL SSSPPSSNSP LTNSVNSSLT TTTTTTTSPV
LSRQSSFRSS GSISSSNSSF RPNSAIMSAV NNSSTTTTTN SNSSSSNGGG SGVDISPTMT
GRASPSIMKR FTTSSSSSPL SSSSDGFAFN SNSNSSSSDL KRHVITPEEL NNSNLVKNKV
KMFEDDNSSG SGSNSPSLST NSSSTNSNNS VTNIKK
