PAKG_DICDI
ID PAKG_DICDI Reviewed; 1179 AA.
AC Q54RV3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine/threonine-protein kinase pakG {ECO:0000250|UniProtKB:Q869N2};
DE EC=2.7.11.1;
GN Name=pakG {ECO:0000312|EMBL:EAL66025.1}; ORFNames=DDB_G0282891;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL66025.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL66025.1};
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; AAFI02000047; EAL66025.1; -; Genomic_DNA.
DR RefSeq; XP_639384.1; XM_634292.1.
DR AlphaFoldDB; Q54RV3; -.
DR SMR; Q54RV3; -.
DR STRING; 44689.DDB0229411; -.
DR PaxDb; Q54RV3; -.
DR PRIDE; Q54RV3; -.
DR EnsemblProtists; EAL66025; EAL66025; DDB_G0282891.
DR GeneID; 8623822; -.
DR KEGG; ddi:DDB_G0282891; -.
DR dictyBase; DDB_G0282891; pakG.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_273250_0_0_1; -.
DR InParanoid; Q54RV3; -.
DR OMA; HLEYQFL; -.
DR PRO; PR:Q54RV3; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 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..1179
FT /note="Serine/threonine-protein kinase pakG"
FT /id="PRO_0000363943"
FT DOMAIN 111..124
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 139..390
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 414..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..53
FT /evidence="ECO:0000255"
FT COILED 621..668
FT /evidence="ECO:0000255"
FT COMPBIAS 421..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 145..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1179 AA; 128266 MW; 97D6B8DC85252EED CRC64;
MEEKIKSNLI HSKTNEDIEL IKQKLKEDRE LLEKERAQFE EERKIIFESL NKVVGSGSAN
ITKNIAKALK KAEKKNGVGS NLNLANSSSG SNISVYNNNN NNNNNNNSNN IGTPFNVQHK
VHVDFDYKWS GCQDLEQVFL IDCILGTGSY GTVYKAIHKD TNFVLAIKSI PIKESEEIEK
EISILKKCKS QNIVSYFGSG QQGDNLWILM EYCSANSIRD MLELTEKSLT EKQISVILQQ
ALKGLHYLHQ SNIIHRDIKA ANILINEDAI VKLADFGVSS QLEDSLRGEA SQLVGTPLWM
APEIIKRQNY NNKCDIWSLG ITAIEMAESF PPLYTMPPTR AMLMIPNKPP PTLSKPHHFS
KELNDFIGQC CQKDPEKRPS AIELLTHPFL VQNISTPQEV LKPLIDECLK KSIKKKKQSP
NNDQPPPPQT PNKLSPPDTP LPNVPVLGKN QGLLNKSNGM KKSHGSSLDE AESMNTFILK
STIGSSSNGS NDTGGDDFDC GTMILKDDTC INGSGNADKI STIPAFIAAL NKSNGKVITQ
NQQQQQQQPI ASSLQQSNPI ASIVNENQYP NTIEKRGLSS INSNNSLLIG NSGNNKSQNF
NNFNNNNNNN NNNNNNNNNN NNNNNNNNNN NEFLINQIKK ELILDFNENM KQYINQQLTN
LKEEMLKEIS KIVIANIPQA PIKTSQSVFN QQLSAAAIIH PISSSSSSSS SFLNSSPSSS
NSSATIFKKF PNPPPTPVLI NKLPPSQQST PVTTTTTTSS PSPSPSPSPS PSPSSPLPSS
STSTVNTPNK PPINYRKSKE LDSTINIFNG LNNNNTNNNN NNNNSNNNNN NNNVIQSPKL
NNRPLSPTTP TKQFNNRPPS PSKFNNRPPS PSKFNNRPPS PSNRPLSPKN SYNSLEKSNN
GSISNNRPLS PKNSLEKSTT QNNTSSEDIS TTTVTVTSEQ GGTPITTPMA FLPRPKPSPP
PIPMNKSSPK RAPSPSSNRR LSSSFTAQSS TASTIAALGK QSSMSPNSPL IKERVPPPLP
PPRTTITSST NSPIKPLSPL NKSPNSPYVP PRITTSNISN NSNINNNNNN NSNSSSNGSG
GTPITLKRAS TTISPIMISS NSPKVMGSNV NKPLALSRNS TEINLPSSSP STPQKPNTPS
SIPTTPTTPT TNGGSVSSKS STIGRKTVLQ VKSIFSPKK
