PKGA_DICDI
ID PKGA_DICDI Reviewed; 1367 AA.
AC Q552E9; O15747; Q75JH3; Q75JH4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable serine/threonine-protein kinase pkgA;
DE EC=2.7.11.1;
GN Name=pkgA; ORFNames=DDB_G0276157;
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=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).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1112-1367.
RC STRAIN=AX3;
RA Loomis W.F., Iranfar N.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000014; EAL69378.1; -; Genomic_DNA.
DR EMBL; AF020280; AAB70848.1; -; Genomic_DNA.
DR RefSeq; XP_643264.1; XM_638172.1.
DR AlphaFoldDB; Q552E9; -.
DR SMR; Q552E9; -.
DR STRING; 44689.DDB0185113; -.
DR PaxDb; Q552E9; -.
DR EnsemblProtists; EAL69378; EAL69378; DDB_G0276157.
DR GeneID; 8620307; -.
DR KEGG; ddi:DDB_G0276157; -.
DR dictyBase; DDB_G0276157; pkgA.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_256614_0_0_1; -.
DR InParanoid; Q552E9; -.
DR OMA; CAMANEE; -.
DR PhylomeDB; Q552E9; -.
DR Reactome; R-DDI-2465910; MASTL Facilitates Mitotic Progression.
DR PRO; PR:Q552E9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005524; F:ATP 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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1367
FT /note="Probable serine/threonine-protein kinase pkgA"
FT /id="PRO_0000353102"
FT DOMAIN 810..1236
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1237..1347
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 933
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 816..824
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1367 AA; 154781 MW; 2830F9BD178FD1ED CRC64;
MYNSQQQNII KINKQDTDGR LQLFIVDAKR TLRNSSIELE SSQIYIDVTK RLIDIASLFC
KQEEIQYESF AEELLSILNS TQFKILGKCR ELVIKLLTII AKYARVNQLL GIESKDRSPS
SSINKNNGFD QLYDFELNRI DENNNNNNNN NNNNNNNNNK NKTISPTHQT IQATIPSPKL
QPFLDHDDKD DKEIIDIVSN KDKDQLNGVD DVDLSNTSGI SCKEIFEKNP INFQKSHYRC
LSYSPKLLEQ QLQQKLVNQQ IKLKNGKPSP IKRPSPPLPP PQQQQKEQQK EQKEQQKEQQ
KEQQKEQQKE QEQKQQEPQK YVKFEIQKSP PSNLLPPLPI SSSNISNEIS KQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQQ QIAQPPPPQS ITSPQTISAN NNILTTPLSS QPTQSLETPS
TIKPPLLSRR VSDIIYSKNE TNLNIKEPIH SKDIIPTPLE TNVGGGGGEI TKKVVGSEEN
LLSSSSEEET LSTSEEHDEY TTSTSGEDEE EDEDDDNIYN TNHYEISERK LKNKRPFKKT
HVHHSLSANS PLSRKPYESP VFLLDPRLND LKTSSDEYIL KRPLVRSKSF SPNKEEEQIK
KEPYRKLARS FSEIPSVKLI EDHNDDSQMA MCRICEEPIH SSLLEDHSKI CAMANEEDMK
AMNVDDHLRA VAKILLTRSN DIPHEKRKMI IELREIALFA VENGIKENLK MIHIMNDIIK
NFDPKDDNRE LAIKIQSLIS DKVNALKRAD DVINSSPRIF RTNSPRILKS PREEELSQTP
LGGRLRSDSD PVHQTQIEYK PKGVPTISDF EFIKPITKGG YGKVFLAKKI RTGDIYAIKR
LKKSDMIKKN QLDHVKVERN ILAYTSNPFV VKMYYSFQTK EYYYLVMEYL QGGDCFSLLQ
MLGSMDENMA KMIIAETVLA LEYLHSHGIV HRDVKPDNLL IDKKGHIKLT DFGLSKVGLL
DRQTVVPPSY FSPTLSGKNN QSSSSSSVSN IGGSNTIGSN ISSTNNNNNN NNTTGATMVG
GHVINTETPI PSNTAIPAKK EKKLLSLAQS KSLFSASSSP SIPSLNLLNS DKPISPMMMG
VKGFIPPPPI NQQPISNIPT TTTTTTTTTT GQQSQQQSQQ QQQTTPPLPP HNIHRKLSCV
GTPDYLAPEI LLGIGHGASA DWFSLGVILY EFLCGVSPFN GSSVQETFQN ILQRNISWPE
DMSPEARDLI DKLLALDPRQ RLGFNGAEEI KSHPFFKSIN WKTILTQEPY FKPKIENLQD
TSYFDPRKEI YKVSDDFAES CKPFVQNQNQ NKESSTILTT SPPSTSSTTA TATATTSNLD
SITINQNTNA NFDDFLYVNF QSLLELNKNY LAEAKPFNSN HRRRNST
