QKGA_DICDI
ID QKGA_DICDI Reviewed; 1553 AA.
AC Q8SSS9; Q557D4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable serine/threonine-protein kinase qkgA;
DE EC=2.7.11.1;
DE AltName: Full=Quick growth protein qkgA;
DE AltName: Full=Ras of complex proteins and C-terminal of roc 2;
GN Name=qkgA-1; Synonyms=roco2-1; ORFNames=DDB_G0273259;
GN and
GN Name=qkgA-2; Synonyms=roco2-2; ORFNames=DDB_G0273635;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14654223; DOI=10.1016/j.bbamcr.2003.08.008;
RA Bosgraaf L., van Haastert P.J.M.;
RT "Roc, a Ras/GTPase domain in complex proteins.";
RL Biochim. Biophys. Acta 1643:5-10(2003).
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 [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 [4]
RP FUNCTION.
RX PubMed=12954783; DOI=10.1093/nar/gng095;
RA Abe T., Langenick J., Williams J.G.;
RT "Rapid generation of gene disruption constructs by in vitro transposition
RT and identification of a Dictyostelium protein kinase that regulates its
RT rate of growth and development.";
RL Nucleic Acids Res. 31:E107-E107(2003).
CC -!- FUNCTION: Involved in growth, and during development, in aggregation.
CC {ECO:0000269|PubMed:12954783}.
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. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AY232265; AAO83648.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70508.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70847.1; -; Genomic_DNA.
DR RefSeq; XP_644434.1; XM_639342.1.
DR RefSeq; XP_644816.1; XM_639724.1.
DR AlphaFoldDB; Q8SSS9; -.
DR SMR; Q8SSS9; -.
DR BioGRID; 1243921; 3.
DR STRING; 44689.DDB0185215; -.
DR PaxDb; Q8SSS9; -.
DR EnsemblProtists; EAL70508; EAL70508; DDB_G0273635.
DR EnsemblProtists; EAL70847; EAL70847; DDB_G0273259.
DR GeneID; 8618918; -.
DR GeneID; 8619059; -.
DR KEGG; ddi:DDB_G0273259; -.
DR KEGG; ddi:DDB_G0273635; -.
DR dictyBase; DDB_G0273259; qkgA-1.
DR dictyBase; DDB_G0273635; qkgA-2.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_002809_0_0_1; -.
DR InParanoid; Q8SSS9; -.
DR PhylomeDB; Q8SSS9; -.
DR PRO; PR:Q8SSS9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:1904269; C:cell leading edge cell cortex; IDA:dictyBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
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:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0031158; P:negative regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IDA:dictyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:dictyBase.
DR GO; GO:0031272; P:regulation of pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:dictyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51424; ROC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1553
FT /note="Probable serine/threonine-protein kinase qkgA"
FT /id="PRO_0000355208"
FT REPEAT 287..309
FT /note="LRR 1"
FT REPEAT 311..333
FT /note="LRR 2"
FT REPEAT 334..356
FT /note="LRR 3"
FT REPEAT 357..378
FT /note="LRR 4"
FT DOMAIN 395..619
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 1242..1546
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1393
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1248..1256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1553 AA; 174817 MW; 734E5D777ADF1C0C CRC64;
MDLEQDEWMS QRQRQQQMEF SRIGIEVIGS KKDLIVNSMK NHETTLTIIN ETYRIVYYDQ
YESKFTSCNI ITFDGKDKRS IKKMKRVVQK LSNESTNSSH QFDLHSHALL QSSSSSSSSS
TSSSPSLTSS PSSPISTSPP YHSSPQLLEH LLHQQQPITS VGSKPSFFVI INLYNDDRQS
YMSEIVSFAG SFQFIEWRND ESWKEVFKLS SNLLTYHVKK NELARACTLG DINLLDEIIL
SGCSKSQLKE AQGAGYTIVF NSYTSYSSGS SLVVSGTMAL LCAIVENGTF LLLSKSNITR
FPMSIINMCS QLVELDMSNN RITEIPIEIT ELKFLKNLNL SDNLINDIPL EICNLTLLKV
LLLNENPLNN FPSSIVELGT KKLLSFCRNI LEGKSCETWN KVKLMFVGEE GVGKTRLCKL
LIGSKYNKKK SSSSSSSSLS SLSSALSSSS SSSSIINSNS ISNSNINMVN IKNENQVTGD
TVSTEGVNIH DFKSKKVEFY AWDFGGQQIF YPTHQFFLTT QSLYLLIFRV NDSNFAERVN
YWVHQIKAKS GISLPIIFFV GTHIDSCTPE QLSMAESILK SNFIKYSRVK QNVINFVSCV
TGKGVKELKK RLIHESEKSR LIKKDIPGSY IILEQRLSNR GANQGRMSIS NSASNSSSSL
LNSSSSSSPS LTSKKSSSHL KHSQQQQQQH QQQQQQLQQS IKEKYIDYDD YLNECKLSYL
KPHEIKDATD FLHNLGIILH FDSPKLNNLV VLDPQWLADV MSSLITFSHS WIKLGILNHS
DLQSIWGGRY KQTLWPSLLK LLEKFEVSYQ LPNLSKSLIP SLLPDDPIGE ILEIKDREWV
PLKLAMENNY VQVFGCDYHF SFMPLGFFAR LLLRILLIQG IDIKTYWKDG VLLDILTPSD
KIKQQQLLQK KSIFEPTTTL SPFLCSLSLT DSQNYSPLEP PPLILNSPRV NRKFISNSTS
TTSTTTSTTS TSTTSSNNIT PLSMSSITPY SPTSPRTPSF SSSSTTTSSS SSSSSPSSQF
CGVGCHRNIN KNNGSSNELI KTLTKINNQN GSSGELIKTT TTTSTSTSTT STTTPTTTTP
TIPIKNNNNK KLPINRTVSS LCLTAKPKLQ ALITFIKKKS FEQSHDNDSY KLNIQVRTYN
TTIDKEHSVS LFFQQLLFTI DTLISGSYQG LEVTRTIPCT HCIQLNPTIE PYHFDLGDCI
SALEDGRSHV YCGNDPNTPV RIDYIAPDIC LKKVPTFTDD QILYERQIGE GGFGLIHKGK
LISNKSDIAI KSLILCNSNN NNNSNNNNNS NNSNNFKNNN NEDEFIEKFQ EFQHEVFIMS
NLNHPNIVKL YGLMHNPPRM VMEYVEHGDL YHLCQDKERY ASLGWTLKLR LMIDIAKGIG
YMQNQNPPIV HRDLRSPNIF LKSLDENSPV CAKIADFGLS QQSVYSVSGL LGNFQWMAPE
TIGVEDESYT EKVDTYSFAM ILFTILTGEI PFDEYSFGKM QFINLIREEN LRPTLPFDCD
PRLSNLIQLC WSTNPKKRPS FTFIIKELLE IRIDSIQTSY FDSPFLKNYP ASI
