Y8013_DICDI
ID Y8013_DICDI Reviewed; 1505 AA.
AC Q54VU4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0280133;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0280133;
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).
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. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67293.1; -; Genomic_DNA.
DR RefSeq; XP_641261.1; XM_636169.1.
DR AlphaFoldDB; Q54VU4; -.
DR SMR; Q54VU4; -.
DR STRING; 44689.DDB0231454; -.
DR PaxDb; Q54VU4; -.
DR PRIDE; Q54VU4; -.
DR EnsemblProtists; EAL67293; EAL67293; DDB_G0280133.
DR GeneID; 8622393; -.
DR KEGG; ddi:DDB_G0280133; -.
DR dictyBase; DDB_G0280133; -.
DR eggNOG; KOG0586; Eukaryota.
DR eggNOG; KOG1882; Eukaryota.
DR HOGENOM; CLU_248489_0_0_1; -.
DR InParanoid; Q54VU4; -.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q54VU4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00060; FHA; 1.
DR CDD; cd00130; PAS; 3.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50112; PAS; 2.
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; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1505
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0280133"
FT /id="PRO_0000367469"
FT DOMAIN 2..72
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 108..178
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 215..284
FT /note="PAS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 542..805
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1399..1463
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 282..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 903..939
FT /evidence="ECO:0000255"
FT COILED 1125..1189
FT /evidence="ECO:0000255"
FT COMPBIAS 449..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 684
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 548..556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1505 AA; 173403 MW; 3FC1B0A6687E903F CRC64;
MNTHNNNYQQ RSMDSAIVTI NDKGYIQSVD RKTCELFGYT IEELQLQKVN ILVPSPYKEQ
HDTYMQSYFE TGVRKIIDKS RVVEGLHKDG SVFPITLSVT EVRIWNKRMF IGSIESIIDK
RLIIYTDVHG IITYCNRNVE ELIGYTPAEL FGKNVSALMP SPHAKSHSEY IEKNYHGGGL
WKMLNRVRNL PIKHKSGVVF LVSILVTKIS TDGIDMFKAI IQTPPKEAVF TINGDGIIKA
CNFNFTEPMF GYTQKDLLGN TIGLLIPEMS KIIDNTSLNL TDSHDPQLQQ QQQTTTTTTT
TTTTTSTTST TTSTPTPASI AVSGNNISSP PIDSPLTTPS TPTTFNHSRG VESWLGRTRK
VDVWHRDGSR FPVNLEIIKL QGENSMFSLQ IKKVENPRVY GKDKDKNGGG GGTTENKDGK
QLDTIKESKE HRHSKEKKKR KKDRDHNNNN NNNNNNNNNN NEQTSDSSDS SDSDSESRSK
KKRSSKKKSR RDDSSSDSSD SETESSSSPH KKNRSSNSSS NSSHSNAPHE SSYYQPEMIG
EYTLGKTLGR GNYGVVKLGT HINTKEEIAI KILYKEQMTE SEFTRCKREI EILKQLYHPF
INKLLNVLEK DDAMFILMDY CQGGDLFHYV NKFGLKGVKM VNSPDIGDQV LMGVPLPEDD
TKRIFTQICL GIAHCHKLNI AHRDIKHKNI LFDNQMNVKI IDFGLSNWSY QEKMSFCGTP
AYAAPEMLLG INYNGPEVDI WSLGVILYSL VTGKLPFINV TDMIVGKFIL PPSIPLDLQD
LIKKMLTVDR EHRLNIMNVL NHPWLSKDPA SSTLISQNLL HSPPVVHQPQ PPQHQKIQPT
SIIPNFNEVE TLKNNILNNN NNNNNNNNNN NNNILNSNNN NNNNNNNNSN NNNIINNSNN
NSNNNNNINN NINNNNNVNN NVNNNKNNNN NNNNNSNNNS NNGNNIPNSS NNTNSIINNN
LYNQSLSPQN NNIYQHSPQH QQHQHQQQHS PQQQQHQQHQ HHQQQQQQLQ QQHHQQHHQQ
HQQHQQQHQQ QHQQQHQQHQ QHQQSHQQPP VYFPTQIISD DFNLTSQLQR TQPNQQVSFD
TNQSYQQQLQ QPQIPHQVLM QQPPQILSHS NNQPINNYYV GQQPIQQIQQ LQQQQQLQQQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQNDP NFQPHLRRIK
MSKRDNSYNK RKSEDGDSYK KRDNQSYDDI LKDEGNKRLR ELQTYSEGDK SRQHYNRDSN
DNSRDNNRYN NRDNNNNNNS NNNRERDRYK KNKNENFDYG KYKFGKSNED EENKDKPNIV
REKPDFKPSG SLKNDSSSNY GTISSGRNNN NGEEDEENKI KLKWHEPAEA KLPTEKWMLY
PFKGKDQLDT IYLHRKKSFL FGRNRDIADI PIDHPSCSSQ HAVIVFRIRK KENPNTGSIK
TFILPYIIDL ESTNGTFLKG EKIEPAKYFE LRPKDKITFG TSTREYILLC EDSIEGDESE
EEDSD
