Y3958_DICDI
ID Y3958_DICDI Reviewed; 1592 AA.
AC Q54B48;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0293958;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0293958;
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000224; EAL60478.1; -; Genomic_DNA.
DR RefSeq; XP_628868.1; XM_628866.1.
DR AlphaFoldDB; Q54B48; -.
DR SMR; Q54B48; -.
DR STRING; 44689.DDB0231281; -.
DR PaxDb; Q54B48; -.
DR EnsemblProtists; EAL60478; EAL60478; DDB_G0293958.
DR GeneID; 8629484; -.
DR KEGG; ddi:DDB_G0293958; -.
DR dictyBase; DDB_G0293958; -.
DR eggNOG; KOG0595; Eukaryota.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_252337_0_0_1; -.
DR InParanoid; Q54B48; -.
DR PhylomeDB; Q54B48; -.
DR PRO; PR:Q54B48; -.
DR Proteomes; UP000002195; Chromosome 6.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
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..1592
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0293958"
FT /id="PRO_0000362053"
FT DOMAIN 1..302
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1342..1592
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 348..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..518
FT /evidence="ECO:0000255"
FT COMPBIAS 465..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1474
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 2..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1348..1356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1592 AA; 186735 MW; 11DF6EB82DF8A46E CRC64;
MTGFEIFKKK YQVIQILNEI NNNLEERLIS IAKDKSGKLC VLKEIKYLNN KKKLEEFKKE
EKNEEGIQKR IYQRNFNLEF NHLKNFSQMN HTSIIKYIEH IESKDEFGLV DRCIFVTEYY
EDGDLSSIKE IEFKDIINLF LKMLINLKEF QNVIIHRDIK PENIFLRKFK NNDGKVELDC
YLGDYGSAQT LYTQNKSTLI GTNQYIAPEV IEKKGHTNLI DIYSLGKTLL SLSKRNTGFV
YNRIYLKLFE IMTNPFETRP NVNQLIEFMC RHHENLKYTL LVSDFQHRDS IKCLNYLKEK
LIGILDNKTN PLKKIHIDME FQGKTYHCNG VLRSEYLRNE YILENYPINN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNEGEVVQVI ELVSTDEKHY
SVLEGHINLS ESPILNSLSF HDFKVIRGTA PIMHFNDINT STTGEEEEEE KKDNLKRQNE
NNQIEQEDKG EKHLKETLNN NNNNNNNNNN NNNNNNNNNN NNSNYNSNRK CLLVLVPMKN
HSFRLYKDIL KNADETTVEI IQLKAIFHSL LASYLVSLTG VDFALQFLIR GDGINVYFEP
PQPSDTTTSN NGEIKLTDYG FKFLFPFKHV STVYSECNST YFDIFPQSIP VKNPLVKEIQ
QFFKDESQTK IPFTTIFQRL ISIVLREEYQ YKKYKELEYY FEAFNSIDHH YQQLKINNEN
LVKSEYITRL IDSKEIIKVV NHLTFMPVDD YFFYVVPHNE KVYGIEVYKN FQDIDFFGHA
INIIRLSLAI LNDHSKHFKF IDAHKDINSS IYYFVYELPP SLASNYKSTS EIQINNKNNN
NFYNNNNNNN NNNNNNNNNN NNSNDKSDNE NKLLFKQLIN QHFNNCIEFI NNINTFAREK
NPINILLYSM HTIITKNEMN VSSLYYSYML FGKVNQCIIG SFYDIGKWVY GDQFEKKIKS
ATFLKNLQYL VWYKMSMISN NHHQVYFSLS NLYSILNEDD KDMMILNLES SLKINENNEN
EESLPQKLFK LDDIEFGDNF KYSKILIGGI CYYILNIKEG DIFKEDQFGL EKKILLLELK
QLESGKKYLC FRKQSHQTNT LKELKFNCRT INKKINDEII LEPLFVVEDS NVTFHFYEYK
SSFENIKSIE SYSKDNSTDY NGIVIIRSLL YYIQYYLSNY KNDDDGSDDD NDNDNNRSLK
LVLVNMKDNE SLIYLDIQYL IYRLYGVDIS LTNEWTKINE SLINGTPSLI TNFIQTNRNK
ILNDSICLEI LSNELMIKFK PIEIEIQREI NHVTSVVSVV DVDVSGNSSK KKFVRKAIGS
IIDLKIIGKN YGGIDLSNPR SLGTYNLIGD SVFRNISFFE NKKLFEKFDT NVNFQKEIEF
VKNYSKFLNF DISNRIPREY SILKSIKGMN GVVQIDSWYL ENDIIYILMD YFDGQNLLEV
SQDLINDFTL FSILNQLSKI LFELETVYSI HHRDLKPDNI LIKNDLTICL ADFGISHFSK
ELKNDQDLYY SKDGTLGYQS PEIYSSELRG NGDIKNQPYK MDVFGLRCVM KYLMSKFNSS
SSKLKELVEK MGFFNYDDRI SLKELIECLN KL
