Y0138_DICDI
ID Y0138_DICDI Reviewed; 1248 AA.
AC Q54XZ5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278509;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278509;
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. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68427.1; -; Genomic_DNA.
DR RefSeq; XP_642407.1; XM_637315.1.
DR AlphaFoldDB; Q54XZ5; -.
DR SMR; Q54XZ5; -.
DR STRING; 44689.DDB0220138; -.
DR PaxDb; Q54XZ5; -.
DR EnsemblProtists; EAL68427; EAL68427; DDB_G0278509.
DR GeneID; 8621612; -.
DR KEGG; ddi:DDB_G0278509; -.
DR dictyBase; DDB_G0278509; lrrkB.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_266059_0_0_1; -.
DR InParanoid; Q54XZ5; -.
DR OMA; VLPETIC; -.
DR PhylomeDB; Q54XZ5; -.
DR PRO; PR:Q54XZ5; -.
DR Proteomes; UP000002195; Chromosome 3.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 12.
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; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1248
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278509"
FT /id="PRO_0000355153"
FT REPEAT 386..407
FT /note="LRR 1"
FT REPEAT 411..432
FT /note="LRR 2"
FT REPEAT 435..457
FT /note="LRR 3"
FT REPEAT 458..480
FT /note="LRR 4"
FT REPEAT 481..502
FT /note="LRR 5"
FT REPEAT 503..524
FT /note="LRR 6"
FT REPEAT 527..548
FT /note="LRR 7"
FT REPEAT 572..593
FT /note="LRR 8"
FT REPEAT 595..616
FT /note="LRR 9"
FT REPEAT 619..641
FT /note="LRR 10"
FT REPEAT 642..663
FT /note="LRR 11"
FT REPEAT 665..687
FT /note="LRR 12"
FT REPEAT 688..708
FT /note="LRR 13"
FT DOMAIN 946..1239
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1069
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 952..960
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 973
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1248 AA; 140971 MW; D0C8EFFFC8A869D8 CRC64;
MSKVIGYIDY GDPDGNEEPS KQNGEYIDYS NENGYNAYHS VNGGYDKDNN NHHHHNQEED
YDYDNNTHVN YLTTKHSQFQ LSRGRLYQGH QSSHIIYPHQ SYKLSNSGES MNRSINQSKE
EDHLENSLHD DEYLYGYEDH HDDQASSISQ ESSQGLDETD FDNIDKYFES NQHLLLQTLQ
NNNNNNSNSN SNSNSNSNNN NNNNNNNNNN NNNNNNTKNN ITDENQLEIH LNDLSIDSDN
SNNKINKQYV NSDNSNNNNS NNSNNNNIGS NINSNCNIEN EKNSNNTDDN NNNNNIENVN
KINIEDNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNKIE VISNKPIQLF SDYDPPILTT
STSTSQSKIK TQQPFLFFSS NYLNSSSTEL DLSEQELNEF PIFDEKEIVQ GYKIIDLSFN
NIKSIPLDAF TNISNLEQLI MFNNNLSDVP SSIEFLKHLT ILDLSHNNLH EICRELGNLS
FLRELYLSNN SLKKFPTTGN LYNLKKLILD NNQITTIPIE CVEPLIQLQT LDLSFNKIGT
ITSSTTTTTT TTTTNNNNNN GGGGSIYQKM KNLKQLNLSH NELQEIPSSL RHLSKLHSLS
IDYNQISVLP DKVVASLSRL AKLTISNNKI KQLPFAINNL SSLIELNASN NVIELLPDSI
CYLSNLKKLN LNNNNLKELP SNIGFLTKLV DLQLYNNQIS SLPISFLKCR SIREIGTDGN
PLPSYYHLGI KAIRYHIKNP DCDLDDLNSI SPTIDSSTIE QQQQPIQLFG GGNYIDSSNN
NGNESFCNSG ELSPLTDSLE CIEMPPPMQI SENLRKPLNV NSPSYPFQKL DPIPQSLYSS
SNPRSHTESD IQKLKNNDET ITTTNSSIST TSSPPSLLFG VSINGNGIIS TTTTTTTTTT
TTNGKTLSRQ SSFQQIPQQF NLSTSTTNIT KLPRIKYTWE IDFDEIQFFN LIGQGGFSKV
YHGVWRSKDV AIKQIELQNN KSLDDFRREV GILSKLKPHE NLLAYYGACK HANYCYIITE
YLPRGSLHDL LHREQLMKLD FKQKVSFAIC VALGCYHLST YEPPIYHTDL KTKNLLVTNA
LKIKIADFGL ASFAKKSLTT IINNNNNTNN TATSSTTTSS ANGANSISNN NNNGTTSVDQ
SRLAYAFYAA PEILNSKHFS EKSDVFSFGT ILWELVTNKI PFDGMDPYEV KELLKSGKRL
EIPENCNEVL KNIIQDCWNQ QSEDRPTFLS IYHRLENLMK SITKKRRF
