Y1199_DICDI
ID Y1199_DICDI Reviewed; 1634 AA.
AC Q54RZ7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0282895;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0282895;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66027.1; -; Genomic_DNA.
DR RefSeq; XP_639340.1; XM_634248.1.
DR AlphaFoldDB; Q54RZ7; -.
DR SMR; Q54RZ7; -.
DR STRING; 44689.DDB0231199; -.
DR PaxDb; Q54RZ7; -.
DR EnsemblProtists; EAL66027; EAL66027; DDB_G0282895.
DR GeneID; 8623781; -.
DR KEGG; ddi:DDB_G0282895; -.
DR dictyBase; DDB_G0282895; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_243069_0_0_1; -.
DR InParanoid; Q54RZ7; -.
DR OMA; AGTPKWE; -.
DR PRO; PR:Q54RZ7; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02493; MORN; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00698; MORN; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1634
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0282895"
FT /id="PRO_0000355156"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 40..63
FT /note="MORN 1"
FT REPEAT 169..191
FT /note="MORN 2"
FT DOMAIN 1377..1634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 84..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1500
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1383..1391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1634 AA; 182700 MW; FDF9B6C94DDD2F34 CRC64;
MNNQFEVFRP NSYTYDVLAK QYTETIASSG HMVLSHHGFY KGNLNENKLK NGKGTFLFPN
SIYSGQWNSD KKEGDGTLII LKPQKIQKKS SQSKSQQQPP SQTKKSSSPI NLSPRLQGQN
PTITTNGSNN NNKVNIESLI NKLNDKFNQC EELINQTSQE EFLKQQDYYN GKWINGKANG
IGCFHFSKDD SMHYDFWRYG VVIRYANQQN ILKPLYDDSV PAGLLNSREI LKDMMEDWKS
VVVGDDDFPC TRPYLTTPTA SISLNRENIN IYSNNNSNGT TSPTSPSILS PTQVPLSPPK
VNTAPSTLIS EDDNNFTSGS GFCSPSSSLS IKMSSPISSG LQHSKTQPNV SQSQNQQIQQ
QQQQQQQQPS LLVNSTIVQT NTNNNKFNDL LINQRNQQKI LKKQLLKSNQ QKQSFGIITS
NYLKSRLENE EKFFMTLILF ISKWEIPFKS FNIPNNPSIH ASFLIFVPDT DNCTFISLSN
LIMQSNVLER LIFKLLIDPM SKVLNSTALN TLTESQTLGN LSTYNNNNNN TINNTISIGQ
SKSANSSPNK ISPSVSLVGV SSLTTLPSST PEERELHKLL PICLDLDETP HIEKECIASI
LNIFKLFPTI EDYQPPQFIP DTICKFISCF KKTRALENYL LQKQFQMSKD YFFKPTATTA
TPNNNNNSSG NSKLTTTTHL TNNTTTTTIV SGSKTLKRTK VTPPSQSSSS SSPSSDQTNL
PSIAISSSNG ISYKSPPVTS PPPTKPTFSV SLTTSNKIDI SASNPNGNGM KLYGSNATTT
AASSILNNNN NNNNNNNNNN NNNNNNNNNN NNNCGQRRQT VESIFPTFKQ QSNTDLLTSL
MQSTSISLSN KYSSSTTTIS TVDQTPPELT LQSLNILLSQ FKQSYLFPDS ITLSFNYLTK
QKENIEQMEK IIQSKIQLIQ ETKPKQQQLQ QQQQKNLLNY SSSFNEYLTN HDNLIDSILI
GLKNDLSQLQ KSFEICLTLY KEMITQQIQL VLKRLKSAHS FINQLIGLPQ SRVSKLPKDF
IVRFIKHTHR IIYQLYNSAN NTFIKLDNEI KIDIDEFIVQ SNDLFSKLPN GAITTNGTTM
NSIPSPVSPI GSPPLPSISA SVYEYFLGKK SSSSLTLNVS QQQQSSNSLD RSSVQFEPSD
ITPGPFSFIS PLDKIIEEIM SGHYQLILPV ASSGDDLLVS VVSLGLIDLR SYLSSNNRLK
EISKSSLIQL FNILLHSTVI CHNINSYLPE VFKTLILLLP FYPKKDELFI KYKEIFIGFM
ELCVIDELCG FSFIYLEFLG LLVKPKKKGL RKELKKEFVE LFPIQLFIDI MEKPIVDATN
KNAEKTRAQA AQILINLSIS SIECLLEVKS KNALGPILDI CKFGQAFAHT QIEESELQIL
QFLGEGALAE VHKGIWKGKE VAVKIFNEGS FSFRLEDFLK EVAILGLISH PNLLKLKGAC
IAPRSHKSTF MIVTELMHKG TLLEVINKNK PLSLEDIIKY ALSVAQGLAY LHSVDFIHRD
IKAANILVDK NNNAKVGDFG LSRVIDNNFN MTAVAGTPKW ESPECLMGEA YTSASDVYSY
GMMLFELATG DEPFLEIQSI VELARSVCDK KLKPKISSSV PNFISSLIKD CLHNSPKKRP
TMNQIIQKLC NHKC
