Y9963_DICDI
ID Y9963_DICDI Reviewed; 1331 AA.
AC Q55A09; Q8MMX0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0272254;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0272254;
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=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 [2]
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}; Multi-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; AAFI02000008; EAL71279.1; -; Genomic_DNA.
DR RefSeq; XP_645175.1; XM_640083.1.
DR AlphaFoldDB; Q55A09; -.
DR SMR; Q55A09; -.
DR STRING; 44689.DDB0229963; -.
DR PaxDb; Q55A09; -.
DR PRIDE; Q55A09; -.
DR EnsemblProtists; EAL71279; EAL71279; DDB_G0272254.
DR GeneID; 8618347; -.
DR KEGG; ddi:DDB_G0272254; -.
DR dictyBase; DDB_G0272254; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_259076_0_0_1; -.
DR InParanoid; Q55A09; -.
DR OMA; HETISVK; -.
DR PRO; PR:Q55A09; -.
DR Proteomes; UP000002195; Chromosome 2.
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 Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Kelch repeat; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1331
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0272254"
FT /id="PRO_0000355170"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 665..710
FT /note="Kelch 1"
FT REPEAT 716..769
FT /note="Kelch 2"
FT REPEAT 770..816
FT /note="Kelch 3"
FT REPEAT 822..868
FT /note="Kelch 4"
FT REPEAT 909..959
FT /note="Kelch 5"
FT REPEAT 962..1008
FT /note="Kelch 6"
FT DOMAIN 1073..1331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1200
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1079..1087
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1331 AA; 147443 MW; ACC419FA8158240D CRC64;
METSSNSSGS SSSPPSQHQQ QQQQNSQLNL SSQSCFSNNS SSAADFNNYM ESKLSEENNY
YKNFNSNLDR GDSFKLEKES IKDTIKDNIK EDKICNDNNN SSSSSSSSSS GNNNNNIKDG
RAPSPITTQQ ISPNKLILNT TKAITKPTPI LNTQQTPTTT ATTNTSTSTT NSTPSKFKKI
KNSTINPTIE FISKPSLSVM FGFSPIYFVE SIFIVLLIYI LSNFVLKETS VYVISIFVIY
FVIYFDNRYQ IINKLSKSSI NDSDSSSNNN NNNNNTTTTN NDSASTKGNN NNEISSPETY
QKDVKSKINF YEHVNISSTN LNNVNTTSNT PITNPSNVNQ PSNITTATTA TTTSTNNNNN
VNNSINNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NGNNNGNNNG NNNNILSKEN
STNSLLNNLI LNNTSVGKTH NRSSSGSDSI QPPPLPTGGS SHNIFYSAFP THPYTDIDQS
STYRTRTFGS SSINNRKSLP PEYYNQYLNF LAHSNNNNNN NNSNTNNNNN NQSVSAPVSQ
LATPVYQTPG TNSVVGNLEN DNENNNDSFS DINDNNSVVG NDFEQDDQIL QNNGISTTTS
TIVPTNDETK QELSQLENSN KVRSTVSKFI KLSTGVEEKL DWAIAQQCTL QPPRSSHSVT
VYGSSLVLIG GEGITGENLV QFIDVERNLF ISPKVTGGKV GPESIYNHDY CRIGNKFYLF
GGYVAGKLSN KLYVLTIMDD STVHWSSPRI SGGCIPSPRY GHTFTRYGNR FLLFGGYDGE
QCLNDLYILE PETMCWSTVT NIKGGQTPSE RFGHTSTILG EKLIIFGGKG INNNNNNNNN
NNNNNNNNNN NNNNNNNNNN KGLVELNDTH ILLLNEIDSS FQWQVASFHQ VSEIPSERSF
HSATRVGRNI VMVGGKKDDS NGNPIALRDC WVLSYRMQWS KVSGVQFSPP RYNFGLIKNG
SKLFILGGKG NNNNINNNSS SGGNNSSSSS GNSNTIITNT TNTTNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNLSILDD IWFVNTVTLP ISSSVTMINY SDIKIDKEIG
KGHFSKVLKG NWKGKDVAVK KLNSNKDKAR EEMIQEFKAE VELLGSLQHP NLVTCYGYSL
NPMCIVMEFL PSGNLFELIH SKPSEQQQSI KLDSTLILAI AFDIARGMQH LHTRNIIHRD
LKSSNLLMDK HFNIKIADLG IARETSFTQT MTTIGTVAWT APEILRHESY NQKADVYSYA
IVLYELLTGE EPYQGIPPMN AGILVASKGL RPELPDNCDP NWKKLVVWCW SEDPNKRPSF
EEITNYLTKT F
