Y3337_DICDI
ID Y3337_DICDI Reviewed; 1128 AA.
AC Q54R95;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0283337;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0283337;
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; AAFI02000052; EAL65809.1; -; Genomic_DNA.
DR RefSeq; XP_639152.1; XM_634060.1.
DR AlphaFoldDB; Q54R95; -.
DR SMR; Q54R95; -.
DR STRING; 44689.DDB0231195; -.
DR PaxDb; Q54R95; -.
DR EnsemblProtists; EAL65809; EAL65809; DDB_G0283337.
DR GeneID; 8624022; -.
DR KEGG; ddi:DDB_G0283337; -.
DR dictyBase; DDB_G0283337; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_279453_0_0_1; -.
DR InParanoid; Q54R95; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-8854214; TBC/RABGAPs.
DR Reactome; R-DDI-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q54R95; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; 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:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1128
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0283337"
FT /id="PRO_0000362051"
FT DOMAIN 777..1054
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 904
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 783..791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 809
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1128 AA; 130435 MW; 37114D1FFA76C2A9 CRC64;
MENNNNNNIN KTNTPNNSFS PIKNRIEHFE RMSSSPNISI PLSQKEYYCS PKKNISLNNI
NHNINYNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NCIVGESNII NNNKDDYNSN
NNSTINYNIV RESNSNNNSN NSNININNNS NNNFEKEKII ENNKEYINSD FDSISNNDNN
NYNNNNIFIF EKIEYNKEEI DCVIAINSDI ESNKNDENDD NYKNHNYEII IVGENNNSKE
DCNSSNNSYD NDSNSNSDIS TSVNCNSINN NDTIDKNNST NIIKSIENNN KNNYNKNNNK
NNIKSIFENI LIKVFTIIDK ESSKLIQGLK IENKLKSQLS YLEEDYIYQT VLAILQTKVL
QVIFNDVFPN SNIYNDNENN NNNNNNNNNN NNNNNNNNNN INNYIVEESN NNISVIDNNN
NSDNNNNNNN NNNNNNNNNN NNNNNNNNNN NNKSNNYIVE ESNNNSVIDN NNSVIDNNNN
INNNSNNNNN NNNNNNNNNN NSEQNFTYNE KKIQNPIIRC IRNLREIRIK KIPKNIHVDL
FQDYRNIQII HNQFPELFTD SINDCYKIFH HFCLTYSGPD VKQFLCEFSK IGVISCSDEN
ENSSLYYAIE NKVNGLQLVC EMVCNGLINI EMAKKTNKHG HSILCKCINL KNIPILKLLI
SFGFDHFEIC QNCKNTDQDI QDIFDDIYFS MAYFSTIPDS VNGKLIKTNI ALLTELIYSQ
EKLKLLFKVA NAPVPTEIEK AVNKFIFKMD DYKTKYNLKK NEIESIEKVG IIDKSQLSDF
SIIGEGGFST VHKATYINLQ NTITPVAIKS FKNYDDDSFE RIYKEVSVHQ SLQGENILKL
IGVSKLKFGL SIIIEKCDMD LKNFISCNQI NLDLFFILST QMVNSVSQVH NHYPEAEINV
YHRDIKLENW LIKTIDGNHT VFISDFGLSR SNTESNGCTL QQIRGTNLHI APECYKGFLF
SSQSDIFSVG ISLYQLAYKL VYGKFVHPYH EYQIADEPEN LNIIQNTGLI PTIPPNLPSR
LKRLLFLMMS KMPERRPSIK ECIEEIQKCK EEYESDRTKW DTEISVHEDY SLLNEQMINQ
YHYIKSDVLD YIRDFDLNQN PHDNYVQELE SFDYSSYFIK CKSFNEDR
