ID A0A0M4ENL8_DROBS Unreviewed; 544 AA.
AC A0A0M4ENL8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=Dbus_chr3Rg1064 {ECO:0000313|EMBL:ALC46314.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC46314.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC46314.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC46314.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pseudokinase which, in complex with CAB39/MO25
CC (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates
CC STK11/LKB1. Adopts a closed conformation typical of active protein
CC kinases and binds STK11/LKB1 as a pseudosubstrate, promoting
CC conformational change of STK11/LKB1 in an active conformation.
CC {ECO:0000256|ARBA:ARBA00034653}.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CP012526; ALC46314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4ENL8; -.
DR SMR; A0A0M4ENL8; -.
DR STRING; 30019.A0A0M4ENL8; -.
DR OMA; KMRTANC; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06610; STKc_OSR1_SPAK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR047173; STRAD_A/B-like.
DR PANTHER; PTHR48014; SERINE/THREONINE-PROTEIN KINASE FRAY2; 1.
DR PANTHER; PTHR48014:SF24; SERINE_THREONINE-PROTEIN KINASE FRAY2; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..311
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 330..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC46314.1"
SQ SEQUENCE 544 AA; 59700 MW; 72FCC54F65EBFF1D CRC64;
SSSIPTVLSS NNVAAATAAA AADASEKQPW PNSKDDYELR DVIGVGATAV VHGAYCIPRN
EKCAIKRINL EKWNTSMDEL LKEIQAMSSC NHENVVTYHT SFVVREELWL VLRLLEGGSL
LDIIKHKMRV AICKHGVFDE ATIATVLKEV LKGLEYFHSN GQIHRDIKAG NILIGDDGTI
QIADFGVSAW LATGRDLSRQ KVRHTFVGTP CWMAPEVMEQ DHGYDFKADI WSFGITAIEM
ATGTAPYHKY PPMKVLMLTL QNDPPTLDTG AEDKDQYKAY GKTFRKMIVE CLQKEPSKRP
TASELLKHAF FKKAKDRKYL TNTLLQSGPS METRVHKAAK RQPGASGRLH RTVTGEWVWS
SEEEDNATGG ASSSRRKHPS SDSESEDRPI NRLERADSSD SDRDELTPEI TRSMSSATMT
PAGAAQELAA GVAALPLPSE AAAAGEAPPV NLVLRMRNLR RELHDIRFEF AVGKDSAEGI
ATELVDAGLV DALDTQPMAV HLDQLIAQCD SMKTITFQLS SGVQPGEVPD ERSLVGYAQI
SITD
//
