ID A0A1A9ZE91_GLOPL Unreviewed; 683 AA.
AC A0A1A9ZE91;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI011995-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI011995-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI011995-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A1A9ZE91; -.
DR STRING; 7398.A0A1A9ZE91; -.
DR EnsemblMetazoa; GPAI011995-RA; GPAI011995-PA; GPAI011995.
DR VEuPathDB; VectorBase:GPAI011995; -.
DR Proteomes; UP000092445; Unassembled WGS sequence.
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}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 160..434
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 454..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 683 AA; 75799 MW; 3F7F2F046BC83A12 CRC64;
MLKVANISQQ TETFSSSLIS QSKSYTITSG TTQLGLQEVA IEAGPITACY KASIDEENLN
FCNNLSKDST VAFEQPLSVN TGNPELKLQC LKEGPERLKV HLLTGSSNEE TGGHIATFDL
EYFLPSFIFE SEMASAAGTS NTGNTSTNDK QPWPNSKDDY ELRDVIGVGA TAVVHAALCL
PRNEKCAIKR INLEKWNTSM DELLKEIQAM SSCNHENVVT YHTSFVVREE LWLVLRLLEG
GSLLDIIKHK MRTTNCKHGV FDEATIATVL KEVLKGLEYF HSNGQIHRDI KAGNILIGDD
GTIQIADFGV SAWLATGRDL SRQKVRHTFV GTPCWMAPEV MEQDHGYDFK ADIWSFGITA
IEMATGTAPY HKYPPMKVLM LTLQNDPPTL DTGADEKDQY KAYGKTFRKM IVECLQKEPS
KRPTASELLK HAFFKKAKDR KYLTQTLLAS GPSMETRVHK AAKRQPGASG RLHRTVTGEW
VWSSEEEDNG GKRHSSDSET DDRPINRLER ADSSDSDREE HSEFSEPTAT ASQAINQQQQ
QQQQQQQQQQ QQQTPAVTSP IMAQATEAMA QIPMPSSIEM AITGEAPPVN LVLRMRNVRR
ELHDIRFEFA VGKDSAEGIA AELVEAGLVD PLDTQPMAIN LHQLIEQRAS LKTVTFQLNS
GVQPGEVPDD RSLVGYAQIS ITD
//
