ID A0A914E2X9_9BILA Unreviewed; 576 AA.
AC A0A914E2X9;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Acrobeloides nanus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Cephalobomorpha; Cephaloboidea; Cephalobidae; Acrobeloides.
OX NCBI_TaxID=290746 {ECO:0000313|Proteomes:UP000887540, ECO:0000313|WBParaSite:ACRNAN_scaffold5301.g15436.t1};
RN [1] {ECO:0000313|WBParaSite:ACRNAN_scaffold5301.g15436.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR WBParaSite; ACRNAN_scaffold5301.g15436.t1; ACRNAN_scaffold5301.g15436.t1; ACRNAN_scaffold5301.g15436.
DR Proteomes; UP000887540; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14336; UBA_AID_AMPKalpha; 1.
DR FunFam; 1.10.510.10:FF:000079; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 1.10.8.10:FF:000055; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 3.30.200.20:FF:000136; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 3.30.310.80:FF:000020; Non-specific serine/threonine protein kinase; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049020; PRKAA1/2_AID.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF110; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF21147; AMPK_alpha_AID; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000887540};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 395..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..434
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 576 AA; 65247 MW; C1C4F3FB9D35DEA4 CRC64;
LTIWKISKIK MASTELTKAD RELKPQIKIG HYVLKETLGV GTFGKVKVGI HEATGYKVAV
KILNRQKIKT LDVVGKIRRE IQNLSLFRHP HIIKLYQVIS TPTDIFMIME YVSGGELFDY
IVKHGRLKPP EARRFFQQII SGVDYCHRHM VVHRDLKPEN LLLDDRNNVK IADFGLSNIM
TDGDFLRTSC GSPNYAAPEV ISGKLLYAGP EVDVWSCGVI LYALLCGTLP FDDEHVPTLF
RKIKSGIFPV PDYLDKSVVN LLLHMLQVDP MKRATIKDVI QHEWFRVDLQ AYLFPPINES
EASIVDIDAV REVCYRYSVT EDEVTSALLC EDPHHHLAIA YNLIVDNKRI ADETAKLTIE
EFYNVTPAGK LHQADQMHRH PERISGSSKI TPTLEHSAAV QAEQGSSQNS SGSTAQTSQT
TPKSPHIKRA KWHLGIRSQS RPEDIMYEVF RAMKYLDFEW KLLNAYHVIV RRRPKNSSQE
MPKMSLQLYQ VDQRSYLLDF KNLVDDEPLD GSGNSSRHAS VSMPVKPAMR PTRAQSLPMP
METDSTSPPP SPSVTKQSQT MQFFEMCAAL IGALAR
//
