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Database: UniProt
Entry: A0A914Z079_9BILA
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ID   A0A914Z079_9BILA        Unreviewed;       477 AA.
AC   A0A914Z079;
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   Panagrolaimus superbus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC   Panagrolaimus.
OX   NCBI_TaxID=310955 {ECO:0000313|Proteomes:UP000887577, ECO:0000313|WBParaSite:PSU_v2.g6144.t1};
RN   [1] {ECO:0000313|WBParaSite:PSU_v2.g6144.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; PSU_v2.g6144.t1; PSU_v2.g6144.t1; PSU_v2.g6144.
DR   Proteomes; UP000887577; 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-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR   CDD; cd12122; AMPKA_C; 1.
DR   CDD; cd14336; UBA_AID_AMPKalpha; 1.
DR   FunFam; 1.10.8.10:FF:000055; 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; 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   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   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000887577};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..61
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          141..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..159
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  52564 MW;  645AF3CD5AA4CD4D CRC64;
     MCGTLPFDDE HVPTLFRKIK SGIFPIPDYL DKSIVNLLLH MLQVDPMKRA TIKDVISHDW
     FRIDLAAYLF PPINENEASI VDMDAVKEVC KLCHVVEDDV TSALLSDDIH NPLSIAYNLI
     VDNKRIADEI SLGDQLLHPT AIQTSRPSSP TQQGSTTTGL EKGIGSVQIH ARSHTAGPTV
     PAASASSPGA GSGYAILSPP HSATKPQGCT FSPVTDDDSQ TSMDEFTAKI NAHNSASITA
     NPAIIEAATR RVRNQRKSAK MSIDEFYNAM PAGKLHHQDQ MMHRHPERIP EQAQQAAAAA
     GGAGNIPQAS PNTRSPHIKR AKWHLGIRSQ SRPDDIMYEV FRAMKALDFE WKMLNAYHVI
     VRRRVPNGND ASDSRPKMSL QLYQVDQRSY LLDFKNLIDD DENMKLLGSR HASVSSPVRP
     NLRNSRAQSL PMPMEVGKRL PIPSSKADRP STTAASRQSQ TMQFFEMCAA LIGSLAR
//
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