ID A0A4Q4XK82_9PEZI Unreviewed; 778 AA.
AC A0A4Q4XK82;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DL770_009819 {ECO:0000313|EMBL:RYP61310.1};
OS Monosporascus sp. CRB-9-2.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211643 {ECO:0000313|EMBL:RYP61310.1, ECO:0000313|Proteomes:UP000294245};
RN [1] {ECO:0000313|EMBL:RYP61310.1, ECO:0000313|Proteomes:UP000294245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRB-9-2 {ECO:0000313|EMBL:RYP61310.1,
RC ECO:0000313|Proteomes:UP000294245};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYP61310.1}.
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DR EMBL; QJOA01000703; RYP61310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q4XK82; -.
DR STRING; 2211643.A0A4Q4XK82; -.
DR OrthoDB; 193931at2759; -.
DR Proteomes; UP000294245; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; cd14334; UBA_SNF1_fungi; 1.
DR FunFam; 1.10.510.10:FF:000544; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 1.10.8.10:FF:000069; Non-specific serine/threonine protein kinase; 1.
DR FunFam; 3.30.200.20:FF:000236; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
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; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 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}; Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000294245};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 79..330
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..50
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..491
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 778 AA; 87184 MW; D32200E5E349493A CRC64;
MAQRAFDEEE LSISISPSQI RRNNRPGRVP EINVTPHQTA ETAAASSNGA AAGGEGRSRA
SSLMGGDQKA KLEQRIGAYN IIRTLGEGSF GKVKLAVHRM TGQQVALKVI ARKKLISRDM
VGRVEREIEY LQLLRHPHII KLYTVIKTQN EIIMVLEYAG GELFDYIVSH GRMPEDQARR
FFQQMLCAVE YCHRHKVVHR DLKPENLLLD DNLNVKIADF GLSNIMTDGN FLKTSCGSPN
YAAPEVISGK LYAGPEVDVW SCGVILYVLL VGRLPFDDDH IPSLFAKIQR GVFTIPHWIP
ADAQALIRKM LQVNPVQRAT IDEIRQDPWF LKDLPAYLQP PVEEFLNTGV DPNRAIRPSD
IAPNAPVKVA EKLYEEVTEK ISKTMGYGKK DVQEALEADE PSAIKDAYMI VRENKLMQVN
PAYGTGADNP YFATSPPSAT HEENMASVAQ TLQDTSIESN EVPEGDQIPE PQASPLAESN
RSTTSTAASS SPRGYVSKVG ILPTSLPALH REYLERQNAG IEEPLSSQPV PDVPLQPRTP
AEQQEAVRRL KPHSKGSVKL DDSARPQTMT PVAPKKPKPT RWQFGIRSRN APWEALLCIY
KSLSKLGATW VVDEDYEKVH ENDQEVQNGS FATNTPLDTP AEQAPNPYEG VPADQIDLKT
FDPVKYYKLP ADPWHIICRW RKDDLRKSTV SSGHMSPEEA SEQNTYVYSV IDKRKQDFVW
MRMEIQIYEM EYGVYLVDFK CSGYERDDGT LLEEKDVMSP FPFLDMAAKL IMQLAEAD
//
