ID S8BNE8_DACHA Unreviewed; 778 AA.
AC S8BNE8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=H072_5118 {ECO:0000313|EMBL:EPS40988.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS40988.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS40988.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS40988.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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};
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:EPS40988.1}.
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DR EMBL; AQGS01000267; EPS40988.1; -; Genomic_DNA.
DR RefSeq; XP_011111004.1; XM_011112702.1.
DR AlphaFoldDB; S8BNE8; -.
DR STRING; 1284197.S8BNE8; -.
DR eggNOG; KOG2464; Eukaryota.
DR HOGENOM; CLU_351604_0_0_1; -.
DR OMA; ASEEYQY; -.
DR OrthoDB; 5491350at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035173; F:histone kinase activity; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 389..778
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 87342 MW; 6DEE1361C2B0FD99 CRC64;
MPSALQKPRM YGTARRGGGT AKASFRGSVR AWDNQRKGGL LMQSAAPQQP QSKPTVQQNH
SGYDSDSDGS DDFELESPPE SPVTTKTLPT ESSVPLPPCT PARQENLKDS EDSSADESEM
PALRNRKPLA QKSVSETNRL LQAPNPNKAK GKGRNRKSKS RKSTVKESVI IEAIRQPTTP
LTAKRVTRSQ DEEISTPDHM EVELPLSLNT DSSVEEAAPA VVDLASDEED SAVTDLTTDE
ASTQSDSSED ARGKGEVESE VEKEELGDTA LLSPQKRAAL HNQARRRGRG RGAPLAFKRD
SLASNFQSLA IESPLKQQQP ELETESEESA ESSPRISTRT PSPSRSPTPE SDPVLTLAPE
SEVFNLLPFC DEKRIMTYTE YLKSISPDFS RIKKIGESSF AEVYIHKTDD GRSVVLKLVP
LAEENNVKEV IQELKITRTL SPLPNFINYL GCQVVAGDVP EGFEEAWRIW AETKDEEYQE
GISKFGEADY YAIIALEDGG CSLEHTVWKT WDVPLEIFRQ TVVAFAEAER QREFEHRDLH
NGNLLVRDLK KEREDNAKEE SGVGRELEVG SFEDVAVTVI DYTLSRAQIP EEFGGGIAYM
ELEEGMFEVE GLYQFDIYRS VREEVVMLKA RSNGTKGRRC SGRVNKPEWS TYCPRSNVMW
LHYLIKILIR SDEGRRNGGK LWIRKPTKAK KNAFDLDCWG KMMKLHEMMD KEADEECNFN
GAVDIEKWCS QEGLFEGLEE ERKKRGRERG EKEEEPEAVE EDAAPKKTRR KGRGKVRK
//
