ID A0A093XQB6_9PEZI Unreviewed; 802 AA.
AC A0A093XQB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=V490_05221 {ECO:0000313|EMBL:KFX92737.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX92737.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX92737.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX92737.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00023596}.
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:KFX92737.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJS01001476; KFX92737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XQB6; -.
DR STRING; 1437433.A0A093XQB6; -.
DR HOGENOM; CLU_000288_5_5_1; -.
DR Proteomes; UP000029320; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR CDD; cd14135; STKc_PRP4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR044092; STKc_PRP4.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-RELATED; 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.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029320}.
FT DOMAIN 480..796
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 802 AA; 90147 MW; 8EA410A6453364EA CRC64;
MPLAPLAQSV RQAFVVSRLE ILDVTSTKHF EQHITFVQTK ASREDADSKY LDNALKTENE
KIYTREWLRR GGDTGCRIRQ EYDLDTRLLR LCQSKTALFL PCGDQQRDVY HQGAQSEIEM
TTTTLAVTET RDDTRATTKT AQPNDVASNP TKTWIGKALP QVVSDMTMET GTATGARAHG
RAADLHIEPP TTPKPETITS RNHSETIMVA PGFKRPVRYS QRRGDNHKSE RDIERSQPPV
EEPPSDTEPL DEAALIEQRR KRREAIKAKY KGSATPLMVQ ALQIGDRATP ETRSQSEQDG
DDNQPTRNAS PDVATPSTPK EIQDPSAFTA LNDQELANNA GGGANPEDGP SAADYDPTMD
MKEDRFRDDK RHTEDVPSSA YDETKPTREQ EVLLPVSVQE AEEKPKKSKD DFDMFADDDD
DDMFAEEPET TAGPTHKTGD VAVAVPIPEA KVLNVGMLDN WDDAEGYYKV ILGELLDGKY
HVQANLGKGM FSGVVRATDI TTKKLVAVKM IRANETMRKA GMKEIEILQK LMDADADDKK
HMIRLERHFE HKGHLCMVFE HLSINLREVL KKFGRDVGIN IRAVRVYAQQ MFLGLTLMRK
CNILHADLKP DNILVNENRS MLKICDLGSA SDASDNEITP YLVSRFYRAP EIILGMPYDF
AIDIWSVGCT LYELYTGKIL FVGRSNNQML RSIMECRGKF TTKMLRKAQF AHMHFDEQTN
FLSVEQDKLS GRDTVKTLPL AKPTRDLRTR LASGAKGLPD DEAKELNLFI DLLDKCLALN
PEKRCTPAEA LKHPFLNRPV GR
//
