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Database: UniProt
Entry: A0A094BJU8_9PEZI
LinkDB: A0A094BJU8_9PEZI
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ID   A0A094BJU8_9PEZI        Unreviewed;       868 AA.
AC   A0A094BJU8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=V494_03809 {ECO:0000313|EMBL:KFY39853.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY39853.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY39853.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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:KFY39853.1}.
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DR   EMBL; JPJW01001253; KFY39853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BJU8; -.
DR   STRING; 1420907.A0A094BJU8; -.
DR   HOGENOM; CLU_000288_26_1_1; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000029288; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 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:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029288};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          243..256
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          588..839
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..406
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..482
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   868 AA;  95442 MW;  7EEE3B02B7141678 CRC64;
     MEEIKSTTRR LTKKPPPHLH QSVSRTSDST TNSRLDNLSI RSQRSSTSLQ RAPSAPFPRS
     HNNTNSGHVR TITSPSFAAY SSSNSSLDRP SGGPSPILAG NELHAPSGAQ NAGKRHSNPQ
     PRGLLETSSE EFVGAPFDGN GILNQIDATK ASGFQNSLRR PPPPPLSHTT PLPQTTSPAL
     RQSASFSNDR NEKNVSRTTE NQIISPKRYS DETNQPKNFA LRKKTGFSGF MNSLVGSPRR
     VNISAPENPV HVTHVGYDND TGKFIGLPKE WQRLLNDSGI TKKEQEQNPQ AAYDIVNFYK
     DNAGKAEDET VWEKFDHARA QDPRTAGAMS PPITSPNYTA AMSPMMSPPA SPRFPPTETS
     FENPRSPPPV PRSTPMMATG PFVPKDTGLV PSRPAPKPPA SGPGRAAPTP PIVVKDVSGG
     VPRQSTDLPA LTYVPPAEPQ HGAAMLPEEH RSRSRSNSKA TGPSPYAAPP PQQQPQQPQP
     QAQPLSPQQA YQQQIVKQQE QAMTQAQQVM SVQRSQSKRQ QTQQPTPPHS QHQPARTPTD
     PNGIPAPNTQ ARNVPGPRPR QRARQSTSLD IIDRLKRICT DADPREIYKN LNKIGQGASG
     GVYMAYERVT NRCVAIKQMN LEQQPKKDLI INEILVMKDS SHPNIVNFID SYLVGGDLWV
     TMEYMEGGSL TDVVTFNIMT EGQIASVCRE TLKGLQHLHS KGVIHRDIKS DNILLSMDGN
     IKLTDFGFCA QINESHNKRT TMVGTPYWMA PEVVTRKEYG RKVDIWSLGI MAIEMIEGEP
     PYLTESPLRA LWLIATNGTP AIKDEAALSA VFRDFLYFAL KVDPEKRASA HDLLRHDFMK
     QCSDLGQLSP LVVSARKARQ QERAMKGA
//
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