ID A0A0D2IF10_9EURO Unreviewed; 877 AA.
AC A0A0D2IF10;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=Z520_08398 {ECO:0000313|EMBL:KIX95691.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX95691.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX95691.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX95691.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN848080; KIX95691.1; -; Genomic_DNA.
DR RefSeq; XP_016629814.1; XM_016778895.1.
DR AlphaFoldDB; A0A0D2IF10; -.
DR STRING; 1442371.A0A0D2IF10; -.
DR GeneID; 27714144; -.
DR VEuPathDB; FungiDB:Z520_08398; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000053411; 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:UP000053411};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 249..262
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 597..848
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 877 AA; 95748 MW; 275C64A873A53456 CRC64;
MDNVHNTTNT TSSNLTTFTS SKRRRNTLTK NPPPSAFPSK GSLRKQQSSA ALQRAPSAPS
PYPRSHDASL SSRDFHQRTQ SSAFASSTSS LEHSSGAPSP IVPSPNFFAS AVNGYQAPQH
LPLTPQTSDD RHKDLIGAPF DASGLLSSFQ ATGMNDNQNA GAQSPYPPPL TQAHTSPDLR
SHPLRNSQTF GPGMVAMMEV TPPKSENGTL SPKRFSGDLH TKPAGPFRKK SGFSSFVNNM
LGSPRTIKIS APENPLHMIH VGYDNQTGQF TGLPADWQRI LADSGITKTE QDQNPQMMVN
IVETYKNNLG GNDDGVWQKF DHAKLSDSPQ SSNSSYQSPV TPIIGSSVAS YSPMAGVISP
PASPRFPQNH EGSFENPRAA PPVPKIPPAS AMAGMKPSQS QMMMMPNRPA PKPPAQSLRD
MAPSRPAPPP PISRDLPLRP VQEQPKPQPP PPPASLPDTP SIPQEEVRSR SNSKGPTATP
PRTQPAIQSP AQYQQQQEQA MLLAQQAIQS KQLDRSRSQR QVAQGAPEVP PKILPQQISP
NIPQAQFAAV TASPALEGTP QVAAVPRPRQ KRQQSNIVDV TARLRAICTP GDPTTKYSNL
NKIGQGASGG VYTAFENGSR RCVAIKQMNL EQQPKKDLII NEIIVMKDSK HRNIVNFIDS
YLHEGDLWVI MEYMQGGSLT DVVTFNVMSE GQIAAVCRET LLGLQHLHSK NVIHRDIKSD
NILLSERGDI KLTDFGFCAQ INDSQNKRTT MVGTPYWMAP EVVTRKEYGR KVDIWSLGIM
AIEMIEGEPP YLTESPLRAL YLIAKYGTPR IKDEQALSPV FRDFLHFALK VEPEKRASAH
DLLHHPFMHN CAPLSSLAPL VQSAKESRAA EKANRGN
//
