ID F8MUW8_NEUT8 Unreviewed; 952 AA.
AC F8MUW8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=NEUTE1DRAFT_88085 {ECO:0000313|EMBL:EGO54593.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO54593.1};
RN [1] {ECO:0000313|EMBL:EGO54593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO54593.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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; GL891307; EGO54593.1; -; Genomic_DNA.
DR RefSeq; XP_009854537.1; XM_009856235.1.
DR AlphaFoldDB; F8MUW8; -.
DR GeneID; 20831086; -.
DR KEGG; nte:NEUTE1DRAFT88085; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_88085; -.
DR HOGENOM; CLU_000288_26_1_1; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000008065; 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 332..345
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 672..923
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 952 AA; 103554 MW; CEFC04E931B9311B CRC64;
MDGQLSLLSP TSSSSTSHSR KRLTKKQRPP SANHRTSSSF NVESLRIDAQ SLDSKRSASS
LRQGPNCNQS PSLARTVSVP VSVPSNAPVH TKASNLSLPR SHTTRSQSAN RPYNPTQTIP
TNRFILSPAS SSQPQSQSPP YPSAVASTTV TSSRNKDTSK QYDPLDSCIG SFDQNKLSTD
ELIGAPFDGN AILSRIEATK LSAAPAPTST TTIAHSNNIS PRRVAPPPPP PALSRSNTDS
KAARSSKPSK SPKSTISNKT MGASSFRHSA SFSSAEQLPP SEKPSKSESS SSSNKRHSGD
GKESRVPGML RKKSGFSGFM NSLVGSPKKP LISAPENPVH VTHVGYDSNT GQFTGLPKEW
QRLISESGIT EKDRREHPQI LVDVLTFYKE TTEKPQEDQQ LEKFHDARAT DFRSPPVTGT
APLVLQTGVG YAHGPMSPMI SPPASPRFPQ VGHEGSFENP RAPPPVPKGP GPLPAKDINL
IPSRPAPKPP AISTRPLVPP ASLPAKDSGI GMPPPGDEAP MPYLPPKDNV QHMYQEEHRS
RSRSNSRTNG AAPFSPVQAS PLHPIAAANQ TAAYQQQLLQ HQQEQAMAQA QAAMSGQLSR
AASKRQQPTP PTSQHQHPRQ PDINGAPRMP QTQGAAPQAS ARPRHRPRQS NAIDVVASLK
RICSDGDPRE IYRGFTKIGQ GASGGVYTGH ERGSNRLVAI KQMNLEQQPK KDLIINEILV
MKESSHPNIV NFIDSYLCAG ELWVVMEYME GGSLTDVVTF NIMTEGQIAS VCRETLRGLQ
HLHSKGVIHR DIKSDNILLS MEGNIKLTDF GFCATINEAQ SKRTTMVGTP YWMAPEVVTR
KEYGRKVDIW SLGIMAIEMI EGEPPYLTES PLRALWLIAT NGTPHIKDEQ SLSPVFRDFL
YFALKVDPEK RASAHDLLRH DFMNKCVDLS TLAPLVRAAR EARAQEKARK GQ
//
