ID G4UBT3_NEUT9 Unreviewed; 1943 AA.
AC G4UBT3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-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=NEUTE2DRAFT_78162 {ECO:0000313|EMBL:EGZ77097.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77097.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77097.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., 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 Genetics 189:55-69(2011).
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. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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; GL890999; EGZ77097.1; -; Genomic_DNA.
DR STRING; 510952.G4UBT3; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000709_0_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd05611; STKc_Rim15_like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF1; SERINE/THREONINE-PROTEIN KINASE GREATWALL; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..105
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 707..1137
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1138..1261
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1508..1622
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1943 AA; 211482 MW; 919C92A28EF5901A CRC64;
MEEQSKAPSL LAPPAVSSLR TGKMERSLSE NIREEREDLR EAAEQTLNVI MDLNLDGTIR
WVSPSWVDVI GTQPEQVTGT AITDLIVSDN KSIFADVIES MQRDDSKSKF IRFAVKVGPL
SRLLPLEQAE EPTIIDVEAQ GIMVYDGASG KDSHTMWMIR PWVAPREIKI DLPAFIVESL
GSGAEVLASY LTQLAESGLD DPNGHPPPAP VLCRICERQI PPWWFEKHTD LCLQEHRAEM
DVQMTQESLI DHRHAIVKVL DALEARHSRT LIGDPANLPI AEYKGMHIGP PTSTTSSPGT
SSPSSNSGRS RDRSSGFGHS RARSFAIRRP QARIVELLLD LCDTAIEIST PAIKETTQNP
AEFRTQSPQS EGRISQVMQW ETPGTNTLEQ EQGLALLCTD TEAVAKAKVE AVFRHRRILE
YAERIRIEFA IVVQECIDEA MRRAAKIAAG RLSDSTEEEE EEDFEQTEDE EATSAQEEGI
FPGSFDAPST LAMALEKAHI SGERPSRRLS ISIKSTRSSS PKECPTPRSN RGTLGNLASA
TQSRRESMLL ESDAGDSDGG SIRSSSVASR MPTRTESPLS EFSDLRRHAS SRQRNRRSLI
LPGTISPRRQ ESPSRNGPPS SPLRLHKPRN LPFPSDSLVS PEASPMLPSS EFTSPTPPSI
HHHRRQSSAA VSASTGDLGF KPPPSPRLSA VVGAPQAKAV PPSIKDFEII KPISKGAFGS
VYLSKKKSTG EYFAIKVLKK ADMVAKNQVT NVKAERAIMM WQGESDFVAK LYWTFSSKDY
LYLVMEYLNG GDCASLIKVL GGLPEDWVKK YLGEVVLGVE HLHSRGIVHR DLKPDNLLID
QKGHLKLTDF GLSRMGLVGR QKRALNNGAD AAPDLLKQGP FVRSSSIASS RSTSLDVHAR
NPSPLSTPQM TPSDYGAGLG QPSYFNLGVL SQEPRRLSAN RSDSGGSEAL SHMLPNLSLN
DTLSVPPQAI QSPGERSETD EGTNPDFVSL SHATTQSNID ANRGTPPQQP HMPPPNWALF
DPQDTNRRFV GTPDYLAPET IRGEPQDETS DWWSVGCIMY EFLYGIPPFH APEAEQVFGN
ILARKLEFPD DSDMEISSEA KDLINKLLCS DPHQRLGANR EDKFQSGGEE IRSHPWFEGV
NWETLLQDDA QFVPQPEHPE DTEYFDSRGA VLQSFAEEME DQSSPPSSAP APDYHNRPHD
ALAKVRSQVN SNINTVKRGL MPLHIPPHVR DLKSRRLSEP VAADDFGNFS FKNLAVLEKA
NKDVIQRLRA EAAESQTKPI SPGALSSISS PGTLGALEGS PVIANPVQRT LSAAKASQCP
QSPSGIGHSN SPNRASQPSS PLLVSFVAGQ GAEGRRKASS NSSSLSHQSG SFQSTVEGIR
VPPTLQKAAT TTTASSPSNG RLVMPPLPLS PQRTVPAHTL TSSPRNTSGP ATGRARSLTV
GSQEGSGSPI SADILAHHKR RSQVLDMSPS SSDTEGDKAN ALLRVQRRRQ SSRRMSQVLD
GPMFRPLDVL ICEDHPVSRM VMEKLLEKLR CRTISASTGQ EACRYALSDI KFDIIFMEFK
LPVINGSDVA RMVRETKNKN HHTPIVAITA YLKELHAPHY FDSLIEKPIS SSKLSEVLST
FCQWKPASPG QAQMLSLGLP PPVPSGLRQE SLRLEDSPVS ASGSSKYTVH SGGSVKEEST
CSTFGDSESV ATDDIPVVVS RKATGDWSEG GLGISGSEEV LVASDDGSKP PVHTQLLTQQ
SAPAQMEHSA GQTKGPVPQR SLEKLRARRE SIEKRRLEGC IDSADDEDEE LGAGQANSGQ
EPHPAKHHRP KSTLPSSKLG IEMMRANSHD SMTAADSEGA SSATLGPPTA QIVTPTTDVQ
MELPPLVVDT AAATMAPYTT VADEEAAAAT VSTPPDLRPE TEGRKICHVE QTPRQLSLAK
VDEEAVEADE EPTPRPLSRS VNQ
//