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Database: UniProt
Entry: G4UBT3_NEUT9
LinkDB: G4UBT3_NEUT9
Original site: G4UBT3_NEUT9 
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}.
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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
//
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