ID M2UN84_COCH5 Unreviewed; 2415 AA.
AC M2UN84;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=COCHEDRAFT_1226495 {ECO:0000313|EMBL:EMD89393.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD89393.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD89393.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of
CC DNA damage, involved in the regulation of DNA damage response
CC mechanism. Required for the control of telomere length and genome
CC stability. {ECO:0000256|ARBA:ARBA00025079}.
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 -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; KB445579; EMD89393.1; -; Genomic_DNA.
DR STRING; 701091.M2UN84; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OMA; MRQHSAK; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 704..736
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1243..1848
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2022..2340
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2383..2415
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2321..2355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2415 AA; 273405 MW; F98DF26DD622003A CRC64;
MAQQSPLSST LDRIVHELRS KNDETRQRAA NTLRQTVESA HRELAPNLFT NFNNEVYTRI
SGLIVTGSDS NERIGGIHAL NALIDFRGDD AGQKTTRFAS YLRAVMRGQD ITAMVVAAKA
LGRLAKPGGT LTAELVEAEV KGALEWLQLE RLENRRFAAV LILRELAKNS PTLMYQWIAQ
IFEVIWVALR DPKVLIRESA AEAISACFEI ISPRDSQMRQ LWFGKVYDEI LRGFTINTNE
AIHGSLLTMK ELLDKSAMFM NDQKYKETVE QVLKYREHRD ALVRREVVLI IPILAAYSPT
EFATKYLHQC MLHLQGLIRK DRDRDKAFVA IGQIANAVGV AISPYLEGIL GFIQEGLIAK
ARNKSVINEA PIFQCLSMIA AAVGQALTKS VERLLDPIFS CGLSDSLFQA LVDMAHYVPP
SRPMIQEKLL DLLSQILAGR HFLPLGSPYQ VSQPPQIWTR DHKDPQTIAQ REAEIALALH
TLGSFDFTGH VLNEFVRDVA IRYVEADNPE IRKRAALTCC QLFVKDPIVH QTSTHATKVV
GDIIEKLLTV GVGDIDSDIR WDVLVALDAR FDRHLGKADN VRTLFLALND EVFGIREAAM
SIIGRLTAVN PAYVFPSLRK VLLQLLTEVN YANSPRSKEE SAKLISSLVG AADSLIKPLI
DPIVEVLLPK CRDPNPEVAS TTLKAIGDLA TVGGEGMIKY IKDLMPVVLD FMQDQTSDAK
RFSALKALGQ LATNAGYVIE PYREYPELMN ILMNIAKTEP EGELRRETVR LMGTLGALDP
DEYQKIMEQS PDTHLILEAQ AITDVSLIMQ GITPSNEEYY PTIVISTLMG LLKDPSLVQY
HTAIVEAVMN IYATMGLKCV PFLNQVVPGF LHVIRSTPAG RSEGYFNQLS QLVRIVRQHI
RPYLPSILST IKEYWSSSPQ LQATILSLIE AIARSLEGEF KVYLADVLPL MLSVLDSDHT
GKRLPSERVL HAFLIFGSSA EEYMHLIIPV MVKMFDKPGQ PVQIRRHAIE TLGRLSKQVN
VSEFAARIIH PICRVLAGSE PTLKQTALET LCALIFQLGP DYIHFVPTVS KILVAHKVPH
ENYARIVSKL QKGEPLPQDL SPDERYGEDD EDLNPAEILT KKLAVNQQHL KQAWEASNKT
TKEDWIEWMR RFSVELLRES PQQALRACTP LGSVYNPIAR TLFNSAFVSC WTELYDQYQE
ELVRSIETAL TSPNIPPEIL QVLLNLAEFM EHDDKALPID VRILGMYAGK CHAFAKALHY
KELEFNAEQN SSAVEALISI NNQLQQTDAA FGILRKAQNY HDVELKETWF EKLQKWDEAL
AAYQRRELEE PDSFDVTMGK MRCLHALGEW DLLSSLSKEK WANASQEYRK AIAPLAATAA
WGLGKFADMD NYLGVMKEQS PDRAFFASIL NIHNNRFEIA VDEIAKARKG LDTELSSLLG
ESYQRAYLPM IRVQMLAELE EIMQYKQNEG NHEKQKSMRK TWMKRLRGLQ PNPEVWQRMI
KVRQLVISPQ EGTDMWIKYT NLCRKSNRMN LANKALQKLL DIESTGDSTV VEFVRNNAHE
ISHPVAYTTY KYMWADQNHK QEALDSMKDF TTRLSEDLAM RSRAAVNPMM AQNGMNGMSN
GQHMFSNVNP FAATNGHNGV NGMHGSSLMN GSVTGTSPTD LAECHRLLAK CYLKQGDWQQ
ELNDGEWDHE FVHEILAAYA AATRYNKDWY KAWHAWALAN FEVINSITSK SDREATDVPH
NIIHDHVIPA IQGFFKSIAL SSTSSLQDTL RLLTLWFSYG GREGVNRTIT EGTKSVPIDT
WLEVIPQLLA RINQPNAVVR QSIHQLLIEV GKAHPQALVF PLTVSMKSDV SRRQRSAKEL
MEAMREHSPR LVEQADLVSH ELIRIAVLWH EQWHEGLEEA SRLYFGDHNI DGMFATLAPL
HAMLDKGPET LREISFIQSF GRELQEARDW CNTFRTSGEI GDLNQAWDLY YQVFRKIARQ
LPSLMTLELQ YVSPKLKEAH DLELAVPGTY QVGKPVIRII SFDPVATVIQ SKQRPRKLEM
RGSDGKAHTH ILKGHEDIRQ DERVMQLFGL CNTLLSNDVE SRKRHLNIQR YAAVPLSTQS
GLLGFVPNSD TLHVLIREYR DSRKILLNIE HRIMLQMAPD YDCLTLMQKV EVFGYALDNT
TGQDLYRVLW LKSKSSEAWL DRRTNYTRSL AVMSMVGYIL GLGDRHPSNL MLDRVTGKII
HIDFGDCFEV AMHREKYPER VPFRLTRMLT YAMEVSNIEG SYRTTCEHVM RVLRSNKESV
MAVLEAFIHD PLLTWRLNHR DASPVEPNYP SERRQSIMGA DTAAATTDPH QMSSIVGRPR
HRSSVAPPQN NEADAKEVQN ARALQVLSRV KEKLTGRDFG KGEELKTEMQ VDRLIKEATN
LENLCQHYIG WCSFW
//
