ID A0A0H1B7C2_9EURO Unreviewed; 2364 AA.
AC A0A0H1B7C2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=EMPG_17631 {ECO:0000313|EMBL:KLJ06877.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ06877.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLJ06877.1}.
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DR EMBL; LDEV01002953; KLJ06877.1; -; Genomic_DNA.
DR STRING; 2060906.A0A0H1B7C2; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000053573; 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; 6.
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; PF13513; HEAT_EZ; 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; 2.
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; 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:UP000053573};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 973..1013
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1229..1798
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1972..2288
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2332..2364
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2364 AA; 266720 MW; 498B5F2754236EDE CRC64;
MAQAASGTDA TQRIFHELKS KHEDTRSRAS YELHDNVIAV SRELPPDKFI EYYNAVSQRI
AQLVVTGNDA NEKIGGLLAL DRLIDFDGVD AAQKTTRFAS YLRSALRSND NAVLIYAARS
LGRLAKPGGA LTAELVESEI QSALEWLQSE RQESRRFAAV LVIRELAKGS PTLLYGFVPQ
IFELIWVALR DPKVLIRETS AEAVSECFEI LAARDVQVRQ QWFGRIYEES LQGLRSNNVD
WIHGSLLTLK ELLLKGAMFM NEHYRNACEI VLRLKDHRDP KIRTQIVLTI PILASYAPLE
FTNLKRDKER NAAFIAIGKI ANAVGNSIGQ FLDGIIVYIR EGLTMKARNR AAVNEGPMFE
CISMLSLAVG QTLSKYMEAL LDPIFACGLS ESLTQALVDM AHYIPPIKAT IQEKLLDMLS
IVLSGAPFRP LGCPENRPPP MPSFAKDYGT FLQEPTDTEI ALALHTLGSF DFSGHILNEF
VRDVAITFVN NDNPEIRKAS ALTCCQLFVH DPIINQTSSH SIQVVSEVID TLLSVGVGDP
DPEIRRIVLE SLDRKFDRHL AKPENVRCLF LAVNDEVFAV REAAISIIGR LSSVNPAYVF
PPLRKLLVNL LTGLSFATTS RQKEESAQLI SLFVANATKL VRSYVDPMVT ALFPKTTDPN
AGVASTTLKA IGELATVGGE DMRQYLPQLM PIILEALQDL SSQSKREAAL RTLGQLASNA
GYVIEPYIEY PNLLAVLINI IKTEQTGSLR KETIKLLGIL GALDPYKHQQ ISESSPDIHH
VNEVQAISDV SLIMQGLTPS NEEYYPTVVI NTLLQNILNE SSLSQYHSAV IDAIVTIFKT
LGLKCVPFLG QIIPAFLAVI RSTPTSRLES YFNQLAILVT IVRQHIRAFL PEIIEVIREF
WDCSYQVQAT ILSLVEAIAK SLEGEFKKYL AGLIPLMLDT LDKDTTPRRQ PSERILHTFL
IFGPSGEEYM HLIVPAIVRL FDKSQGPPGI RKSAIETLGK LSRQVNVSDF ASFMIHPLSR
VVAGSDRTLR QAALDCICTL IFQLGQDFNN YIQLMNKIIQ THQISHHNYQ ILVSKLQKGD
PLPQDLNPDE HYGTLGDDST FADVGQKKIL VNQQHLKNAW DASQKSTRED WQEWIRRFSV
ELLKESPSHA LRACASLAGI YQPLAKDLFN AAFVSCWTEL YGQYQEELVR SIDMALTSQN
IPPEILQILL NLAEFMEHDD KALHIDIRTL GKYAGKCHAF AKALHYKELE FEQDQNSGAV
EALISINNQL QQSDAAIGIL RKAQAYRDVE LKETWFVKLQ RWEEALAAYK RRELIDPDSF
DVTMGKMRCL HALGEWKMLS DLAQEKWNQA SNEHRKAMAP LAAGAAWGRG QWELMDSYIG
VMKEQTPDRS FFGAILAIHR DQFDEAAMFI EKARNGLDTE LSALLGESYN RAYNVVVRVQ
MLAELEEIIT YKQNANDPEK QEAMKETWNK RLLGCQQNVE VWQRMLKVRA LVVSPRENLD
MWIKFANLCR KSNRMGLADR SLSSLESGEG SDQPTPPEVI YARLKYDWTA GRQKEALQML
REFAIGLTEE FSRYSSVLIA HGEHANSDKP GLVNGITDHP DLATARQHIG DVGKFRRLLA
KSYLKQGEWQ TALQKGDWTS EGVRDVLNSY SAATQYNLDS YKAWHAWALT NFEVVNALST
HTNRETFVPH HIVLEHVIPA IRGFFRSISL SSTSSLQDTL RLLTLWFNHG GDAEVSGVVT
EGFSSVSVDT WLEVTPQLIA RINQPNARVR GAVHRLLAEV GKAHPQALVY PLTVATKSNV
VRRSQSATHI MDSMRQHSPR LVEQAEIVSH ELIRVAVLWH ELWHEGLEEA SRLYFGDHNV
EGMFATLAPL HDMLDKGAET LREVSFAQAF GRDLAEAKHF CILYRESRVI GDLNQAWDLY
YTVFRKIARQ LPQLSTLDLK YVSPKLKDAV DLDLAVPGTY QSGKPVIRIM SFDPVSTVMQ
TKKRPRKMTL KGSDGNSYMY VLKGHEDIRQ DERVMQLFGL VNTLLDHDSE SFKRHLTIQR
FPAIPLSQNS GLIGWVCNTD TLHALIKEYR ESRRILVNIE HRIMLQMAPD YDNLTLMQKV
EVFGYAMDNT TGKDLYRVLW LKSKSSESWL ERRTNYTRSL GVMSMVGYIL GLGDRHPSNL
LLDRITGKIV HIDFGDCFEI AMHREKYPER VPFRLTRMLT FAMEVSNIEG SYHITCEAVM
RVIRENKESL MAVLEAFIHD PLINWRLGAR ESPARPSFPT DRRQSIVDEI NVDHPVQPSN
FSRRRPSILE GGILDAQQGV PNEAREVQNA RALQVLSRVK EKLTGRDFKS TEELNVSDQV
DKLLVQATSV ENLCQHYIGW CSFW
//
