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Probable serine/threonine-protein kinase MEC1 homolog (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1 homolog)

 ATR_ENCCU               Reviewed;        1805 AA.
Q8SSE7;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
23-MAY-2018, entry version 102.
RecName: Full=Probable serine/threonine-protein kinase MEC1 homolog;
EC=2.7.11.1;
AltName: Full=ATR homolog;
AltName: Full=DNA-damage checkpoint kinase MEC1 homolog;
Name=MEC1; OrderedLocusNames=ECU02_1130;
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
Encephalitozoon.
NCBI_TaxID=284813;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GB-M1;
PubMed=11719806; DOI=10.1038/35106579;
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M.,
Weissenbach J., Vivares C.P.;
"Genome sequence and gene compaction of the eukaryote parasite
Encephalitozoon cuniculi.";
Nature 414:450-453(2001).
[2]
GENOME REANNOTATION.
STRAIN=GB-M1;
PubMed=20003517; DOI=10.1186/1471-2164-10-607;
Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
Cornman R.S., Evans J.D., Delbac F., Peyret P.;
"Identification of transcriptional signals in Encephalitozoon cuniculi
widespread among Microsporidia phylum: support for accurate structural
genome annotation.";
BMC Genomics 10:607-607(2009).
[3]
PREDICTION OF FUNCTION.
PubMed=17784954; DOI=10.1186/1471-2164-8-309;
Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P.,
Doerig C., Barton G.J.;
"The complement of protein kinases of the microsporidium
Encephalitozoon cuniculi in relation to those of Saccharomyces
cerevisiae and Schizosaccharomyces pombe.";
BMC Genomics 8:309-309(2007).
-!- FUNCTION: Serine/threonine protein kinase which activates
checkpoint signaling upon genotoxic stresses such as ionizing
radiation (IR), ultraviolet light (UV), or DNA replication
stalling, thereby acting as a DNA damage sensor. Recognizes the
substrate consensus sequence [ST]-Q. Recruited to DNA lesions in
order to initiate the DNA repair by homologous recombination.
Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites
of DNA damage, also involved in the regulation of DNA damage
response mechanism. Required for cell growth and meiotic
recombination (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to
nuclear DNA repair foci in response to DNA double strand breaks.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
{ECO:0000305}.
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EMBL; AL590442; CAD25142.2; -; Genomic_DNA.
RefSeq; NP_584638.1; NM_001040827.1.
SMR; Q8SSE7; -.
STRING; 284813.NP_584638.1; -.
PRIDE; Q8SSE7; -.
EnsemblFungi; CAD25142; CAD25142; CAD25142.
GeneID; 858628; -.
KEGG; ecu:ECU02_1130; -.
EuPathDB; MicrosporidiaDB:ECU02_1130; -.
eggNOG; KOG0890; Eukaryota.
eggNOG; COG5032; LUCA.
InParanoid; Q8SSE7; -.
KO; K06640; -.
OrthoDB; EOG092C00SN; -.
Proteomes; UP000000819; Chromosome II.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
Gene3D; 1.10.1070.11; -; 1.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
Pfam; PF02260; FATC; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
3: Inferred from homology;
ATP-binding; Chromatin regulator; Complete proteome; DNA damage;
DNA repair; Kinase; Meiosis; Nucleotide-binding; Nucleus;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 1805 Probable serine/threonine-protein kinase
MEC1 homolog.
/FTId=PRO_0000385338.
DOMAIN 955 1420 FAT.
DOMAIN 1520 1805 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 1773 1805 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00535}.
SEQUENCE 1805 AA; 209007 MW; 3D7FB94CD0F14A46 CRC64;
MNRDYLKNLY LQRLESERYS DVFRESMSSL VSTEIINAVI SLAVQDDDET MLVDLLELFL
QNLESNVVFH EKLTKSSFHL LLFKRPLGIQ SYTKLKSIYD RVGSRRVVPG FEHTEFLSKN
FYNYCLYKHA YKDYQFDLEL DAGSLGPVET NLFKDLLKAV CIENRENEHL ANYIKTLPMD
VSVFLAIVMP DFRIDASRLG PEDVFLVCPS QVRGYDPKQF TKAFLCSLNS EGGLCRVCGR
RVLGCGFEEI DREEYLDSVS GNIEEMCFGV SHWEKIRTPR MLTTILRSLF KRPGCLECYK
CLRYFPIEEQ GEMEDIVLRF LRYAASILSI GNIQVSLRMF PFIRHTPRVV FSYFVILFEG
FLKYSGNLFL KNVIRNVSTR NKAKFMGVRA MIFEYYLKGS IESASSTEEN TKNEGGSGAV
ENPGRKRADD LGDLFAPLSE FFDEERKAFV RNNMFYIYPI MYSLSFPYYT PDLAFTQANN
HFLIISLFLR GEESRIDEIG YGKDELYRMG VDVMIPLLCN GYFKYDVLSR FFGNVQEYIR
AHLPKFLFAL KKVYVERPFE FRVCVFKILK CIIEAISGNV RMLFNYLFPF VEFFMRSHEE
SCGTDCKMIF IEYYSSFFKN DCLVRNMSRI FPYLDAEKIA RWSNVKSEDD YLDIVIGLLD
TRGHFSQEMA AKKAVELLAR VFGDPGKGKG FDEESFVENV LRRFFKSREF RMKIGNVYGK
LKELGNDAAF LIGCISQEFL DANPLPSVCS VLIEECTPEA IARVMVEKYL FEMDPGKQDL
HFFIIQETLR FIKGPLSDRM EEVVEQFRST QYFYEYVPVH PVEGVYEKTY TFKRFLGRLY
RYSLNEIAKS EMQEYFSLLK YGNLLDTLFL EFHCLCLCRL LLEAGDHKVL GMVREIANNL
QEGVDKRIAR FVLKLHGFTS GKHIEDQQIL RISFFLKDHH NAIQTLEKMI RKERKSELFD
LLQYCYYSIK DYDKVLGINS VFARPSLINL FFRFCVDKNF AAARRCLEPK PGHDGVKEES
GEDHKGQAPR ELDVKILMEE IIDECQDDEV TKFMNDCKKI EGDFSEWKRL ESRNEVFKHF
IKDCELVSKS KNLLKTLDLI AGRRELAGDN RMLLECHESL VASIRSMMDA RDDMSCDEMF
ESLLTAEKQD TIGNSSQGLH SREYFDDFAS VDMVRAERRS ERIGYMDRSK SGSTSGYSSL
EEFERDLKLA IIRNYRGDDD VGRCIQEIGG MLLKREWCVL YELAELNVLQ GKIGDAKTSL
KKVLEIFPKT SMLYKKALIR YSELLDTKTA YTSALSILKD SGKLFLLGAK KFESTEPVKA
MEMYINSVIH DNQCSDEAVP RIFHLFSEMM PPGDINAGAV LLKKFLESSI SLLPPYYNQI
LSRLSHPNQD VANVVSRIVF ELMENYPSKT FWRSLIMMNS QVPSTRKRME GIVSGLTLDN
KVALSNVKRI SEELTCISRS KKNELTMEED FPAFAKMFPA GVTVPNTKVL ISGVRNEVKV
FNSLQRPKRI CFVGSDGKNY YWLCKNQDDL RKDSRFMDLN LIINSILKKQ SSRKYIRTYA
VIPFSHESGI IEWIGGLSSL KAICDTYYAR DGISISETAC RFVHNKKIGM REWHRVASKF
HPKFHLWFHD SFPHPFSWLV ARNNYTQTYA IMNIVGWFMG LGDRHAENIL FDSNTGDTVH
VDLNCIFGKG KELQVPERVP YRLTQNIVDA FGVLGLEGSY NTSLCTTLDL FLKNKNILVS
NLLSFVYDPL FEWRRKSATT PKKIIEDLWH KMDDLDACSK CDVLNEEATN DENLCMMYIG
WLPFI


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