ID   ATR_ENCCU               Reviewed;        1805 AA.
AC   Q8SSE7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable serine/threonine-protein kinase MEC1 homolog;
DE            EC=2.7.11.1;
DE   AltName: Full=ATR homolog;
DE   AltName: Full=DNA-damage checkpoint kinase MEC1 homolog;
GN   Name=MEC1; OrderedLocusNames=ECU02_1130;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
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. Recruited to DNA lesions in order to initiate the DNA repair by
CC       homologous recombination. Phosphorylates histone H2A to form H2AS128ph
CC       (gamma-H2A) at sites of DNA damage, also involved in the regulation of
CC       DNA damage response mechanism. Required for cell growth and meiotic
CC       recombination (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear
CC       DNA repair foci in response to DNA double strand breaks. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
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; AL590442; CAD25142.2; -; Genomic_DNA.
DR   RefSeq; NP_584638.1; NM_001040827.1.
DR   AlphaFoldDB; Q8SSE7; -.
DR   SMR; Q8SSE7; -.
DR   STRING; 284813.Q8SSE7; -.
DR   PRIDE; Q8SSE7; -.
DR   GeneID; 858628; -.
DR   KEGG; ecu:ECU02_1130; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_1130; -.
DR   HOGENOM; CLU_241340_0_0_1; -.
DR   InParanoid; Q8SSE7; -.
DR   OrthoDB; 37330at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR014009; PIK_FAT.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromatin regulator; DNA damage; DNA repair; Kinase; Meiosis;
KW   Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1805
FT                   /note="Probable serine/threonine-protein kinase MEC1
FT                   homolog"
FT                   /id="PRO_0000385338"
FT   DOMAIN          928..1420
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          1494..1793
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          1773..1805
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          406..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1500..1506
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1660..1668
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1680..1704
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ   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