ATR_ASHGO
ID ATR_ASHGO Reviewed; 2324 AA.
AC Q75DB8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine/threonine-protein kinase MEC1;
DE EC=2.7.11.1;
DE AltName: Full=ATR homolog;
DE AltName: Full=DNA-damage checkpoint kinase MEC1;
DE AltName: Full=Mitosis entry checkpoint protein 1;
GN Name=MEC1; OrderedLocusNames=ABR108C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 609; 628; 983; 1610-1622;
RP 1630 AND 1642-1647.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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. 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}.
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DR EMBL; AE016815; AAS50879.2; -; Genomic_DNA.
DR RefSeq; NP_983055.2; NM_208408.2.
DR AlphaFoldDB; Q75DB8; -.
DR SMR; Q75DB8; -.
DR STRING; 33169.AAS50879; -.
DR PRIDE; Q75DB8; -.
DR EnsemblFungi; AAS50879; AAS50879; AGOS_ABR108C.
DR GeneID; 4619161; -.
DR KEGG; ago:AGOS_ABR108C; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_0_1; -.
DR InParanoid; Q75DB8; -.
DR OMA; YETMHEI; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0070310; C:ATR-ATRIP complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:EnsemblFungi.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IEA:EnsemblFungi.
DR GO; GO:2000105; P:positive regulation of DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 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; Chromatin regulator; DNA damage; DNA repair; Kinase; Meiosis;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2324
FT /note="Serine/threonine-protein kinase MEC1"
FT /id="PRO_0000227708"
FT DOMAIN 1349..1901
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2005..2308
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2292..2324
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2011..2017
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2177..2185
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2197..2221
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2324 AA; 266385 MW; 1908F70242808242 CRC64;
MDGQTRYLDE LVGALRAERA QGRAGGYAGE FPPREGGGRA RRVARTVVAK LADAEVADAA
FWRACEALDL VFTGRPMVLA EALDEEAGVL WAVRSCWRVA AVHFGRRERG WALRRASSRW
VRLCADLYGQ RWRARVGAEL DRELCAGEAA VRAVLGGGQE AGEHMRALRA LCVAAEWAVS
REFWFVTGGA ERVGLRLQRL ARLARYIGDA VELPLAEYEE VQVRLLGVSV QAYLEPDRPG
LGELRFALEQ LQYFVRGKHL RREFAAWSRL LLRLYVRCRS DRAALLLVRE VLVLDAAELP
EAATDAQRSL QLVRYDLERQ FAADHALRWD PALRAKLLAA GTPPVILEPF TSNRQLEKLR
LRVLCDFQVG DSALLVHQFS AAGVPLGADP VALYTHLDEG IARAFGRQDT EAQVRYLSLV
RKLACLESRK PSPGFDCDLC DHTNLWLPRE SIDPSRPEAA SDSLAFKLLV GYYLREQLES
SGEALVIGIL ITLRSIFTHF QPPKLVENHY GDMVDEHGCI QLFRMAFMSL NRHVRILSVL
LIPYWNLSRS YNADEQQTAL IIKFLQRNPD PHITETYLMA WTQLTLSTSG ELFDSLLLKL
IDIFNSSNFV EHVVMASQLK FIARVLNKTA YQLLSPILPI LLKQIGKNLG EKKLSLERLL
NLLEYSAKTV IENFQRYIVP YALTQYKGDA LTEIAKIMCQ NNEPSMVSEQ KKRLLDRNSR
QIFAVALVKH GLFSLETIET LFINNDPTFD RSYVAGFLPD YKTLAEVLKL FKPVEKVDSP
MNDNERAVLS SLRFLFLTNF SVDKHRGSKF KNVTEWTQEK EAVFQKKLKD NILGIFQVFS
SDMHDIEGKT TYFEKLRVIS GISFLIKYAS KECIISALAQ VSICLQTGLE IPEMRYNTLR
CWLHLVKYLS EEELSTVIDV LICFILQKWD EFSGKIQQAA IDILDALILE KQTLLTNSRP
YIVLAFLNKS ELHIFENHGF FARTASKLLK NTNWVSVFVS NLKSHNIYVI KQTLQDIRLF
LEKKQDAGID IKLISKDGKN ISELLGALLD TSHKYRNSDL IICETCALCI SMIGVLDVTK
HELQRCNVYD NDICDFNNPT QTTKFLINII NERLVPSFWQ SENPTKQLFV ALVIQESLKY
CGLSASSWDV TKPDLYPNES KLWNRFNDIS KTTLYPLLSS LYLAQSWKEY VPLSYPSFKV
KDGYSTWIKN LSLDLLKTAT ESSHPLHVFS SLIREDDGTL SDYLLPYIIM DIIIKAESGT
KYFDYLQNVI KDFEYIFNYT LYDLNHYQID GLKMCYDSIF RVFEYCKKWV NQFRQNYSKQ
HGTFTIREEK YTRMLNRAGK FADIIPSHVL AQKSLETNSF ERSALYLEQS YREKSSNGLQ
DDKLLPYLQT TYAEINDIDA VVGVLKVFCS NNLTSRIEEL QYSDNWKMAQ DCFDALGDSL
LNEQGGVENS VPTSRMLKLM YDHQLYDQTL KKLELNIPSK KRQLPLNLDE FYNMGIETAS
LSGNITELKI WIRRIEQLET LTDPSILLHY NLAKSLLAVL EGKTDMIETH SKYCYRLIGS
HFTTPSHSTT LLKRRNLFIK LHGIRDNSIL SKCSTDIQFN RSVRNLAVRF KNVGSDFEPN
FYLLSMRKSH NLMRSEEFVK QDLADTYFKM AQLARENDRL DIASDCLMHA LKLEHTEAEL
EYAEILWKQG EKELALKTVA EIHQKRKGIK TLKDRDRAKV LLKYTEWLDL SNNATSVQIS
HQYKEVIGLD KDWDEPYYSF GLYYSRLLEK KRADGFVTTG SLEYKAITYF LSAFEKNTVK
VREALPKVIT FWLDTASRSV ESGSSEGEYH FKRYTKEICK CIDVAIQNCP THIWYTVLTQ
LLSRLLHKHT DSATLIMNIL LKLTLEYPSI MLWYITVLLN SQENKRVHAG KQIMDAIKKR
MPDKSSLISS AISLVQAMTR VCIKDVKNMS SRSGKSLQND FKFDINLAPS EMVVPVNINL
ANLSPSYADT SGKHGSSKRV TINCFTPHYK VYSSLKKPKK INIIGSDGEL YGIMCKKEDV
RQDNQYMQFA NMMVFLLGKD SESRRRSLNI TTYAILSLRE DCGLIEIVPN VDTIRSILMA
KYDSMKIKYT LSVLYEKWKS VSEEQRLGFY KSCTDTFPPV LYQWFLETFP NPIRWYNARN
AFVRSYAVMA MVGHILGLGD RHLENILLDL QTGKVLHVDF DCLFEKGKTL PVPEIVPFRL
TQNIQDAFGV TGTEGTFKKS SEVTVRVMRN NELALVNIIE TIMYDRNMDH SIQNALRVLR
NKVRGIDPRD DLPLSVPGQV DTVVQQASSD ENLAQMYIGW LPFW
