ID A0A175VZK6_9PEZI Unreviewed; 2439 AA.
AC A0A175VZK6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=MMYC01_206522 {ECO:0000313|EMBL:KXX76695.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX76695.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX76695.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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:KXX76695.1}.
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DR EMBL; LCTW02000198; KXX76695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VZK6; -.
DR STRING; 100816.A0A175VZK6; -.
DR VEuPathDB; FungiDB:MMYC01_206522; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000078237; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF69; SERINE/THREONINE-PROTEIN KINASE ATR; 1.
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; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Kinase {ECO:0000313|EMBL:KXX76695.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Transferase {ECO:0000313|EMBL:KXX76695.1}.
FT DOMAIN 1423..1990
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2104..2410
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2407..2439
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2439 AA; 274085 MW; 6E0035E232F7B7B2 CRC64;
MASESHGKAV RPGRHDLNNS VGGPPPSTLA AQLVENVSTS SRSSRPDETT ELKRLSAVIE
KVKNDPGCLK THEERVEHNH LLVYVCGGVF LESLKLDDAF ADGERLRAEA LKAINFLRVT
IAETPAVLKC TTDGKAFLSR GKEPLWLWIL PKLLRMLGHR RCLAISAEIE GLCQDVLLLT
SRNASLWDLG PSLIQYFQAN LGAILTQLKS AVPSTRETST EIRLPPKTFL EVVSDTVPSG
CSFNLSDDEY AIRHAASLLT ILKNTILSKN DSQAFFSYDQ NLVWLLDTIQ PLSSILATWP
VPLEVGLATL VQIALDLAKA HISSRGTKSI LNHKANASLA LVCTDVFRDP SQFLAGNEDG
SRLRRIVCLA LIHLAQASVN HEPTSRLIAS AFLASALRLV SENPIVGAGT DVWRSVHLLH
LATTAPSDLA LDENIAPALF VDGVMRRQVQ KLVSRLENDK SSGPAPKRRK LNDEPSELLE
LAARLCRMVD ADPSSQVENL ESHITERFPE MGEDDQCQII DLISRIPCAA DDTLRFKRTE
QGSPAHFQCS FCSGPTLSVS APNCQHEEGK ALGITLFSSV IKLPSFLESR RPRVFAMIVL
RRIARHSTDN EFWDLEKSGP GLWCLQSLQS SIRELRIAAG RALSVFITEP AATKFDGDIL
KRNRTNALGI LKSVSDKESP RLHETCIMAW GQVGRVVSAD ELNLVVLKLV EYLGHGNMIV
PSLAFNEILN LADSRGETPG RLLQPFWASL AFSVVKDLVS KPQTAGRVAE LLQMSVPDLL
RMLQKYALPW LVLTKKREVI QKIAEARGED ETWQPCLDAA NLPSILALLL VQDTSDIVGH
AMSLLSHVSP HFEASELVEL LRTDPLMIAL ELFKAGAEAN EARKARVRAA LNTMASLLLA
DQKDKRTKKS HMVGRYLQQH ALGLAARLSE VINDTLLLRP PVAEQKQCLG AMEEMIRICN
SYVCIARPQI SACLISAMAS DELRSAAFSC WEVMLVEMEE ADVEAQIETT FFIIGYYWQS
FDETTRRKAK NLISTLLNKY QRIVVDYSHR LPSLSHIDEL ADLCKALDNL CTPLDNRDTF
AVFAQRLKHE NPGVVEQALV ELVAFLEKNQ DYLQTSAISE HPDSVVTTLA RALLDCSAKY
NGWQLDITRL CAQAIGLIGC LDSNRLETAR GQKQFVVIHN FEDAREATDF VAFLLENVLV
EAFLSTTDTK FQGFLSYAMQ ELLGRTDFKF ACTSQGQVTH EAIYRKWLAF SENTREVLTP
FLSSRFIVAP MQQQTTEYPI FRPGRSYAFW IRALVHDLLR NGQNLFSQAI FEPLCRLIKV
KDLAVTEFLL PYVVLHVIVG QEHVDDFRNK ISAELVAILK HQPPETASYV EKEDTKLYYQ
AVFRIIDYCM RWVQLKKSHG LNSRNQKWIK WVEGVVGALD PELISQRAVD CNEYARALFF
LEPHLESREK RAGKEENDRI MQSLQNIYTQ IDDPDGLEGV SAHLQHVTLD QQALNHRKAG
RWTAAQTWYE IRLAESPENA DIQLDLLTCL KESGQHDVLL NYVEGMKRTV NTVNRIAPFA
VEASWATGRW QTLEKYLGMY NGGDVSEVFD LGIGQALLYL RDGNMEKFKE HVQMMRDKVA
GSMTYAATSS LRACHDAMLR CHVLSDLEMI ANEKLKGDGD QQAVLRTLDR RLEVLGAYVS
DKQYLLGVRR AAMELMRPKF GNEDISSQWL SSARLARKSG SMHQSFNAVL HAQQLGDGSA
IIENARLLYK DGHHRKAIQV LQLAITTNSF ITANTSSIPP TSSKNPDSQR NLLTARAHLL
LAKWLDSTGQ THASALRSQY QQAAKTYPQW EKGHYYLGRH YKKVLESEQT LKPDDQTDEY
LSGETAKLVI ENYLRSLNFG TKYLSQTLPR ILTLFLELGA QVDKAPDGKV SLSRELHIRR
KTILTELCKH FKKHIPRMPA YIFYTVLPQI VARIAHSNPE VFNVLEEMIL KVVEAHPRQA
LWSLFPLMTT RQASERRTRG FRILQAARGM SKKVDGSSYD LKQLLRMGEK LAEQLLLACN
NGDFQSNRTT TASITRDLNF NHKCTPCPLV VPIEACLTAT LPTLTDNVRK HKAFSRDVIT
IDSFLDQVLV LGSLAKPRKL TARGSDGNLY GLLIKPKDDL RTDQRLMEFN GLINRSLKRD
AESSRRQLYI KTYAVTPLNE ECGIIEWVDG LKTLRDILLG IYKTRNIQPN YSEIMQKMKQ
ATLSDDNIRL FTEDVLGMFP PVLPDWFIAQ FPNPSAWFAA RLKYTRSCAV MSMVGTILGL
GDRHGENVLL EEGNGGIFHV DFNCLFDKGL TFAQPERVPF RLTHNMEAAM GIYRYEGPFR
HCSELTLRVL RQQEETLMTI LEAFIYDPTL DLQKPKKRHY EVVMLNPTSV LESIRRKVRG
LLPDESIPLG VEGQVEELIK QAVNPKNLAA MYIGWCPFL
//