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Database: UniProt
Entry: A0A175VZK6_9PEZI
LinkDB: A0A175VZK6_9PEZI
Original site: A0A175VZK6_9PEZI 
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
//
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