ID C6HHH4_AJECH Unreviewed; 2377 AA.
AC C6HHH4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=HCDG_05655 {ECO:0000313|EMBL:EER40258.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER40258.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; GG692427; EER40258.1; -; Genomic_DNA.
DR STRING; 544712.C6HHH4; -.
DR VEuPathDB; FungiDB:HCDG_05655; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OMA; MRQHSAK; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF13513; HEAT_EZ; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 986..1026
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1242..1811
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1985..2304
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2345..2377
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2377 AA; 268255 MW; 59EA5354B03AD138 CRC64;
MAQAASGTDA AQRIFHELKS KNEETRSRAS YELHDNVIAV SRELPPDKFI EYYNAVSQRI
AQLVVTGNDA NEKIGGLLAL DRLIDFDGVD AAQKTTRFAS YLRSALRSND NAVLIYAARS
LGRLAKPGGA LTAELVESEI QSALEWLQSE RQENRRFAAV LVIRELAKGS PTLLYGFVPQ
IFELIWVALR DPKVLIRETS AEAVSECFEI LAARDVQVRQ QWFGRIYEES LQGLRSSNVD
WIHGSLLTLK ELLLKGAMFM NEHYRNACEI VLRLKDHRDP KIRTQIVLTI PILASYAPLE
FTNVYLHRFM IYLQAQLKRD KERNAAFIAI GKIANAVGNS IGQFLDGIIV YIREGLTMKA
RNRAAVNEGP MFECISMLSL AVGQTLSKYM EALLDPIFAC GLSESLTQAL VDMAHYIPPI
KATIQEKLLD MLSIVLSGSP FRPLGCPENR PPPMPSFAKD YGAFLQEPTD SEIALALHTL
GSFDFSGHIL NEFVRDVAIN FVHRDNPEIR KASALTCCQL FVHDPIINQT SSHSIQVVSE
GIGTLLSEGV GDPDPDVRRI VLESLDRKFD RHLAKPENVR CLFLAVNDEV FSVREAAISI
IGRLSSVNPA YVFPPLRKLL VNLLTGLSFA TTSRQKEESA QLISLFVANA TKLVRSYVDP
MVKALFPKTT DPNAGVASTT LKAIGELATV GGEDMKQYLP QLMPIILEAL QDLSSQSKRE
AALRTLGQLA SNAGYVIEPY IEYPNLLAVL INIIKTEQTG SLRKETIKLL GILGALDPYK
HQQIIESSPD IHHVNEVQTV SDVSLIMQGL TPSNDEYYPT VVINTLLQNI LNESSLSQYH
SAVIDAIVTI FKTLGLKCVP FLGQIIPSFL SVIRSTPTSR LESYFNQLAI IVTIVRQHIR
AFLPEIIEVI REFWDCSYQV QATILSLVEA IAKSLEGEFK KYLAGLIPLM LDTLEKDNTP
RRQPSERILH TFLIFGPSGE EYMHLIVPAI VRLFDKNQGP PGIRKSAIET LGKLSRQVNV
SDFASLMIHP LSRVIAGSDR TLRQTALDCI CTLIFQLGQD FNNYIQLMNK IIQTHQINHH
NYQVLVSKLQ KGDPLPQDLN PDEHYGALGD DATFADVGQK KILVNQQHLK NAWDASQKST
REDWQEWIRR FSVELLKESP SHALRACASL AGIYQPLAKD LFNAAFVSCW TELYGQYQEE
LVRSIDMALT SQNIPPEILQ ILLNLAEFME HDDKALHIDI RTLGKYAGKC HAFAKALHYK
ELEFEQDQNS GAVEALISIN NQLQQSDAAI GILRKAQAYR DVELKETWFV KLQRWEEALA
AYKRRELIDP DSFDVTMGKM RCLHALGEWK MLSDLAQEKW NQASNEHRKA MAPLAAGAAW
GRGQWELMDS YIGVMKEQTP DRSFFGAILA IHRNQFDEAA MFIEKARNGL DTELSALLGE
SYNRAYNVVV RVQMLAELEE IITYKQNAGD PEKQEAMKET WNKRLLGCQQ NVEVWQRMLK
VRALVVCPRE NLDMWIKFAN LCRKSNRMGL ADRSLSALES GEGSDQPTPP EVIYARLKYD
WTAGRQKEAL QMLREFTVGL TEEFSRYSSV LIAHGEHASS DRPGLVNGII DHPDLATARQ
HIGEMGKFRR LLAKSYLKQG EWQTALQKGD WTSEGVRDVL NSYSAATQYN LDSYKAWHAW
ALTNFEVVNA LSAQTNRETF VPHHIVLEHV IPAIRGFFRS ISLSSTSSLQ DTLRLLTLWF
NHGGDAEVSG VVTEGFSSVS VDTWLEVTPQ LIARINQPNA RVRGSVHRLL AEVGKAHPQA
LVYPLTVATK SNVVRRSQSA THIMDSMRQH SPRLVEQAEI VSHELIRVAV LWHELWHEGL
EEASRLYFGD HNVEGMFATL APLHDMLDKG AETLREVSFA QAFGRDLAEA KHFCILYRES
GVIGDLNQAW DLYYTVFRKI ARQLPQLSTL DLKYVSPKLK DAVDLELAVP GTYQSGKPVI
RIMSFDPVST VMQTKKRPRK MTLKGSDGNS YMYVLKGHED IRQDERVMQL FGLVNTLLDH
DSESFKRHLT IQRFPAIPLS QNSGLIGWVC NTDTLHALIK EYRESRRILV NIEHRIMLQM
APDYDNLTLM QKVEVFGYAM DNTTGKDLYR VLWLKSKSSE SWLERRTNYT RSLGVMSMVG
YILGLGDRHP SNLLLDRITG KIVHIDFGDC FEIAMHREKY PERVPFRLTR MLTFAMEVSN
IEGSYHITCE AVMRVIRENK ESLMAVLEAF IHDPLINWRL GARESPARPS FPTDRRQAIA
DEISVEHPVQ PSNFSRRRPS ILEGGILDAQ QGVPNEAREV QNARALQVLS RVKEKLTGRD
FKSTEELNVS DQVDKLLVQA TSVENLCQHY IGWCSFW
//
