ID B2B6R7_PODAN Unreviewed; 3875 AA.
AC B2B6R7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP73494.1};
DE SubName: Full=Transcription-associated protein similar to TRA1 of Saccharomyces cerevisiae {ECO:0000313|EMBL:CDP25895.1};
GN ORFNames=PODANS_2_8620 {ECO:0000313|EMBL:CAP73494.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73494.1};
RN [1] {ECO:0000313|EMBL:CAP73494.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP73494.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP73494.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP73494.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP25895.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (SEP-2014) 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 -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
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DR EMBL; CU640366; CAP73494.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP25895.1; -; Genomic_DNA.
DR RefSeq; XP_001911667.1; XM_001911632.1.
DR STRING; 515849.B2B6R7; -.
DR GeneID; 6196539; -.
DR KEGG; pan:PODANSg8711; -.
DR VEuPathDB; FungiDB:PODANS_2_8620; -.
DR eggNOG; KOG0889; Eukaryota.
DR HOGENOM; CLU_000129_1_0_1; -.
DR OrthoDB; 3666795at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd05163; PIKK_TRRAP; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
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; IPR046807; Tra1_central.
DR InterPro; IPR046805; Tra1_ring.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF1; TRANSFORMATION_TRANSCRIPTION DOMAIN-ASSOCIATED PROTEIN; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF20175; Tra1_central; 1.
DR Pfam; PF20206; Tra1_ring; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 2699..3254
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 3520..3845
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3842..3875
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 170..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2049..2088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3267..3344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3875 AA; 441624 MW; 08CD868332E4F808 CRC64;
MASGTFEDIV RKLSVPDIAC LAELRVKVEA ATALRDQLEH YTTGQVYPNF LKRLMPAFII
ILRSPCIFQA NTPEQANAQR LRNCVLEILH RLPTQPSPPE PFAPYAEEVV DLLMTLVRTD
NEDNAIICIK TISDIMRHQH AVLGSKVQTF LSLIQDLFEQ LDRVVREQID NTSSTGPPGA
PSTPGSTQAA FPPHQQSPRP GSPVATGGPP DFNADANQQS NRPLLKGMQS FKVLSECPII
VVSIFQVYRN TVAQNVKAFV PLIKSALSCQ AKAQDQAHKD AAARGTIHTG VSPNIKNRAA
FGDFITAQVK TMSFLAYLLR QYSQQLTDFL PSLPDIVVRL LKDCPREKSS ARKELLVAIR
HIINFNFRKI FLPKIDELLE ERTLIGDGLT VHETMRPLAY SMLADLIHHV RESLTPEQIR
KTVEVYTRNL QDNFPGTSFQ TMSAKLLLNM AECIARLPNK VDARHYLIMI LNAIGDKFAA
MNRQYHNAVK LSKLYALQTA GLFPETYLAD KKHPPEWDEI DIFTAMPIKT TNPRDRAADP
VVDNKFLFKN LMNGLKNTVY QLKSCNPQGS VDLTGAPHPW AEVAHGFTAE EVKVIIKLFR
EGAYVFRYYE IEKPVTESLY SSPVEFMANF YMVSSGKEEK DLLETFATVF HCIDAATFHE
VFQQEIPRLY EMMHEHTALL HIPQFFLASE ATSPSFCGML LRFLMERIED VGSADIKKSA
ILLRLFKLAF MAVTLFASSN EQVLLPHVVD IVTKSIELST KAEEPMNYFF LLRSLFRSIG
GGKFEHLYKQ ILPLLEMLLD VLNNLLLAAR KPSERDLYVE LCLTVPARLS NLLPHLSYLM
RPLVVALRAG TDLVGQGLRT LELCVDNLTA DYLDPIMAPV IDDLMTALFD HLKPHPYSHF
HAHTTLRILG KLGGRNRKFM TDALPVTFEQ YVDDRASFDV RLIGSKRDRA FPAHLGIDLA
VQKLMETPKP GKGLSSVAAK QYDAYYKKQA LSLITAQVKL RIGFDNLPDD LPRLVRLQAQ
DLVKRNRAVD ISAFETTDRE RSIVKKNEEE ALLKRLIKAL VFAESIPAFK SEVDGFLMNL
ARHFTIVEVG RALVDMKRLV SPFDHKAGEG PLFLESRVFS DAILDSLASE NPEIREAAER
MIKEVYNSAL TIFNDAKNVS RLAFFNTLAS AFCHGCYEEE WFTKTGGTLG IKYLLNDIDL
GDQWVVSKQM DLVRALMYVI KDMPQDLSEK TRRSAQVTLE MLLTRLTKGI KKSDCFHQQP
PTPAAGQQPQ PPTPQSQVNP KFARIPNIIV MLNGELSHMN RHVRETARRS LELIAKAAGA
EVWELLEPNK AQLLRPIFNK PLRALPFAIQ IGFVDAVSYY MSLKKDFVPF DSDLNRLLME
SLALADASDD SLAQKALEFR TQHFIVNLRV SCIKILSSAM SFDEFGQGQN NPTRGKVVGV
FFKCLYSDSQ PTIEAANNAL RSVLQHTTKL PKDLLQSGLR PVLASLQDAK RLTVHSLENL
ARLLRLLTTY FKVEIGSRLL DHIKQIADPA FLQEASFTFF EQQQSMKVIA AVFNIFHLLP
DAARHFKERV VDNVLDLEEK LRRTHLSPFR VPLYRYLNKY ATDVWAMFIG KLDELKYGRF
MSQALRHPDS QELRAWGAAN VDTIMKRCIT AGQQNKDNKF VAIVNTINLL DALCQFPSSN
LMYWLDGKER IDWLKQVGKE LERSLKNNSL PPYLRLPADQ ASEQLMSILT KALERKPEDL
EPLLSLIESV TADDFRETQV LLSHIYKHII CSNSIDFWRA VVLRCLDIYA GRTASQRTKW
YLIHNIVNPI LAMDVMRHWP NKTTGPKFLD KSVIDSINTK IWRANPTGPH DDLSQPRIDH
TRMEVLQLSA MLVKYHSGML ESFRKDFIKF GWTYIRLDDV INKHAAYVVI GYFIAHYETP
VKIVTQIYSS LLKTNQNEGR SLVTQALELM APVMPKHCAV SPGDRNPPWA MAPRRILAEE
SQNAQQIACI FQFLVRHPTL FYDSRDKFAM VIIQCLRKVA SPPNPSNESK KLALNMMWLI
WEWEKQRVEG KPTEPPRALS ESPNTKKRRL EDATGSSPSA TRQPERGEYQ IPALARQKMI
KYLVEFIAQL NERYPLPSAR PHAAATPSLP APAPPSTDLC CKALTLLYNL LQPQYWGDLE
VDLFPNVTDL VLVSDKAVAV LTAEPSGDKE SPKFDDKFTT NIINTLQVVR TILNFKSDDW
IQKNMTQIQR ILEKCLKCEN PEIQDCLHYD DGGYHGDLDI KPIVKRILDA VPEDVPMEDA
DADGETEAQT SEIITFLSNI ATESMNAGNY VSGINILWSL GRRRPESIDQ HIPAIMKSLQ
AKLARDHVSH YAFVAQTTTG TRPADGQSSA TEMKPYDLQV QTCLILKAIE VTALRMDILG
DNRRPFLSVL ATLVEKSLHV ELCEKILEMV EGWVFRSEGT WPSLKEKTAV LHKMVTFEHR
QDPKLLMKFL DLVIRIYEDP KITRTELTVR LEHAFLIGTR AQDVEMRNKF MSIFDKSLSK
TASTRLAYVI LNQNWETLGE SYWLAQASQL LLGGVDMNPT IQLQSDDFRT LPLSALAGVY
AKDSREPELI PDDKYEAFMA GHRRFISEIG DVRVRDVLEP ITQLQHIDPK LSDQLWVALF
PMFWSATAKE DRADLERGMV TLLTKDYHSR QIDKRPNVVQ SLMNAAVRTW PDCKIPPHVL
KFTAKTYDAW YTALYQLEKA AIKPEIDSVA VRESNLDALV ELYASLGEED LFYGTWRRRC
QFVESNAALS YEQHGMWEKA QRMYENAQIK ARTGVVPFSE SEYMLWEDQW VICAQKLQQW
DVLQDFAKHE NFQDLVLECA WRSQEYWQNA ENREGLDTII AGVMDAPTPR RAFFRAFMSL
IKFYHKQESL QDFNRHVDEA IQLSIRKWHQ LPERLTAAHI PVLQNFQQLV ELHDASIICT
SLANTTQQNL DVKSGELKLL LTTWRDRLPN TWDDIVAWHD LVTWRQHIFG LINNTYLQLV
PAQGQNAGGA SYAYRGYHET AWIINRFAHV ARKHALPDVC VTQLTRIYTL PNIEIQEAFL
KLREQAKCHY QNADELTNGL DVINNTNLNY FNTTQKAEFY TLKGMFQEKL GQKEEADGSY
GTALYYDITA AKAWAEWGYF NDRKFKDNPA DLSTAKQAVT SYLQAASSYK NYKSRKLVAR
ILWLLSLDDA NGTIAGGFDD FKGDIHVWWW ITFVPQLLNG ISHKEAPRVF AILIKIAKTF
PQALYFQLRT SKEDYLAIKK AQENKARQRS QQAAAAAANK PNGSPAVAKQ EAGAAGAKTE
GADGSRPATA NGDANQVKTE PKEAGNPNNA APVPAEQQAG HKKQPWELTE DIMSVLKTAF
PLLALSMETM VDMIQKHFKC PPDDDAYRLI VALFNDSLSY VSRSPQLYAR EVKLPQATES
NIIKFAETIL PAHIRSSFEA DFVRVKPTMY EYIHKLRKWR DKFEEKLDRR QTPQPLESFA
HYSPHLSEFR YQKFDDVEVP GQYLQHKDKN QDFIRIERFL PNVDLVRNTG STHRRLKIRG
HDGSMHAFMV QHPAHRQCRR EERVLQLFRQ LNQTLASKKE SRRRDLQFTL PLMIPIAPTF
RLVQEDTSWI SLQAIYEDHC RRNSISKDEP IMYTMEKLRA LMDNKGGQKQ EQLNTARLEV
MRAIQEKYVD HTIALEYFQL AYPDFSEFWL FRRRFAYQLA ALTFMTYTLH IDKRYPNKFN
ISRKTGNIWG SELLSQIAQN RPIFYHSEHV PFRLTPNMQT LMGPLATEGI FAASIMAIAR
CLTEPQFQLE HALTLYVRDE MMFWFTSNRT TGLTETQLRE TVQANCDIVV KKAVSLAQAP
AANLPAHQTV IDLISKAVNP VSLAVTLDPL WMPWL
//
