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Database: UniProt
Entry: A0A1J9PTH4_9EURO
LinkDB: A0A1J9PTH4_9EURO
Original site: A0A1J9PTH4_9EURO 
ID   A0A1J9PTH4_9EURO        Unreviewed;      1507 AA.
AC   A0A1J9PTH4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   02-APR-2025, entry version 26.
DE   RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN   ORFNames=AJ78_00815 {ECO:0000313|EMBL:OJD19202.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD19202.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD19202.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD19202.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OJD19202.1}.
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DR   EMBL; LGRN01000015; OJD19202.1; -; Genomic_DNA.
DR   STRING; 1447872.A0A1J9PTH4; -.
DR   VEuPathDB; FungiDB:AJ78_00815; -.
DR   OrthoDB; 129353at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:TreeGrafter.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR   CDD; cd17745; BRCT_p53bp1_rpt1; 1.
DR   FunFam; 3.40.50.10190:FF:000083; DNA damage repair protein (Rad9); 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR047249; BRCT_p53bp1-like_rpt1.
DR   InterPro; IPR041297; Crb2_Tudor.
DR   InterPro; IPR047252; TP53BP1-like.
DR   PANTHER; PTHR15321:SF3; TP53-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR15321; TUMOR SUPPRESSOR P53-BINDING PROTEIN 1; 1.
DR   Pfam; PF18115; Tudor_3; 1.
DR   SMART; SM00384; AT_hook; 3.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182235}.
FT   DOMAIN          1171..1302
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          37..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..351
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..399
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..513
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..563
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..954
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1453
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1507 AA;  164088 MW;  61C8F50B63FBD3E8 CRC64;
     METQDDSLDL DYLKQAALGM ANEQFKLDVS KSLQLQGFHH ASPKQSHDPT HLNTTDYSSD
     PESPTKKMAT ATGSLPSDTQ PISQSALESF LSKARINQAG PKDQESKDDD DLMARDATLH
     EGDTGHLDLL AAFGETPVAN REFVDEDEQL EDLDMVGGVS SPTQYQHFPE SQRFINRTPA
     TQNRRSSQSE LSTTQILPSF PLSMECQNGS TVMALSQVFN ATQNPSSPFT NGPPLSSDMP
     SPNLPVEPRL TGMPTTIFSP LLPSPITRLK YLEPQTNYVS MKESQAVREK MARLHSTNEN
     GFSDDDFEKD DSYVRRHVRE KYTEEEVRKQ FANVTAPPRP SSKGHGKRRA TNHSSPEPTE
     PRNGRPRGRA LSTAIEVGIL ERHNSGNSEE ETEQEDELEV SQNQRLLPCQ LSGDDDKENV
     DSGPVHVADT TASAHDALSQ VLELYSSASH QTYIKDVSGS GSGSQEPVNQ AQSTPRKNGS
     NTRAGSQIVN IANSQPSSDS GQKRRRGRPR KVITHSAHSP DEECIPSSPV CASHRQRSFP
     PNPQVLNHSS KRGRGRPRSR KANKTLGQSP EEECIPSSPI YGPYEQGSTP KQPALVGRDT
     SESTCHVHHS AADATLETSH QRLSQQGRSD EEVAEAVESP NDQEDHPETG AKISDNPSTE
     ETAGAAKASS MPSRVLETPT QNQKPSKGFH QIIPQTSPSD HRNSPSTHFS KSVPPFNNNS
     SASPTHDDDQ LPVVPQFSRV PGGHLGVPDL LPSGGPQRTI PAVLSSPSGR QRRSMTEIAA
     EQSPCQSLPE FLPDFGLISA EDKEFAFITR EVGPRSQKRR RGNDGRAISS SNLLDRDQTP
     TPEEPPAAPQ PGIAVSGPMN DVSEPATPGP VQHAQMDAIP IQNRRQAKSA ANIWEVECSP
     VQPAKQVRKG PKPRLNHPLE PAVFRPRTSQ HLRHSIAGPI KTQTSKSPSP TPTQLIDRAE
     SPDPIQSEET HAHSKLGCVS PSLNNPVLAN KVFAFFNGRP QGYFPATCVG ISRSANAIRY
     LVRFEDSIKP DEVNVDAVKR LELIVNDVVK VDLLQVPKIP HTVVGFPKPN EVPAFSSGEA
     APFLTMTDVH GHHSVILRPK GPNGSFRNGP DITVPISNVY FDRILWTRLE NRHYSYSPPP
     LSTSVSGLQT SLDHRPSSAL STSRTPHQFP SVSGLFFGMA FAVSYKDDEE KRVRIEELII
     QRGGRILKDG FTELFNQPLS NIPSAPFDKS SVATSSADNN DELLSLRPTA QNTGFVCLLT
     DEHTRRVKYM QALALNIPCL AGRWIYDCIA KDQIVDWEPY LLPAGESAFL NGAIRSRAIA
     PNPVPTARLQ NTIAARPKLL AGQSVLLVMD RGKIAEQRKP YSFLTCALGP SRIACVQDMN
     AAIKILVTSE RESPVSTADS DVGWDWIYVG DEKAAAAARA QLLKASQSGS PKGTSTGRPR
     GRPPKKSQSR GRPAKGATVV AAAAAGLVDG VCCPIGGSDV CINGKRVRIL DNEFICQSLI
     LGKLFEP
//
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