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
//