ID A0A165JL20_EXIGL Unreviewed; 796 AA.
AC A0A165JL20;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN ORFNames=EXIGLDRAFT_834572 {ECO:0000313|EMBL:KZV95002.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95002.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV95002.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95002.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV425964; KZV95002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165JL20; -.
DR STRING; 1314781.A0A165JL20; -.
DR InParanoid; A0A165JL20; -.
DR OrthoDB; 20296at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR CDD; cd00027; BRCT; 2.
DR CDD; cd17731; BRCT_TopBP1_rpt2_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 4.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR PANTHER; PTHR13561; DNA REPLICATION REGULATOR DPB11-RELATED; 1.
DR PANTHER; PTHR13561:SF20; DNA TOPOISOMERASE 2-BINDING PROTEIN 1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR SMART; SM00292; BRCT; 3.
DR SUPFAM; SSF52113; BRCT domain; 3.
DR PROSITE; PS50172; BRCT; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 47..119
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 138..237
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 510..560
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 85345 MW; 6E2B8BE2355660D4 CRC64;
MRKGHGSTKV PGVKLRPPPK TLAARSIDTA ADDDHDSVST GTTSQLNSSG PFVGVVVCAT
GVTNKSQLFN QAKQLGAASS THFTNLTTHL VAEEAGSAKY LCALERGIPI MSPEWVRESH
AIWVSGGEVD FEESVAKHRL PIFLNVKLCL TGFEDVQERL RLHQLVAKNG GVYSKGFEPS
VTHLLVCGDS AESIKTQTAL KLNKTRAREN QIHVIWEEWL WDSVEYQGMW DPAQYSFENP
RPQRKPPKPT TPSVDDAPKR TVAPLPPSIK NDLLISAQDP SEQARTRHIP GISSHMWQSI
LRARGGVDKI RASLQQHSTD ELPAFKGAVI SRVSSAKAAA LQSSSAAKPT TTSARQPFSR
VASAAVPGSS RQLAPLRATA SLVASLPSTS SDSQHRTFLG KSFFALGSAN CDALAAAVQD
NGGVWATCDE SADFVLVRLT ESALFWAEYD DNDGRGRTEC WMEKCLYDER IVGAGEHLTF
VPLRNPGPLP DADKLSICFS GLGSAEGCWI KRLLRAIGAN YLPAFSRKCT HLICDSGEGQ
KCERAREWDI PIVGTAWLFD LATGDNVPTQ RTGSQPAPAM ADITNAGASA GFSSLTFDAP
SETHFFDDAP TPATSLGRPS LLIPNATSSK DAVDTPVVPS SCTPSPMKFA SPHPGAESVT
ITTTTTGKRT RSDDRDSEAR SQSVKKARPG SRSKIALERG SSVVSMRSES APATTSAGAD
DVAMLNGTQE ESMVVRYMDT EGEVHRSALL RAISAPEEVI PSSKKAKSKK EVATSGRAVQ
VAADGGRRQS RRMAGF
//