ID A0A094DU93_9PEZI Unreviewed; 397 AA.
AC A0A094DU93;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=BRCT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V499_09697 {ECO:0000313|EMBL:KFY69849.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY69849.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY69849.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY69849.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY69849.1}.
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DR EMBL; JPKB01001788; KFY69849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DU93; -.
DR HOGENOM; CLU_019904_0_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd17742; BRCT_CHS5_like; 1.
DR CDD; cd13945; Chs5_N; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 6.20.120.50; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
FT DOMAIN 75..169
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 163..251
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 264..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43020 MW; 5C979A5FE6830814 CRC64;
MLISLTVGKV DAGVAVLLTQ DKRLIEFPSI LLPPHISSGS IVDITVARNF ESESESQDSF
SHLQDSIFRS FGESEPSAPV LRCRNATQTS IVLEWDPVQL ATADVISLSL FRNGQKAGNI
PQPTTMESTK ISGLAVDTEY TFHLVLRTTA GTFASDRLTV RTHKMTDLSG ITVTPGILPA
QLRESLVAAV ERIGGKLADT VRIDTTHFVT TEGRGITWEK AVEMNIPVVR PEWVEGCERG
GRIVGVRQYY LDADPRQRMA NLGPAAGQQA TPAEPASAKD EAPLPALPNN NRKEQANGDE
ASEAGQTNNE KEEDKDEESE EDDSEDKKVE ALDEQKVRVE DNDQHKVALR PAASPADEKE
PSVDKNPVTK SPSLEVDADT EEGAKTPGAA SFQDVAL
//
