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Database: UniProt
Entry: A0A397ISY5_9GLOM
LinkDB: A0A397ISY5_9GLOM
Original site: A0A397ISY5_9GLOM 
ID   A0A397ISY5_9GLOM        Unreviewed;       405 AA.
AC   A0A397ISY5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=BED-type domain-containing protein {ECO:0000259|PROSITE:PS50808};
GN   ORFNames=Glove_169g66 {ECO:0000313|EMBL:RHZ77902.1};
OS   Diversispora epigaea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX   NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ77902.1, ECO:0000313|Proteomes:UP000266861};
RN   [1] {ECO:0000313|EMBL:RHZ77902.1, ECO:0000313|Proteomes:UP000266861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT104 {ECO:0000313|EMBL:RHZ77902.1,
RC   ECO:0000313|Proteomes:UP000266861};
RA   Sun X., Fei Z., Harrison M.;
RT   "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT   epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL   Submitted (AUG-2018) 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:RHZ77902.1}.
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DR   EMBL; PQFF01000159; RHZ77902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397ISY5; -.
DR   STRING; 1348612.A0A397ISY5; -.
DR   Proteomes; UP000266861; Unassembled WGS sequence.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR44858; TETRATRICOPEPTIDE REPEAT PROTEIN 6; 1.
DR   PANTHER; PTHR44858:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   Pfam; PF02892; zf-BED; 2.
DR   SMART; SM00028; TPR; 3.
DR   SMART; SM00614; ZnF_BED; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
DR   PROSITE; PS50808; ZF_BED; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266861};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT   DOMAIN          10..64
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   DOMAIN          98..145
FT                   /note="BED-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50808"
FT   REPEAT          278..311
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          312..345
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          346..379
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          152..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  46348 MW;  9E08A1D018D7DF2A CRC64;
     MFSSISSNSH TKSKVWDYFT KPYGPPQSRK TKCHECGNEF SYHGSTSSLK YHLKNRHKID
     MSTNLSQVNR QSQQIPSQQS NFSLYPEPSF SENKNSSLQS STVWDYFTKP YGPPQSRKTK
     CHECGNEFSY HGSTSSLKYH LKNRHMSINL RQSQQIPSQQ SNFSLYPEPS FSENKNSSLQ
     SSTISLANKK NKVWDYFTKP SSSSNHGSPS SLKYHLIHLH NIDMSTNSVD QIQNQNQPLN
     LQLQNLEQKN ADILTAEEGF FTVLNKLLET NRNDKGNKDA LIIRGKFYRK MGIYEESTAD
     LNKVLEIEPN NVKVLISKGK VYKKMGKYEE SITNLSRALE IEPNNVKVLI SKGKAYKKMG
     KYEESITYFS RALGIEPNNV NALKSRGDAY YRIGEYEKSI ADSRD
//
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