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Database: UniProt
Entry: A0A9N9PR55_9HELO
LinkDB: A0A9N9PR55_9HELO
Original site: A0A9N9PR55_9HELO 
ID   A0A9N9PR55_9HELO        Unreviewed;       497 AA.
AC   A0A9N9PR55;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   02-APR-2025, entry version 7.
DE   RecName: Full=DM2 domain-containing protein {ECO:0000259|PROSITE:PS51925};
GN   ORFNames=HYFRA_00003913 {ECO:0000313|EMBL:CAG8956526.1};
OS   Hymenoscyphus fraxineus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Hymenoscyphus.
OX   NCBI_TaxID=746836 {ECO:0000313|EMBL:CAG8956526.1, ECO:0000313|Proteomes:UP000696280};
RN   [1] {ECO:0000313|EMBL:CAG8956526.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Durling M.;
RL   Submitted (JUL-2021) 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:CAG8956526.1}.
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DR   EMBL; CAJVRL010000070; CAG8956526.1; -; Genomic_DNA.
DR   OrthoDB; 10263741at2759; -.
DR   Proteomes; UP000696280; Unassembled WGS sequence.
DR   CDD; cd10568; SWIB_like; 1.
DR   Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR13844; SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY D; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   SMART; SM00151; SWIB; 1.
DR   SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000696280}.
FT   DOMAIN          270..350
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..50
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..187
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  56245 MW;  E2EAFD1039280A37 CRC64;
     MQPHPQYRGM PQRSPHAAVA QSNQRRGIGP MVGVHPTPSQ MQAQQQAQSR ASDRAKIRSQ
     KPTDRNIPEG VEDCIIGDGV QRYRDLREIE RRLDSTMMRK RLDLQDSVNR NVKRYRTLRV
     WISNTVEDQP WQADSLDVDT FDFSTNLDSS FRVKIEGKLL DEPAEDLDSD DSDSEDEAAD
     PDAMDEDGKE KKKKTVIPPK EYKLSHFFKA MTVDFDRKGR DGTDQSVEWK KPALPANAKD
     LPNAADFDQL EFKRGGDENM NITINLTRDE TPERFKLSPV LSQILDTTEA TRSEAIMGIW
     EYVKANGLQE DDDKRSFTCD DALRTLLGGR EKGYIPYLTE NILAHMTTLP PVKLQYTIRT
     DKAFHEDPQP TIYDIQVQVD DPLRAALISY LGNDSYTQNL IEIGRLNEHA AVLVQKISNS
     KSKHAFYDAL SKNPTSFIAK WLSSQKRDLE VISGRATRGG GEDASGDEWR RGGKDGIWGS
     TNVKESVNLI VGQKARM
//
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