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Database: UniProt
Entry: A0A2N5T5S5_9BASI
LinkDB: A0A2N5T5S5_9BASI
Original site: A0A2N5T5S5_9BASI 
ID   A0A2N5T5S5_9BASI        Unreviewed;       397 AA.
AC   A0A2N5T5S5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=HMG box domain-containing protein {ECO:0000259|PROSITE:PS50118};
GN   ORFNames=PCANC_08244 {ECO:0000313|EMBL:PLW20836.1}, PCASD_17419
GN   {ECO:0000313|EMBL:PLW30071.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW20836.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW20836.1}, and 12SD80
RC   {ECO:0000313|EMBL:PLW30071.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) 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:PLW20836.1}.
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DR   EMBL; PGCJ01000791; PLW20836.1; -; Genomic_DNA.
DR   EMBL; PGCI01000310; PLW30071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5T5S5; -.
DR   STRING; 200324.A0A2N5T5S5; -.
DR   OrthoDB; 1540759at2759; -.
DR   Proteomes; UP000235388; Unassembled WGS sequence.
DR   Proteomes; UP000235392; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR46040; HIGH MOBILITY GROUP PROTEIN 2; 1.
DR   PANTHER; PTHR46040:SF3; HIGH MOBILITY GROUP PROTEIN 2; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00267};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT   DOMAIN          171..237
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        171..237
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          83..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  44890 MW;  B42F5DCB67FF9029 CRC64;
     MDSREGSVES FLGSLGLGDY LSIFLSEGFD TIQAIQEITE EDLEQMRVKR GHRRILQRAL
     GKRFSANAPA DLRLDPACLS QAPISPPPFS GEARLQSALT QRSASWDPES SHSESSFFAN
     ADRNLTPSQN QCRPTGFSQA DLTSGSTAQF CLPPKPKRRY RRHPKPDLNA PKKPLSAYVM
     FSNTVREQLQ GQQISFTEIA RIVGDRWKKL DPSTKEVFER EAAEQKDRWT RSMLAYKRTR
     EYEQYRRYLQ QFKEAQQVRN STTQPPPKRY SDVDCCSTQS MGVESECNDD SREASDVDEA
     GERNDITSHP VMASSVSPAQ RSTDGSYPNP SPRDGAQFHP PQPARSASEN QYYHLPPPLT
     RSCSRRPTIP NLRTLDKHLT ESQTLFFKSN CSVRSTQ
//
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