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Database: UniProt
Entry: A0A176VYE2_MARPO
LinkDB: A0A176VYE2_MARPO
Original site: A0A176VYE2_MARPO 
ID   A0A176VYE2_MARPO        Unreviewed;       285 AA.
AC   A0A176VYE2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=HMG box domain-containing protein {ECO:0000259|PROSITE:PS50118};
GN   ORFNames=AXG93_2145s1280 {ECO:0000313|EMBL:OAE25829.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25829.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25829.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25829.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) 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:OAE25829.1}.
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DR   EMBL; LVLJ01002289; OAE25829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VYE2; -.
DR   OrthoDB; 1222751at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00084; HMG-box_SF; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR045881; MNM1-like.
DR   PANTHER; PTHR34682; AT HOOK MOTIF-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34682:SF1; PROTEIN METABOLIC NETWORK MODULATOR 1; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          48..104
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        48..104
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          106..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  30812 MW;  8C01ECBC5A0AE74A CRC64;
     MLLLLLVGTS VKDDGQAIVM EEQAATIIIS DVPEEKKVPA EKEGSVGKLV KLRAFNLFAS
     KIRDTIKDEN PVANGHEIKR IVGQKWAKLG NQDKQEYIDV AQNETDLLGQ MPVDPNAPKR
     RRRRRTKAEI ELDDGSGFPK KRRGRPRKNG DAMRGEVSNG TVPSNGDGQP KRRRMRKQGD
     ASGKAVDPAF VGKCVSGTVD GSFDAGYLVT VRVGDTDMVF RGVLFEPSIA MPPNNTNDVA
     PNVKLVRRND GIVFPSTGPM HSSSGPASSS KQMLGGPMHS AGTVV
//
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