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Database: UniProt
Entry: A0A176VPI6_MARPO
LinkDB: A0A176VPI6_MARPO
Original site: A0A176VPI6_MARPO 
ID   A0A176VPI6_MARPO        Unreviewed;       777 AA.
AC   A0A176VPI6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=SWIRM domain-containing protein {ECO:0000259|PROSITE:PS50934};
GN   ORFNames=AXG93_496s1150 {ECO:0000313|EMBL:OAE22819.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE22819.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE22819.1, 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:OAE22819.1};
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   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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:OAE22819.1}.
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DR   EMBL; LVLJ01003060; OAE22819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VPI6; -.
DR   OrthoDB; 5402444at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          105..206
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          13..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  84761 MW;  B693DCFADFE00D6D CRC64;
     MVEMELEVKL NTGTSRTSAV GQTNAQQRDV KGAVEKRKRK RLETSSVVLQ ETTVGVASGK
     SIRSLRQQTR APTYDEDLLD AVIDQQLGGT PFPARGRKRK PLSVEKEVDV EAMIAASIGF
     PRESLTEEEI EAGVVASAGS LEQANYIVVR NHILAKWREN VNAWLDEDTV MESIRSQHKS
     LVAAAYKFLS TFGYINFGVA PAIKSRIPEE ATKATVIIIG AGLAGLAAAR QLLAFGHKVI
     VLEGRQRPGG RVYTKKMVGE GLAAAADLGG SVVTGIHGNP LGVLARQLGF PLHKIREKCP
     LYQPGGLPVK EEMDARVEAQ FNKLLDRASK WREEMNTVAD SISLGTTLET LREDAGVAVN
     AEERQLFDWH LANLEYANAG LLSNLSLAFW DQDDPYEMGG DHCFLPGGNV RLVAALAEGV
     PIFYGKTIHT IRYSSEGVQV IAGEQIFEGD MALCTAPLGV LKREAIKFEP ELPVRKIDAI
     KRLGFGLLNK VVMLFSHPFW GAELDTFGHL AESTNRRGEF FLFYSYAAVS GGPLLLALVA
     GEAAINFECM PPIEAVTRVL SVLRVGASGD DYDILAECVG DGRLFFAGEA TNRRYPATMH
     GAFLSGLREA GNITTFAGSR IVSSKGERGI QKDIQSFATI LVDIFKEPDL QFGCFSVVFD
     PQTNDLKSYV IVRLTIGKGE RKEEPESSPT DQQSVHLYTI ISRRQAFELL ELRGGDKLRL
     IYLSDKLGVK LVGRRGLGVI GDGIVSVTKW NRAARKVNSP LNITPVTSFA AKTPKSQ
//
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