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
//