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Database: UniProt
Entry: A0A176WPM5_MARPO
LinkDB: A0A176WPM5_MARPO
Original site: A0A176WPM5_MARPO 
ID   A0A176WPM5_MARPO        Unreviewed;       520 AA.
AC   A0A176WPM5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE34503.1};
GN   ORFNames=AXG93_1299s1160 {ECO:0000313|EMBL:OAE34503.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE34503.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE34503.1, 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:OAE34503.1};
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 plant acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009861}.
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:OAE34503.1}.
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DR   EMBL; LVLJ01000396; OAE34503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WPM5; -.
DR   OrthoDB; 64824at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   PANTHER; PTHR31642:SF266; HXXXD-TYPE ACYL-TRANSFERASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR31642; TRICHOTHECENE 3-O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF02458; Transferase; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   REGION          226..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  57555 MW;  E5FC7096D3DEFD47 CRC64;
     MPMAQLLVDV SRLELQKVSV SNVKPSGRNQ HVEKYDVALL DLLIPDYCMP VLFLFKPHPG
     DQIGLSGSEF VRRLKESLSK LLVPYYPYAG RFCKTYDHRI RELLCNDEGV PFIEAEIDQE
     MDKVVSFDDF QPVPILSGFK FVNLDAGVFF HDKADLFLPA LFIQATKFRC GGVSVNMTFT
     HMLADGKAIF QFVKDWSQMT LEGHCTNLPI HDRSLSHPVS LLQSLIPSGN PRESHVETNH
     SQNGHAPLRP DDKSLGGGKR DRSDEGTDNG GAPASLMDHR AVRQDCADAK AAVDPALAVR
     FPILPAWARK TLHVKKASVM KLKQRAMANE ERGLVPTALD CIQSHIWRGL CSIPSSLDGK
     KGCVYGVAVE GRARMHTPAL PESYAANAFV IAYTQPLEHP SDDHLTDASK IHDIVRSVNP
     ESWPGQLGRT VGILLNGAAI QQRAFFSSSW YRFPMYEVDF GYGKPVLVTG SAACSSPLTG
     YAFILPPRPG SDFLASVQMV LPPELLQALL DNSEFRSFFH
//
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