ID   A0A176VWY5_MARPO        Unreviewed;       453 AA.
AC   A0A176VWY5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Serine aminopeptidase S33 domain-containing protein {ECO:0000259|Pfam:PF12146};
GN   ORFNames=AXG93_4620s1430 {ECO:0000313|EMBL:OAE25329.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25329.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25329.1, 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:OAE25329.1};
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:OAE25329.1}.
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DR   EMBL; LVLJ01002341; OAE25329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VWY5; -.
DR   OrthoDB; 167818at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   PANTHER; PTHR43358; ALPHA/BETA-HYDROLASE; 1.
DR   PANTHER; PTHR43358:SF4; ALPHA_BETA HYDROLASE FOLD-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          19..102
FT                   /note="Serine aminopeptidase S33"
FT                   /evidence="ECO:0000259|Pfam:PF12146"
FT   REGION          250..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  50188 MW;  1858CB3BF0BAB60C CRC64;
     MYSGCRADAN EAAIILLPSN VTVFTLDFSG SGLSDGDYVS LGWNEMEDLK AAVTFLRTEK
     HVSRIGLWGR SMGAVTCLMY GAQDPSIAGM VLDSPFSNLF DLMMELVDVY KIRLPKFTVK
     VAVQYMRKVI QKKAAFDIMD LDTVQVAGKS FIPALFGHAT EDLFIQPHHS DLLFKAYSGD
     KNIIKFEGDH NSPRPQFYYD SITIFFYNVL RPPDEPVAPE APDTVYFDTD GLEMDDDVDE
     SILYEIMGAE RPAAHGTPQT PTSTSSGPRQ DGLTAESTEE ALNQTRSRWQ MSRTVVPVNT
     SNSQDDLSEL LRGDLSTDGL EGSSSCAVLE NGDSGNYRDD FARYRSSKDY SDSWGRHSSN
     GVSLDSSGMM SPRTEDSFAH FPSNRDDEER MVMEAIAASL QDVEIKETEQ KEPAEVGSPT
     SEDTAAATRV DSFTQRMRLS FFRGMGSRRS ASR
//