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Database: UniProt
Entry: A0A176VPD4_MARPO
LinkDB: A0A176VPD4_MARPO
Original site: A0A176VPD4_MARPO 
ID   A0A176VPD4_MARPO        Unreviewed;       571 AA.
AC   A0A176VPD4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=AXG93_1175s1510 {ECO:0000313|EMBL:OAE22141.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE22141.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE22141.1, 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:OAE22141.1};
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 peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:OAE22141.1}.
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DR   EMBL; LVLJ01003272; OAE22141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VPD4; -.
DR   OrthoDB; 1212336at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05476; pepsin_A_like_plant; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034161; Pepsin-like_plant.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47967:SF109; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          213..564
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        444
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   571 AA;  61921 MW;  1DC95E54675A1FB2 CRC64;
     MRRPDAIRLT PLKVPEAGLR AYQNELILAK LEFLLRGGIG GVGLLTEAEK ETISVANLRS
     REEEIANELD TDSENEQIDS PQGKNAELET RISGKTDVEP LKKALNNQQT GWVTAHLKRP
     TGSHLHAGRH LGETAKGETA TASSRNGWRA SLIVRSAGTE NFTILQLVHR DVEASIARGK
     SLDRKARNAP YHKHKGRSML DFTTNIEATP NAYSMEISLG TPPQNFIAIA DTGSDLVWLE
     CKACTVCINA SAVFDPSLSS TYSPLGCNGC NVLGSNELTC TPNCQYTYEY GDLSSTQGNF
     SLDTLTLQNT NGTSTAIDSF HFGCGLQNNG SFLEVDGLVG LARGPISFPS QIAPFLNNVN
     KFSYCLLGRY DPAAARSPLL FGKSAVPTNV SFTVFTPQLT PYDPSVLSFY YVNLTDISVG
     GAALNIPASA FAIDTQGNGG VIFDSGTTVT LLNTVAYRSV VDTFTSQIDT TYPRVNLLSL
     TGLEVCYNTT AFSYVNVPTV VFKFDGADFD LPFQNIVLLL NFTDTESAMC LAMQESQGMS
     IFGSVQQQNF QVLYDEDNLQ IGWVPTDCQT L
//
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