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
//