ID A0A176VGM3_MARPO Unreviewed; 465 AA.
AC A0A176VGM3;
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=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=AXG93_2958s1120 {ECO:0000313|EMBL:OAE19737.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19737.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19737.1, 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:OAE19737.1};
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:OAE19737.1}.
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DR EMBL; LVLJ01003787; OAE19737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VGM3; -.
DR OrthoDB; 398606at2759; -.
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:SF23; OS04G0448300 PROTEIN; 1.
DR PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 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|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 94..458
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 465 AA; 51270 MW; F0152C68D65F4F54 CRC64;
MMFLSEVIVI ANRSKREATL SPQVGEEHSP LENSFKTKMR RLEPRFQTMG ERVAHHVKSS
WSRATILRAR MQDFLELDHD SGYQSKMTAV PGGYAMSISL GSPPQEFMVI ADTGSDLTWV
QASACDACFS QASDPYDQDK SSTYQSLSCP SYMCNALGTQ AQCSDDEDED GLCQYAYQYG
DNSVTEGNFS TETITLQNTD GEMLAVPNFA FGVGLHNSVD FYGVDGLVGL GQGPISFPSQ
LGKQYGNVFS YCLQSIFSDP TTSSPVIFGR SALPTSENVQ YTALQTSENK RIPTFWFLNL
IGVRLNNKMV NVDSEQSLIA GGEIGEQSMI IAAQSPMGTV IDSGTTITML DPRVYLTLAR
MVETRVKYSR TSSQVSGLDL CFDVGNDRDP DLPGLTLIFQ DQSWDLPKVN VFVPVDELAQ
IWCLAVIPTN QGIQIIGNLQ QQNFQMIYDQ PNARIGWIPS NCESI
//
