ID A0A176VJ90_MARPO Unreviewed; 511 AA.
AC A0A176VJ90;
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_3256s1870 {ECO:0000313|EMBL:OAE20940.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE20940.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE20940.1, 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:OAE20940.1};
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:OAE20940.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVLJ01003561; OAE20940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VJ90; -.
DR OrthoDB; 335768at2759; -.
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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 143..489
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 375
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 511 AA; 54231 MW; 88930C0EE0F79D2C CRC64;
MSRPDTLHLF SSSCSRSFEI ITLLSLRLKM AAIRSCVEFL LLATVALVHT ADPSLATENV
KAPFVGLKHL DYHQDSPLHD AHTTFVERIH TSVRRSEARA SAFRSIVAAG ITPRGTHFDS
TVEVSSKAAS SFQSAVSAAP GGYIMSISLG SPPQTRTAIA DTGSDLVWLQ CAPCSVCFRQ
SDPLFDPRKS ATFTRIRYFS PLCGELPQVS YDGGFCTYRY GYGDQSTTQG DFALETLTLT
AIDGSTQSIN NFAFGCGRRN QGTFAGTDGL VGLGRGAISF TEQIGSRTGS KFAYCLVDAG
TSGSEVSPLI FGDSAAETGN ALNLSYTPLI RNPAADTFYY VKLNGISVNG QPVAGIPANA
YTLNVLTGRG GVILDSGTTI TQLVQSAYIR LLTVLQSLIA YPQVDGSPVG LDLCYDVSGV
SSPSLPSVTL QFQGIDVVLP ADNVFLQVDA QGTMCLAFAG TSDFSIIGNI QQQNFYYLYD
VENERVGIAP LDKCAALAST AASTGGLLDE L
//
