ID A0A176W9G1_MARPO Unreviewed; 736 AA.
AC A0A176W9G1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_1513s1040 {ECO:0000313|EMBL:OAE29778.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE29778.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE29778.1, 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:OAE29778.1};
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 S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:OAE29778.1}.
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DR EMBL; LVLJ01001412; OAE29778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W9G1; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF542; SUBTILISIN-LIKE PROTEASE SBT1.5; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 18..65
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 90..565
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 346..421
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 620..726
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 99
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 506
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 736 AA; 76908 MW; 6894AE3BB257777D CRC64;
MAQTQQPVMR HTQSVFAVNE LDGILHTYST VFQGFAARLT EAEAEAMRLR PGVMAAYPEQ
VRQLHTTHTP EFLGLNSSVA TDLTEEAKYG EDVIIGVLDT GVWPERASFL DHKMGPIPAR
WLGGCADEES FSASLCNRKL IGAKYFAKGY EAATGPVNTT VEFKSARDGE GHGTHTASTA
AGRMVSKASL LGFAEGVARG MASKARLAVY KVCWESGCYD SDILAAFDEA VADGVDVISL
SVGGGVVPYY LDPIAIGAYG AMKKGVFVSC SAGNSGPGSL TVTNVAPWIT TVAASTIDRS
FPATVTLSGG DEFQGTSLYS GPDLGDSLHP LIYAVNASKA GVNAYSASLC LDGTLDPAKV
KGRIVLCDRG SNARVAKGQV VKAAGALGMI LANLPVDGEG LVADSHVLPA TAVGAKAGAK
IKDYILSTKS PKANILFRGT VYGVQPAPVI SSFSSRGPNP ETPEVLKPDI TAPGVNILAA
WTGAAAPTGL EGDNRTVEFN IISGTSMSCP HISGIAALLK GARPGWSPAM IKSAIMTSAY
VVDNTGAPLA DEATGNVSTP FAYGAGHVDP QRAMNPGLVY DLEVADYIKF LCALNYSQAA
IRVIDPDVGA CPTKIGSPSE LNYPSFSTLF DQTGSSSAML ETTFSRTVTN VGPANSTYTV
DVVGPKNVKI TVSPSILEFT EENQKLHYTM KVSAPPVKLP PGTIGSAFGF VAWTDGIHVV
QSPIVINWQE SFPTSL
//
