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Database: UniProt
Entry: A0A2K3N8M8_TRIPR
LinkDB: A0A2K3N8M8_TRIPR
Original site: A0A2K3N8M8_TRIPR 
ID   A0A2K3N8M8_TRIPR        Unreviewed;       784 AA.
AC   A0A2K3N8M8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Subtilisin-like protease-like protein {ECO:0000313|EMBL:PNX99388.1};
GN   ORFNames=L195_g022653 {ECO:0000313|EMBL:PNX99388.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX99388.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNX99388.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX99388.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNX99388.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNX99388.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
CC   -!- FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM
CC       symbiosis with AM fungi (e.g. Glomeromycota intraradices).
CC       {ECO:0000256|ARBA:ARBA00002076}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271}.
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:PNX99388.1}.
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DR   EMBL; ASHM01017707; PNX99388.1; -; Genomic_DNA.
DR   STRING; 57577.A0A2K3N8M8; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
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:SF785; SUBTILISIN-LIKE PROTEASE SBT1.4; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|ARBA:ARBA00022523};
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:UP000236291};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..784
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014383605"
FT   DOMAIN          36..118
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          142..610
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          385..469
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          676..773
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        557
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   784 AA;  83364 MW;  3C1D626696381CA2 CRC64;
     MASSLSSPHS LLLLFFTFFF FLFSLSXSQQ SNTPQTFIIH VSKSQKSSSS LFSTNQNHFS
     SILNTLPSSP SSTPPSILYT YTSAIHGFSA QLTPSQADHL KSHPDILSIQ PDQIRHLHTT
     YTPSFLGLAE TSGIWPSSHF ASDVIIGVLD TGIWPEHQSF SDPSLSKSTL PSSWKGSCQI
     SHDFPSSACN NKIIGAKAFY KGYESYLQRP IDETVESKSP RDTEGHGTHT ASTAGGFVVG
     NASLFGFARG EAKGMATKAR IAAYKICWNV GCFDSDILAA MDEAVSDGVH VISLSVGSNG
     YAPHYYRDSI AIGAFGAAQQ GVVVSCSAGN SGPGPYTSVN IAPWILTVGA STIDREFPAD
     VILGDDRVLG GISLYSGDDL PDYKLPLVYS ADCGSRYCYV GSLDSSKVKG KIVVCDRGGN
     ARVEKGSAVK KAGGLGMIVA NTEESGEELL ADAHLIAATM VGQTAGDKIK EYIKSSQNPT
     ATIKFKGTVI GGSDLPPAPQ VASFSSRGPN YRTSEILKPD VIAPGVNILA GWTGKAAPTD
     LEIDPRRVEF NIASGTSMSC PHVSGIAALL RKAFPNFSPA AIKSALMTTA YNVDNSGGKI
     KDLGTGKESN PFVHGAGHVD PNKALNPGLV YDINTNDYLS FLCSIGYDAK KIQVFTREPT
     SYNICENEKN LASPGDLNYP SFSVEFGAYN GLVKYKRVVT NVGGSDDAVY TVKVNAPFGV
     DVSVSPSKLV FSSENKTQAF EITFTRIGYG GSQSFGSIEW SDGNHIVRSP IAVRWSNGFS
     SASF
//
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