ID B1NNU2_9PEZI Unreviewed; 465 AA.
AC B1NNU2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ABV46590.1};
GN Name=SPR2 {ECO:0000313|EMBL:ABV46590.1};
OS Dactylellina haptotyla.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=430498 {ECO:0000313|EMBL:ABV46590.1};
RN [1] {ECO:0000313|EMBL:ABV46590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:ABV46590.1};
RX PubMed=18028414; DOI=10.1111/j.1462-2920.2007.01457.x;
RA Fekete C., Tholander M., Rajashekar B., Ahren D., Friman E., Johansson T.,
RA Tunlid A.;
RT "Paralysis of nematodes: shifts in the transcriptome of the nematode-
RT trapping fungus Monacrosporium haptotylum during infection of
RT Caenorhabditis elegans.";
RL Environ. Microbiol. 10:364-375(2008).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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; EF681770; ABV46590.1; -; mRNA.
DR AlphaFoldDB; B1NNU2; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..465
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002769345"
FT DOMAIN 199..438
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 465 AA; 49289 MW; 3F12D52F21EFB06C CRC64;
MKSIAIISTS LLLSVLPATL AAPTARNGVV GRRWFNPDAP KAAKVAEVEA QDTDPKNEYI
VVMSANETRP WAEIFAEMGC NSSDTKTFGT NIRAFTMTMK KSEGVSMFSL PNVAILEKNT
IYKAAVMPGT SQPKNMARNL VKESLRARND LTKRQNNIFI EQSTAPWNLQ RISSSDTVTA
GDRQATDLAF KYRFDQASGS GVDVYMLDTG INVDHVDFVG RAKMVFSVDN TQNDAQGHGT
HTAGTVGART FGVAKNVNLL GVKVLQDNGS GSIAGIVQGI DFVISEHQKR QQQNDFQGSI
ISMSLGGDGL PQSMFTALKK ATDAGVHVSV AAGNENQDAC NTSPAGFSQQ IPIISVGATD
ITDQRAGFSN FGKCVDIHAP GVDIVSTFNK GTTSTTSLQG TSMACPAVSG MIADLLVLNP
NLRTNPDGMK KLLLSKALGN AIKAGGNVPQ NGQILLNSGF PGNPN
//
