ID A0A0C9SUU1_PAXIN Unreviewed; 615 AA.
AC A0A0C9SUU1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695};
DE Flags: Fragment;
GN ORFNames=PAXINDRAFT_20535 {ECO:0000313|EMBL:KIJ06265.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ06265.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ06265.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ06265.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; KN820414; KIJ06265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9SUU1; -.
DR MEROPS; S53.007; -.
DR HOGENOM; CLU_013783_4_0_1; -.
DR OrthoDB; 2326650at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 205..614
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 171..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 530
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT NON_TER 615
FT /evidence="ECO:0000313|EMBL:KIJ06265.1"
SQ SEQUENCE 615 AA; 66248 MW; B674BB72970F17D3 CRC64;
ANADPTLSPW VLHERRSHIP PGWARARKHD TSAAIPLRFA LVQPNLENIE KYLYDVSHPN
SPNYGKHWTA SQVAATFGPS QESVDAVRDW LLENGIESHR VKISPSRGWL QFEATVEEAE
DLLHTTYHVY GHETGAEHVA CDSYYLHEHL VHHVDFVTPT VHFDAKLSKR SGGSMRVGQP
GSGNGPKTTG VVSNSTNQLE DCDKQITPIC LRALYGLNYE PLSGDKNSYG IAEFTPQSYR
QDDLNLFAKN FSSDLYGVSP TMVSIDGGSL STEISVDING ESSLDLEYAM NMVTSKQKVT
LYQVGDMVAG AYLNNFLDAL DGTYCSFEGG DDPNLDITYP DTQAGGYNAK DCGTVKPANV
ISTSYGYNEA DLTPAYTARQ CAEYAKLGLM GVTVLYSSGD HGVAGGGNVC LNPDGSQTSD
GKIFNPTFPS TCPYVTSVGA TQVNPGNSVS DSESACEQFI YSGGGFSNNF AIPDYQKDAV
SSYLKNYPPA YPSSIWNSTG MSRAYPDISA NGANYVVAID GNFILVFGTS ASSPVVGAIL
TMINDARINI GKGPIGFINP LIYSANFTDG FHDITNGTNR GCGTLGFNAT KGWDPVTGLG
TPNFPALLDK WRSLP
//
