ID B6HVF5_PENRW Unreviewed; 659 AA.
AC B6HVF5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Pc22g19110 protein {ECO:0000313|EMBL:CAP99199.1};
GN ORFNames=Pc22g19110 {ECO:0000313|EMBL:CAP99199.1}, PCH_Pc22g19110
GN {ECO:0000313|EMBL:CAP99199.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP99199.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP99199.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920437; CAP99199.1; -; Genomic_DNA.
DR RefSeq; XP_002565814.1; XM_002565768.1.
DR AlphaFoldDB; B6HVF5; -.
DR STRING; 500485.B6HVF5; -.
DR MEROPS; S53.007; -.
DR GeneID; 8313569; -.
DR KEGG; pcs:Pc22g19110; -.
DR VEuPathDB; FungiDB:PCH_Pc22g19110; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR OMA; EFYEHEH; -.
DR OrthoDB; 1405251at2759; -.
DR BioCyc; PCHR:PC22G19110-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c22.
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; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 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:UP000000724};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 223..658
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 304
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 576
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 618
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 636
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 638
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 659 AA; 72533 MW; B3334AAA6D2D24D7 CRC64;
MAGYHYSFIV SRDAAPVKHV LHEKRSEHVD WVKGERIKRD SVLPVRIGLA QNNLERGDEY
LMAVSDPDSA KYGQYWSAEE VHEFFAPSKD SVDSVRRWLQ SSGIHESRIV HSDNKGWLAF
DAYAHEVEDL FKAEFYEHEH ASTSSMKIGC EEYHVPENIQ AHIDYITPGV KLSPIVKKNT
KAKRMSHLAH SKGTVEADNS IKTTVISEKA QSLPADLQRC GTDMTPACIM ALYDIPDATK
AAKGNSLGLY EQGDYFAKSD LDLYYKHFAP WIPRGTYPIP ALIDGASFSV PDYSPLNAGE
ADIDIDMAYS LIYPQSITLY QVDDQTYEPE EEKTTNLFNT FLDALDGSYC TYSAFGETGN
NPDIDPVYPN PRPGGYKGEL QCGVYKPTTV ISASYGQAEA DLPIAYTKRQ CNEFMKLGLQ
GHSILFSSGD YGVASFHNDG AVNGCLGPEG KIFNPQYPSN CPYVTSVGGT MLYADQTVKD
AESVMSANLG GDSANFTSSG GFSNYFPQPS YQKKAVEKYF QKAKLTYPYY SEMEVNINKT
KGLYNRIGRG YPDVSANGAV FPAYNGGKLT HYYGASLASP LFASVLNLIN EERLDQGKGP
VGFVNPVLYA HPEVLNDITN GTNLGCGSDG FSAIPGWDPA TGLGTPNYPK LKELFLSLP
//
