ID S7ZX06_PENO1 Unreviewed; 1182 AA.
AC S7ZX06;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDE_09949 {ECO:0000313|EMBL:EPS34984.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34984.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34984.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; KB644415; EPS34984.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZX06; -.
DR STRING; 933388.S7ZX06; -.
DR MEROPS; M16.008; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_2_1; -.
DR OrthoDB; 129328at2759; -.
DR PhylomeDB; S7ZX06; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 220..279
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 306..484
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 490..778
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 782..962
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 182..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 134516 MW; A23BD18FB0E7A0AF CRC64;
MPPRSSTAHP WLWYCRSSTC RSNLRSTLSL RPISFKSPLT VANAPTFERK SSPTRSFCRS
SQVLSSTSPV MSQIQRITES LEKPDLDDRS YRVIRLPNKL EALLVHDPDT DKASAAVNVN
VGNFSDQDDM PGMAHAVEHL LFMGTKKYPK ENAYNQYLAA HSGLSNAYTA ATETNYFFEV
SATGDSSPAP STGQNDSAES TGASDQVADK SSSDSAADSD KKSPLYGALD RFAQFFVSPL
FLESTLDREL RAVDSENKKN LQSDLWRLMQ LNKSLSNPKH PYHHFSTGNL QTLKEDPQKR
GLEVRSEFIR FYEKHYSANR TKLVVLGRES LDVLEGWVAE LFADVENKDL PQNRWDDVQP
FSEEDMCTQV FAKPVMESRS MDMYFPFLDE ENLNDVQPSR YISHLIGHEG PGSILSHLKA
KGWANGLSAG AMPICPGSAF FTISVRLTPE GLKLYQEVAK VIFEYISMIK EREPEQWIFD
EMKNLAEVDF RYKQKTPAIR FTSRLSSVMQ KPMPREWLLS GSLLRRFDPE VIKNAMSYLR
ADNFRLIIVS QDYPGEWDQR EKWYGTEYKV EKIPHDFLSG IQKALRSTET TRTSSLHMPH
RNEFVPTRLS VERKEVAEPA KIPKLIRHDD RVRLWFKKDD RFWVPKATVH VTLRNPLVWT
TPANLIKTKL YCELVRDSLD EYSYDAELAG LDYHLFTTTL GLEISVGGYN DKMSVLLEKV
LKTMSGLLVN QGRFNIIKER LARAFRNAEY QQPFHQVGDY DRYLLSERSW INEQYIEALE
HIEAEDVIKF FPSLLEQTHI EVLAHGNLYK EDALRMTDMV EKILGGRTLP ASDWYLYRNM
IIPPGGNYIY PRTLKDPANV NHCIGYYLHI GSFSDDVLRA KLQLFSQLTD EPAFDQLRSQ
EQLGYVVWSG SRYNTTTMGY RVIIQSERNA QYLESRIDAF LTQFGQTLEK MSDDEFEGHK
RSVINKRLEK LKNLGSETGR FWSQVRSEYL DFLQHETDAA CVRVLGKVDL IEFFKQYIDP
SSPTRAKLSV YLNAQSDAAS TETGPVQQRT RLIEAVKEDL DSAGLTVNSD TLTAAFEQLD
MAVVDLSQIM YILKGFLATE LPESAGQNHA VISKLEAKLG AQLKQLGLGT KEHADSANGT
SSNLPKPVIV EDVRSFKARL PVSTGPVPVS DLTDYEDFEA KL
//
