ID A0A137NQJ2_CONC2 Unreviewed; 586 AA.
AC A0A137NQJ2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
DE Flags: Fragment;
GN ORFNames=CONCODRAFT_13536 {ECO:0000313|EMBL:KXN65027.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN65027.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN65027.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN65027.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; KQ965013; KXN65027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137NQJ2; -.
DR EnsemblFungi; KXN65027; KXN65027; CONCODRAFT_13536.
DR OMA; STWNDVI; -.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000070444; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 2.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024, ECO:0000313|EMBL:KXN65027.1};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 12..101
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 146..298
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 363..562
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXN65027.1"
SQ SEQUENCE 586 AA; 66242 MW; 37B2984ACF04D521 CRC64;
ADQFIISRRY LGGQREAFID PNQLFEKGTT KILNYKISPN GKYLAYVISR KGSDWQSIYV
VDILYRTQVS EIQWTRYNDE ISWLSDSSGF YYRSYAPANG ITFDQAGLEN EPPKYIGYNL
HTVKGGRSQE FSITPEAEDN HYGSKARLIE LGQGIASAKD FILSANSDHF IKYLSSDEDG
MEFITDIGAR NRHIVKVNFN SLDKYEVIVS EFPDKMITDR LFFGSKVVLF SIWDGISFAA
YIDYRKGSEP IEINMPFGVA SNPRLSGDGS SLAFNLDSFL HYSQSYRFDF DTNTLTLVNT
FTHPNFDASK FVQYRTLYTA KDGTEIPLLI AHKKGIKPDQ SHPGFLYGYG GFKSIQKPNY
DQFWAYLLQE KNMVLAIALV RGGSERGYDW WESATKLNKY RSYSDYADAV EFLHKDPKYG
FVGKNMQFIN GVSNGGLLTA ATCNLIPEKL GGCIADVGVQ DLLRYDRWTV GDGWKEDYGK
PSDSKEQFNA LMKISPLENV LPAVNATQTK YYPPYLINTA DYDDRVSPVH SLKLAATIQN
NHKASPHPAL LYVAHHSGHN PSSNTKYLDK CVNAVSLINI ALNKLY
//