ID   A0A168NI32_ABSGL        Unreviewed;       712 AA.
AC   A0A168NI32;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN   Name=ABSGL_06295.1 scaffold 8040 {ECO:0000313|EMBL:SAM00587.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM00587.1};
RN   [1] {ECO:0000313|EMBL:SAM00587.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM00587.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR   EMBL; LT553293; SAM00587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168NI32; -.
DR   STRING; 4829.A0A168NI32; -.
DR   InParanoid; A0A168NI32; -.
DR   OMA; NGYWYIT; -.
DR   OrthoDB; 7264at2759; -.
DR   Proteomes; UP000078561; 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; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
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};
KW   Protease {ECO:0000256|RuleBase:RU368024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          34..435
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          494..707
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          31..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  80974 MW;  1C8F358408270506 CRC64;
     MWAGTRLLHT PHLRSPQRTL FTSIKAALTP KLRPPQPRKV ADQQSHHGRS RNDPYSWMEN
     LADPHLPGYI QAENDYCRKF MRQHRFLHRV VLKEMKQKLA TADHAGPLKT AAHGYEYYTT
     TSPYGLIYLR KPLGQGRHAP EQVLLNAGFL RSMNTSVRKV LLSPDHSIFA YNTEREGMEY
     GDLHLKDLDN RGRDETLEDV FNFVWANDHT VYYTMADTQL RPCQVFAHRL GTDQTEDRLV
     YEESDGTAFV DITSTKDSKY ITINSNSLSS SEIRVVDATI VPEANTLLTP TLIEPRQHGV
     EYYVDHHHDS FYILTNADGA TNFKLVKTPD AATGRAHWKN VITVAPTEKI EDVDLFQNHI
     VIYGRRDGLP MILCHDLKTQ ETHTVDLPMP FAVVSPGSNL AFDTSTLRFS LTSPFTHEST
     FEYDMTERKV KPVRVQLIRR FDKEKYTCTQ IHVRSHDNKS IPVTLIHQKN LQMNGRNPVL
     MRSYGAYGIT TDPEFRLEHF PLLERGWVIA LAHVRGGSEL GRDWYEDGKL GNKINSFKDF
     ISVAEHLITT QLTSSNSLAA MGTSAGGLLV GAMAQMRPDL FKALVLRVPF VDPLSSMLNP
     DLPLTQIEYP EWGNPTTSQE AYDWIRQYAP YDNITSQPSP AVYVTAGMKD QRVPYWQPLK
     YMARRRELLG EATSVLKVDL DRGHFGGQGE QEARLSDTAE QVVFLISQVQ TS
//