ID   A0A165E7I3_9BASI        Unreviewed;       647 AA.
AC   A0A165E7I3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:KZT54265.1};
GN   ORFNames=CALCODRAFT_500098 {ECO:0000313|EMBL:KZT54265.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT54265.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT54265.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT54265.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV424018; KZT54265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165E7I3; -.
DR   STRING; 1353952.A0A165E7I3; -.
DR   InParanoid; A0A165E7I3; -.
DR   OrthoDB; 2785676at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR43056:SF5; ACYL-PEPTIDE HYDROLASE; 1.
DR   PANTHER; PTHR43056; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZT54265.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   DOMAIN          438..643
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   647 AA;  69536 MW;  15CC345604F379D9 CRC64;
     MPPTVAPYGS WKSPLTVEAI TSSATSLVAL AADPSTHAIY ALESRPAEGG RSVLVQRSLA
     DPAKVKDVFG SGWNARTGVH EYGGGAVWAE GGVVYFSDYG SGRVYTVKDG QLEAFTPENK
     DLRFADFRPH PKDPSILASV MEDHAHPAPA DVVNSIVLLR RGEPPQPVVT GADFYSSPRW
     SPDGKWLTWF QWVHPNMPWD GGLLQLAPVT ASPSGISVGP PKTIAGKEGE ISVAEPVWLS
     PTRLLFQSDV SGFWNPWLYD VTTGHAGPVL PQPISEECAT PHWTFGNSSL AVLGPETALV
     ISVDQGIDRL NLLTLGSSPT FKRLDVPFVA MAQLWSLSDT KAVMLGATDT TPLSLILLTL
     KGDSVTYETL SKPANLDLSP ELFSAAQPRT LTTPDGPVHV LYYPPKNPEY VAPEGEKPPA
     LVSVHGGPTG AAHAGLSLGV QFFTTRGYAW IDVQYGGSTG YGKAYRDLLN GEWGIVDVRD
     SAACVAALGE AGLIDTQRVG IRGRSSGGFT VLAALCDYPD VYTAGVSLFG ISDLKALATD
     THKFESRYGD KLLGGTVDEI PEVLRDRSPI YKAEKIKAPL LLLQGSIDPV VPPNQAELIL
     QKIQERGGKV DMVVYEGEGH GWRKAETMKD AAEKELAWYE EVWGLKQ
//