ID   A0A1Y2HRZ1_9FUNG        Unreviewed;      1171 AA.
AC   A0A1Y2HRZ1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Prolyl endopeptidase-like {ECO:0000256|ARBA:ARBA00039290};
DE   AltName: Full=Prolylendopeptidase-like {ECO:0000256|ARBA:ARBA00042165};
GN   ORFNames=BCR44DRAFT_1044451 {ECO:0000313|EMBL:ORZ37367.1};
OS   Catenaria anguillulae PL171.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX   NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ37367.1, ECO:0000313|Proteomes:UP000193411};
RN   [1] {ECO:0000313|EMBL:ORZ37367.1, ECO:0000313|Proteomes:UP000193411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PL171 {ECO:0000313|EMBL:ORZ37367.1,
RC   ECO:0000313|Proteomes:UP000193411};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORZ37367.1}.
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DR   EMBL; MCFL01000013; ORZ37367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2HRZ1; -.
DR   OrthoDB; 7264at2759; -.
DR   Proteomes; UP000193411; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
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; 2.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193411}.
FT   DOMAIN          300..721
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          827..901
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   DOMAIN          926..1034
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  126102 MW;  D817902AD60CD8A1 CRC64;
     MPPKVKATYI RSASPSPSRD PNAPLMPGGI RPVNPITSTT TAPFSSPPAG HRGGQGESIP
     LQASPPRQQQ QPRQQHQANL LPPGDDLSKR PSPISTAPPV AQKSAAVKAD AALVTHSQDN
     ISKGGGGQTV TFGKDHVDYN DDDADDDYDE ESDDDDRHGL TSHSTSSRFR SSPSTSASRR
     PRYSSLHSTG AYAHGGRLPD RVIDPDELLA NPPGYSRLAS YLPWWLPPRV LLFVLTGALI
     VGVTLSFTLR KIHNRLVVAH CIPVAPRNAT AQPRYLPDLP APLPPDPWAE MIAGTALLDA
     HVARENTYFD GMTADLASLR SELVSEINAR GASSAGGGNP PLEHWRHTDG MYYALRADLA
     AYVRAPVREA LATDAAEKIV YLRALLRLRL NDELPAIGFF EVSPDGSHLA LAVDRSGNER
     FDVYVWDVVH QRRVGTGLAA KDAYYTARWV SNSVLVASVV DALGVPRGAV RIAVEGAGGA
     APTTTMVQVY WEERPERTLN VGASADGSML VLQSAGQISQ RPRVVSAEAM GAADWTPDQM
     SSLTATVGDD DADEYGISEV EHHQGYLYVR TNEALPDRVA PNLNMFEVVR LPYDTRFPTN
     VTRAQLANAE RIWAHSPGIF VEKMEVLQRY LVLWVRTNGR REIRWRAIGL GVSDPSWKRL
     GEWDSLAFYS VTPGFASDIG DPSSRVYRRF DASAIEFSNS SLVQPQAMWE LDLAGGGVVP
     VVAEQASAID PTRYARFRVW VNAATLSVSG QLPPSSFFAN PAGGDYVPVD LAWRYADGEQ
     VPQGKTRDGS TPLWVRTPGT PARPTLVSAY GAYGTMNDAS YDPGLLALMD RGVVVALLHP
     RGDGDLGPAW YHAGARMHKA NTMVDVERAI AGLINAGVAE KEKVALMGRS AGGLVVGSAV
     AATFQTCGQR ATGTNGRALW SGLALVIAQV PFIDLVADMA DVSVPWTTYE HREWGDPRNA
     TELAYLANLS PYDRLNVDLD RGACWGTVAN RTLDDNADDD PTMPWPAVVV TTGKNDARVP
     YSEPVRWAAR MRHVQALAFG AVAVSNSTAT SGGGGRGAVA TAEQVGSEQD VGGRRSSAFS
     DPIAPEWASS AAKRVVSQPH GGLQVRDAIN PSSKAKCRET TDITKDRPVL VRVYSGGHFS
     GKDAAGEAEW MSIALQVFGL WTPPESLPKR K
//