ID A0A409WMV5_PSICY Unreviewed; 1108 AA.
AC A0A409WMV5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF00326};
GN ORFNames=CVT25_002988 {ECO:0000313|EMBL:PPQ79834.1};
OS Psilocybe cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ79834.1, ECO:0000313|Proteomes:UP000283269};
RN [1] {ECO:0000313|EMBL:PPQ79834.1, ECO:0000313|Proteomes:UP000283269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2631 {ECO:0000313|EMBL:PPQ79834.1,
RC ECO:0000313|Proteomes:UP000283269};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00004576};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004576}.
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:PPQ79834.1}.
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DR EMBL; NHYD01003360; PPQ79834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409WMV5; -.
DR STRING; 93625.A0A409WMV5; -.
DR InParanoid; A0A409WMV5; -.
DR OrthoDB; 1655369at2759; -.
DR Proteomes; UP000283269; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000283269};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT DOMAIN 2..89
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 175..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..976
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 119142 MW; 23F270F8DA774E84 CRC64;
MSSKVVEADA KIHSLAMAVA PVTSWKLYDS IYTERYMNLP ELNEGGYVNA SISNVEGFKK
VDYLLAHGSG DDNVHYANSA HLLDMFTREQ LSNCTMAAAC CSSSACHSHS ASSSASSSSS
CSPYSREDSV LNAMSIDFPA AQTAASTSAA ATATRAQATR LARPRGLWKA RGTLASKLGH
ASDNTTPPTP PTSITRRYHD PAAAAAPDSA PADSHSDRWH SPDPFSECEY DSDSSAASLS
RHQHFNLYLN GQIFPPPPAS SAKRRRRDLD SPPTSLDERD SEEIIYWDYS RKCTPNLPDS
EKDWTRSKLM DTSAISGSLI GPMSPGAIEA AAAAERASTD LEDWEDLKEL FAKAAEMYES
QSPSETLPLL RGVIHECHRF LQMYQDPSVV YTSPLPNNRA PTPPAVDKKI INDWLLAERL
HAQHQAESSK TDNSTAAPST TTPAEKKCKC KDLPTAFYTV LGTTLFFFGN IVDASPSLCM
LGEPANPVVY WLCALDAFEI GESLPVRTSG GVRNGKGDYF SSGGSGGTTS SRSAYHARAI
GATPPPEDWR MAVVWGRTLV CIAEEVVRRQ SERAKQGLPP RQPQNAQLSF ALAPGMQLAG
YAEMVPLAPT MPTSPSAFPV QQQLAAARAA EAQKEADPNM DSPVWPANSP FGAIVSRRPA
LPSRLSLESG VTPHELLLLA QDQFSRGILH MPHPQHLVHA RFAGGSTRGS EQPRMHAAVP
DSFLFTPALG PSMSYETNTR SASSHSSHSS SRNTALTSPP TTASSSSSAS ASTSPPSHTP
ITVETFSRAK ELYTIAYEVL LLSEKLDLAS ERQTWAQWAD SVFSQMKMEA DTDAWRGHIT
AARGRCCVVI GSALAEGVEG RLERAAGTTG GDDDDAMGGG RKKRKAGDEN GEGEGEKETE
AEILESEDAR EAREVLVEAI GYLERAKEVF EARKLEAQEQ ASRGGAEERQ EEEEEGMIVI
EDADDEDEEE DSDGIVADDS SATPTPANAS RPASGSGGAA STPISHLRVP VLPSNKVSTS
TQTTTTTPKN AHPPASSNPN PMTSGGPVTA EDEVEELKTL LAEALLSLAN LTADVSEREK
LYARAQKEGG DKFELDEWDE EDRMDESD
//
