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Database: UniProt
Entry: A0A3M2T5U3_9EURO
LinkDB: A0A3M2T5U3_9EURO
Original site: A0A3M2T5U3_9EURO 
ID   A0A3M2T5U3_9EURO        Unreviewed;       623 AA.
AC   A0A3M2T5U3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Proline iminopeptidase {ECO:0000313|EMBL:RMJ25159.1};
GN   ORFNames=PHISP_03986 {ECO:0000313|EMBL:RMJ25159.1};
OS   Aspergillus sp. HF37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ25159.1, ECO:0000313|Proteomes:UP000272442};
RN   [1] {ECO:0000313|EMBL:RMJ25159.1, ECO:0000313|Proteomes:UP000272442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF37 {ECO:0000313|EMBL:RMJ25159.1,
RC   ECO:0000313|Proteomes:UP000272442};
RA   Tafer H., Lopandic K.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:RMJ25159.1}.
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DR   EMBL; RAQS01000136; RMJ25159.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2T5U3; -.
DR   STRING; 1960876.A0A3M2T5U3; -.
DR   Proteomes; UP000272442; Unassembled WGS sequence.
DR   GO; GO:0008233; F: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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SMART; SM00674; CENPB; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS51253; HTH_CENPB; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272442}.
FT   DOMAIN          61..136
FT                   /note="HTH CENPB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51253"
FT   REGION          42..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  70637 MW;  3C9113A0F1D60E4B CRC64;
     MSAAHVEAED RLKNAMDAYE RDNTLRITDL AREFGVPYPQ LYHRAKVKPK RTTQSKKDSS
     KYNGARHALN RRQEDEVRQW RDQLDSAGHP PTGEQLRLCA NSILREQHTD PDSPPPTVSK
     MWAYRYLKRH PRQSLPPGTL PVTRPVTRRP PATLLHPASP MAAKLIDRRV HNVPGKLRIS
     ELFFDVPVNH SKPDDGTLRL FARSVSRLNT TIDPEPSSNK QLPWMVYLQG GPGMGCRAPQ
     DYGWIGTVLD KGYQILFLDQ RGTGLSSTIT AGTLFRQGNA VKQAEYLKNF RADSIVRDCE
     AVRHCLTADY PNDKRKWSVI GQSFGGFCAV TYLSKYPEGL REAFLCGGLP PLVNGPDEVY
     AHTYGMLDLQ PSLRTGLISE DKVEQRNEAY YAKFPEDVER IRRIVQYLKE NQIPLASGQL
     TPERFQQLGI LFGMHGGLDS IHDIVLRAWN DLETFGGFTL PTLNTIDGYG GFDNNVIYAI
     LHEAIYCQGQ ASNWSAHRIR SSNPRFQVDS DQPLFFTGEM IFKDMFGSYT ELNRIKEAAD
     ILASTSDWPV LYNEDQLATN KVPVYAASYI DDMYVHFELA SRTAAKIKGI KQFITNVMYH
     DALRSKSDEL MRQLFALRED SID
//
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