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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//