ID A0A1V6QU91_9EURO Unreviewed; 496 AA.
AC A0A1V6QU91;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Xaa-Pro aminopeptidase {ECO:0000256|ARBA:ARBA00012574};
DE EC=3.4.11.9 {ECO:0000256|ARBA:ARBA00012574};
DE AltName: Full=Aminoacylproline aminopeptidase {ECO:0000256|ARBA:ARBA00030849};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=PENSOL_c038G09836 {ECO:0000313|EMBL:OQD92775.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92775.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000256|ARBA:ARBA00002443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000256|ARBA:ARBA00001424};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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:OQD92775.1}.
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DR EMBL; MDYO01000038; OQD92775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QU91; -.
DR STRING; 60172.A0A1V6QU91; -.
DR OrthoDB; 1377484at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF3; XAA-PRO AMINOPEPTIDASE AN0832-RELATED; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 36..166
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 496 AA; 55805 MW; 8B33EB60496C1543 CRC64;
MRATRATQGS TAQDVMINPL DSYNIRVVTP TSCDKYPAKH HARNVARKLG ASSGLIFLSG
QPTINLRDSD QSRPFRQRRY FYYLSGVDEP DCSLTYDIGQ DLLTLYVPDF DLHRAIWMGP
TLSREDAQDK YDVDHVRYRA SLKYELQVWL DERKQGSELY LIHDSEKPEH LPKDLPLDLE
QLGPAMDAAR GIKDEYEIRM IRQANKVSGL AHRRILESIQ TMSNEAQIEG SFLNTCISHG
ARNQAYQIIA ASGPNAAVLH YDRNNETLNK KPLVCLDAGA EWNCYASDVT RTFPLTGEWP
SDYVRDIYKI VERMQEETIR LIRKGVRYLS LHDLAHDIAI EGLLALGVFK NGTNLEIRQS
GASKVFFPHG LGHHVGLEVH DVSERSIMAL HRGFDQLQYR PILNSTCLSP CTLSAPLLEE
GMVVTVEPGL YFSPLAMANA RHQPFARYIN FDVAEKYVHI GGVRIEDDIL VTATGYENLT
TAPKGEEMLA IIGGSA
//
