ID A0A1F5LNZ0_9EURO Unreviewed; 465 AA.
AC A0A1F5LNZ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Probable Xaa-Pro aminopeptidase PEPP {ECO:0000256|ARBA:ARBA00039424};
DE EC=3.4.11.9 {ECO:0000256|ARBA:ARBA00012574};
DE AltName: Full=Aminoacylproline aminopeptidase {ECO:0000256|ARBA:ARBA00030849};
DE AltName: Full=Probable Xaa-Pro aminopeptidase pepP {ECO:0000256|ARBA:ARBA00039164};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=PENARI_c005G02540 {ECO:0000313|EMBL:OGE54934.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE54934.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE54934.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE54934.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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}.
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:OGE54934.1}.
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DR EMBL; LXJU01000005; OGE54934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LNZ0; -.
DR STRING; 1835702.A0A1F5LNZ0; -.
DR OrthoDB; 1377484at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
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 PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF1; XAA-PRO DIPEPTIDASE; 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.
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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT DOMAIN 12..146
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 465 AA; 51083 MW; 059D832638C3387C CRC64;
MTTVDTILAA KYPAKAHARR VAESIKIRHG GAGAIYLEAQ KTRLIEDSDE AMPFRQRRPF
FYLTGCLLPD AAVVYDAVAD QLTLFIPPID PESVIWSGLP LSPEEAAKLY DVDRVLFTTD
VNSTLASIAS THNGQTTAFA IAEQVSGETK FEGFAEINIS TLKSTIEDTR VVKDAYEVAL
LRKANDISAK AHIAAIKAAK TATNEREIEA AIIGACIANG CREQSYHPIV AGGEGGATLH
YVRNDVDLVD PATGKRKNNV LIDAGGEYQT YCADITRVIP LGGRFAPETR QIYEIVLQMQ
TECIAMLKEG VCWDDVHALA HRIAIRGLLK LGILRGSEEE LFEKRVSVAF FPHGLGHYLG
MDTHDTGGNP KYDDKDTMFR YLRVRANLPA GSVITVEPGI YFCRFIIDPV LKAPETGKYI
DTEVLERYWS VGGVRIEDNI HITKDGSENL TTAPKIIEEV ESLAL
//