GenomeNet

Database: UniProt
Entry: A0A1Y2DQM8_9PEZI
LinkDB: A0A1Y2DQM8_9PEZI
Original site: A0A1Y2DQM8_9PEZI 
ID   A0A1Y2DQM8_9PEZI        Unreviewed;       510 AA.
AC   A0A1Y2DQM8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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};
GN   ORFNames=BCR38DRAFT_440612 {ECO:0000313|EMBL:ORY61602.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY61602.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY61602.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY61602.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY61602.1}.
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; MCFJ01000010; ORY61602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DQM8; -.
DR   STRING; 1141098.A0A1Y2DQM8; -.
DR   InParanoid; A0A1Y2DQM8; -.
DR   OrthoDB; 1377484at2759; -.
DR   Proteomes; UP000193689; 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   PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 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:UP000193689}.
FT   DOMAIN          92..228
FT                   /note="Aminopeptidase P N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01011"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  56167 MW;  5131907C56137805 CRC64;
     MKPRKLPSWR PLEQQVKRQA SSLPSPCPRS ARPQPPTSTL YRCPSPAVAR TQPSLPSIRS
     YSSVPASQLL FGQPVHETHP HLLQAGELTP GITAQEYHDR RSRLLSSLPP NSAVLLPSAS
     VQYRSGAVFH AFRQETGFLY LTGFSEPESL ALLVKTGPEE GDFTFYLWCR PKDPKAEQWH
     GPWSGIDAAR DVWNADEALD FARVEQGLVE ALKGVSKIYT DGELSKYGVP TKIGNMLRQV
     APGISIAPLR PVLNTIRALK SPAEIACMRK AGQASGRALT NAMRRGWKYE KDIAAFLDYE
     YHQAGLDGPA YIPVIAGGPK ASLIHYTLNN GSLRDDELIL VDAGGEYGTY ITDITRTWPA
     SGKFSPAQRD LYEAVLKAQR SSVSLCRASA NVTLDKLHSI TETTLRDQLQ RLGFEVGGNA
     MDLLFPHHVG HYIGLDVHDV PGYSRGITLR EGHCVTVEPG IYVPDDERFP KHFRGLGVRI
     EDSIAVGDDN PFTLTTEAVK EVVDIEALRD
//
DBGET integrated database retrieval system