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Database: UniProt
Entry: A0A395NDK1_TRIAR
LinkDB: A0A395NDK1_TRIAR
Original site: A0A395NDK1_TRIAR 
ID   A0A395NDK1_TRIAR        Unreviewed;       583 AA.
AC   A0A395NDK1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase P {ECO:0000256|ARBA:ARBA00020658};
DE   AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN   ORFNames=TARUN_8091 {ECO:0000313|EMBL:RFU74176.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU74176.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU74176.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU74176.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU74176.1}.
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DR   EMBL; PXOA01000564; RFU74176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NDK1; -.
DR   STRING; 490622.A0A395NDK1; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 2.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 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:0000313|EMBL:RFU74176.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:RFU74176.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT   DOMAIN          29..130
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          382..509
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          520..582
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   583 AA;  64482 MW;  84E9313E93062731 CRC64;
     MFKYMLTIVS SSVVPSEDSH SSEYIASCDA RREFISGFTG SAGCAVITED AAALATDGRY
     FNQAAQQLDD NWTLLKQGLQ DVPTWQEWAA EQSAGGKTVA VDSTLVTGSA AKKLAEKIRK
     SGGSDLVPLD VNLVDKVWAA DRPPRPQQRI TVLSEKFAGK SVQSKLSDLY AELEKKRSPG
     VFISMLDEVA WLFNLRGNDI PYNPVFFSYA VITPKGAALY VDESKLDEEC RAHLAKYDVA
     VKPYETFFRD AEQLHQQFVA STENQEGDSA GSFLMSNKGS WALKRALGGD TGVEEIRSPV
     GDAKAVKNET EMEGMRACHI RDGAALIEYF AWLEDQLITK KAVLDEVQAA DKLEELRSKH
     EHFVGLSFPT ISSTGAKWRL RAQYLDGTTD TTRTLHFGEP TEAEREAYTL VLKGNIALDL
     AIFPKGTTGF ALDSLARQHL WRAGLDYRHG TGHGVGSFLN VHEGPIGIGT RIQYTEVPLA
     PGNVISNEPG YYEDGRFGIR IENIIMVKEV QTKHAFGDKP FLGFEHVTMV PYCRNLIDES
     LLSQAEKAWL NASNAEILEK TKGFFEGDAL TTAWLTRETR HIE
//
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