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Database: UniProt
Entry: A0A1V9YPN7_9STRA
LinkDB: A0A1V9YPN7_9STRA
Original site: A0A1V9YPN7_9STRA 
ID   A0A1V9YPN7_9STRA        Unreviewed;       618 AA.
AC   A0A1V9YPN7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OQR87736.1};
GN   ORFNames=ACHHYP_08084 {ECO:0000313|EMBL:OQR87736.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR87736.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR87736.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR87736.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQR87736.1}.
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DR   EMBL; JNBR01001424; OQR87736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9YPN7; -.
DR   STRING; 1202772.A0A1V9YPN7; -.
DR   OrthoDB; 869at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
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   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; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:OQR87736.1};
KW   Hydrolase {ECO:0000313|EMBL:OQR87736.1};
KW   Protease {ECO:0000313|EMBL:OQR87736.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579}.
FT   DOMAIN          33..147
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          327..544
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          556..616
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   618 AA;  66669 MW;  8E39966D3F0B9D72 CRC64;
     MSPTLEKLRR AFTGLVPRAL DAELTVSAAA NLRVKALLVE SEDAHGSEYV SDRNKRRAFV
     SGFTGSAGTA LVTTDKALLW TDGRYFLQAE QELSAEWTLM RQAQKDVPTV EEWLEAHLEA
     GDALAIDPLL TSVATARKLV KALGNVKAGV VVCEYQKNLV DQVWADQPPQ ALSDVYALSN
     EYTGASVADK LAALRTEIAK KGAGAMVLTA LDDIAWLFNI RGSDVACNPV VTAYALVTSD
     AATLFMDAKE LTPALLAHFG SDVQVQGYAA IVSAIEAYAA SSTAGLVLVD PAQCNVAVFS
     AIPVALRKEL PSLVMKQKAI KNEAEIEGMR QAHIRDGAAL VKFFSWLEEQ LAAGNETLTE
     VSVARVQQAF REEMDKFVSL SFETISGAGP NGAIIHYDPK EETCAAVTAA HMYLNDSGAQ
     YLDGTTDVTR TVHFGTPSAH EVHCFTHVLK AHIALATAVF PNECDGVKLD ALTRAPLWRA
     GLDYRHGTGH GVGAFLNVHE KGVLMSFKLN PTGLLISENM IVSNEPGYYE DGQFGIRIEN
     LMVAKKASGL PTTYGQFCVF ETITMCPIQR RLINTALLTA DELAWLNAYH ATVRTKLAPL
     LVGAPLAYLL KETEPLSA
//
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