ID A0A316YG86_9BASI Unreviewed; 694 AA.
AC A0A316YG86;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative aminopeptidase P, cytoplasmic {ECO:0000313|EMBL:PWN88116.1};
GN ORFNames=FA10DRAFT_268339 {ECO:0000313|EMBL:PWN88116.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN88116.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN88116.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN88116.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(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}.
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DR EMBL; KZ819638; PWN88116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YG86; -.
DR STRING; 215250.A0A316YG86; -.
DR InParanoid; A0A316YG86; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000245768; 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:SF21; X-PRO AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43763; 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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:PWN88116.1};
KW Hydrolase {ECO:0000313|EMBL:PWN88116.1};
KW Protease {ECO:0000313|EMBL:PWN88116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..694
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016341662"
FT DOMAIN 88..223
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 402..617
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 630..691
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 77039 MW; 71B2DAD26115C8E6 CRC64;
MVLLLRRPLL FHLRLQAAAA RPSTASSLST IALARTSVQS ALRARLGDQS VIARPFSRSS
LHNHNHHHHH QSDKMGAVSQ GKVDTTQRVA TLRDLMDKHG LEAYVVPSED AHASEYPAES
DLRRGYISGF SGSAGCAVVG KKEAALFTDG RYFLQAGQQL QPDVWKLMKQ GEANVPTWQE
YLSKNVGPKS KIGMDPTLIS AEDARSISAD LESVGSELVG VEENLVDQVW GSQRPKRPSE
TIFVLDEAIA GRSAADKIQD VRNEIKGKGS HLKGYVANML DEVAWLFNLR GSDVPYNPVF
FAYTIVLLDK VLLYVDATGQ MDQKTRDYVT STGAEIRPYE NFYSDLKAIG NEVLGQDDKV
LIGKKASLAV QEALGGASKV LIDRSIIVDQ KSIKNKVEIQ GFRDSHIRDG AALASFFAWL
EEQLVSGQKI SESRAADELE NCRKKQDKFR GPSFTTISST GSNGAIIHYS PNPADCPDID
PKQLYLCDSG AQFTDGTTDV TRTWHYGKPK DEEIRAFTRV LQGHIAIDRA VFPQGTTGYL
LDPLARRPLW QDGLDFRHGT GHGVGHFLNV HEGPQGIGTR AVFNETSLKE GMILSNEPGF
YKDGSWGIRI ENLVVVKKAE TRNNFGNKGY LGFEHLTLCP YQINLIDQSL LYQDERDWIN
AYHDETYEKV APLLEKMGDR RGLDWLKRHC SARV
//
