ID A0A0C9TGZ4_PAXIN Unreviewed; 491 AA.
AC A0A0C9TGZ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=leucyl aminopeptidase {ECO:0000256|ARBA:ARBA00012565};
DE EC=3.4.11.1 {ECO:0000256|ARBA:ARBA00012565};
GN ORFNames=PAXINDRAFT_103031 {ECO:0000313|EMBL:KIJ07262.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ07262.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ07262.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ07262.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; KN819959; KIJ07262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9TGZ4; -.
DR HOGENOM; CLU_013734_1_2_1; -.
DR OrthoDB; 2899215at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR PANTHER; PTHR11963:SF52; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 328..335
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 491 AA; 52211 MW; 78AAE18BB87EEFBA CRC64;
MSSKAHIIPV DPKNPGLSAA SNLNPAVLWA TLPPTQKPAK VGTSHLFYGT GGNDVTALVS
LGEGFETKQG DARREIIRKA VGSGVKSVKG LGDGVSEAIL DASTDPHAAA VAAHLALYKF
TLKTSPPSVF DPRAKGPAPE KLKISPGAHT FDWERGVVYA KAQNLARTLM ELPANIMTPT
AFTERVKEEL KGLANVEVIV RDEAWAAEKG MRTFLSVTKG TSEPAKFLEI HYKGGPNPDA
QPIAFVGKGI TFDSGGISLK PSAGMKLMRG DMGGAAAVVS SMLAIAQLKL PVNVVAFTPL
CENLPGPSAN KPGDVIYAMN GKSVEIDNTD AEGRLVLADA LYYASTEFKP HTVIDVATLT
GAMDIALGEI FTGVFTTSDE LWQQLHAAGE SEYDRFWRLP LDEDFGPQIY SSNADLCNSG
GKPGGACTAA LFLKAFVNGI ESKEGEQAAV RWAHLDIAGT MEFTRPTPYQ ETGMTGRPVR
ALVEFVRRLS Q
//
