ID A0A0C9YFC0_9AGAR Unreviewed; 474 AA.
AC A0A0C9YFC0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=K443DRAFT_674082 {ECO:0000313|EMBL:KIK06798.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK06798.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK06798.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK06798.1,
RC ECO:0000313|Proteomes:UP000054477};
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 (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
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 aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; KN838551; KIK06798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YFC0; -.
DR STRING; 1095629.A0A0C9YFC0; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 51979 MW; 678EAD394C9506B3 CRC64;
MMLYPSSPEA ATRFIKFVNA SPTPFHAVHN AALRLEKAGF QKIREKDSWE NEVQPGGKYF
FTRNQSALIA FTLPQKWKQG TGLSVVATHV DSPNLKVRPI SKRSKSAYLQ VGVETYGGGI
WHSWLDRDLS IAGRVVTADK AGGFTSKLVK LDRPILRIPT LAIHLDRNVN ESFKFNQETE
FIPILGLIED QFNAKLSDSD DEKDEKAPNN GAKVASSIQD NHHPALLSLL AGELSIAPEE
IHDFELSLYD TQPACLGGLN NEFIFSPRMD NLVSSFCAVE AIADVVQATS VEGNVNCIAL
FNHEEIGSVS TSGAESNLIP SLLNRLSPTP SALAQSIANS FLISADMGHA LHPNYSSKHE
EKHKPIMNRG IIIKTNAKQR YASDAISTFI VKQLVERKGG RVQEFEVRND MACGSTVGPM
LSKIGIRTVD VGNAMLSMHS IRETAGSHDI QNAIDLFSSF FEGFSALDRE LSVD
//
