ID A0A165S6C5_9APHY Unreviewed; 471 AA.
AC A0A165S6C5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=DAEQUDRAFT_724122 {ECO:0000313|EMBL:KZT71588.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT71588.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT71588.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT71588.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429045; KZT71588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165S6C5; -.
DR STRING; 1314783.A0A165S6C5; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 471 AA; 51572 MW; 201FF21B45BC8C79 CRC64;
MFNSAVPEAA TRLLQFVNAS PTPLHAVAAA ALRLEKAGFR KLREKDDWES DLKDGGKFYV
TRNQSCILAF TVPQKWKPGG GVSIVATHVD SPNLRVRPVS KKAKAGYLQV GVETYGGGLW
HTWFDRDLSL AGRIILKDKN GGFTSKLIRV DRPLLRVPSL AIHLERGSEN NFTFNQETEM
LPILGMVEEQ LNAPTDKKST TEVKVSGVQE QHHAALLEVL SQELSVVPED IHDFELHLYD
TQPSQFGGIK NEFIFSPRMD NQFSSFCALD ALAAFSASSS YSAYSSSPSN NVNAIALFNH
EEVGSVSTTG AESSLLPSLL SRLSPAPSAF SQTIARSFLV SADMTHAVHP NYMGKHEENH
APKINGGVVI KTNAKQRYAS ETVGRFLLKR LVEKRGGKVQ EYEVRNDMAC GSTVGPGLSK
MGVRTVDIGC PMLSMHSIRE TAGTHDAQSL IDLFTSFFEG FAELDNELVV D
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