ID J4GD55_9APHY Unreviewed; 481 AA.
AC J4GD55;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=FIBRA_07006 {ECO:0000313|EMBL:CCM04813.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM04813.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM04813.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM04813.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797169; CCM04813.1; -; Genomic_DNA.
DR RefSeq; XP_012184096.1; XM_012328706.1.
DR AlphaFoldDB; J4GD55; -.
DR STRING; 599839.J4GD55; -.
DR GeneID; 24099724; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR InParanoid; J4GD55; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000006352; 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:UP000006352};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 481 AA; 53049 MW; 15C760E96EA39078 CRC64;
MVQLPTPDYP SEIPLPLTVH QMTVPEAVSR LLSFVNSSPT PFHAVQVAAL RLENAGFSKL
RERDDWERTL QGGGKYYMTR NQSCILAFTV PPKWKPGVGV SIVGTHIDSP NLRVRPVSKR
TKAGYLQVGV ETYGSGLWYT WFDRDLSLAG RIILKEKHGG FVSRLVKINR PILRIPSLAI
HLDRGAADKF SFNQETEMVP ILGLVENELN SASTSSKITS GVQENHHSSL LALLSQELSV
SPEDIHDFEL HLYDTQLSQL GGLNEEFVFS PRMDNQFSSF CAVDAIVNFA ESRSYSTFQG
NVNCIVLFNH EEIGSVSTTG AESSFILSLL NRLSPTPGTL AQSISRSFLI SCDMTHALHP
NFMSRHEDNH APMINGGIAI KINAKQRYAT DAIGSLIIKQ LAEKKGGKVQ YYEVRNDMVC
GSTIGPALSK TGIRTVDVGC PMLSMHSNRE TAGTRDVQSA LDLFTAFFES FAELDQTLPV
D
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