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Database: UniProt
Entry: A0A285JKF9_9ACTN
LinkDB: A0A285JKF9_9ACTN
Original site: A0A285JKF9_9ACTN 
ID   A0A285JKF9_9ACTN        Unreviewed;       399 AA.
AC   A0A285JKF9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SNY60297.1};
GN   ORFNames=SAMN05421748_12191 {ECO:0000313|EMBL:SNY60297.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY60297.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY60297.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY60297.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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DR   EMBL; OBDY01000021; SNY60297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285JKF9; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000219612; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:SNY60297.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219612}.
SQ   SEQUENCE   399 AA;  42906 MW;  FDBBB33B0978F89B CRC64;
     MSLVERFADL VVRVGVNVQP GQGVVVRSDT AHLEIARAVV AAAYGAGAGW VEVDWDDGPI
     RRQAVDHQTL EQLTANRPWA LERTEWWRKE GVAFIRLMGD ADPHLLDGAD PAKAAAIPVQ
     ESQAMRRALF DGVRWTAVGA PNPGWARQIF GEPDMDRLWE AVGTAMRLDA GDPVEAWRER
     SATLGERARR LDELELTEVR YVGEGTDLTV GLLPGTRWTG GGLVDPAGVP YMPNIPTEEV
     FTSPDKSRAD GVIRLTKPLV LGGALVTGLR VTFAGGRITE VTADSGADVV RAQLDSDAGA
     RSLGEVSLVD RDSRIARAGI VFHNTLFDEN AGCHVAWGQS FPFAIDGGLA LSEKQRAEAG
     LNMSSVHTDV VIGGDGITVT GRGPKGVVEI IREDEWVLD
//
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