ID   A0A0M4QK50_9PSEU        Unreviewed;       868 AA.
AC   A0A0M4QK50;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE   AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE   AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN   ORFNames=WY02_09825 {ECO:0000313|EMBL:ALE78681.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE78681.1, ECO:0000313|Proteomes:UP000067245};
RN   [1] {ECO:0000313|EMBL:ALE78681.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE78681.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; CP011862; ALE78681.1; -; Genomic_DNA.
DR   RefSeq; WP_062397036.1; NZ_CP011862.1.
DR   AlphaFoldDB; A0A0M4QK50; -.
DR   STRING; 445576.WY02_09825; -.
DR   KEGG; psea:WY02_09825; -.
DR   PATRIC; fig|445576.3.peg.2177; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000067245; Chromosome.
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; cd09602; M1_APN; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR012778; Pept_M1_aminopeptidase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR   PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:ALE78681.1};
KW   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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          97..189
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          234..444
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          529..843
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   868 AA;  95389 MW;  30F5557B7E4F643B CRC64;
     MTPPNLTRAQ AEERAALLDV STYDVTIDLT DGAGAPSERT FAVTTTVRFT AAEPGGSTWI
     EWVGDGITSA TLNGTGLDAA AWTEEDGLAL PGLAAENELT IVATGLYTNT GEGLHRFVDP
     VDQAVYLYSQ FETADCKRLF PCFDQPDLKA RYTLTVTAPE DWKVISNAPA TVEGGVHRFE
     RTEILSTYLV ALIAGPYASW HDTYRDEHAE IPLGIFCRAS LAPHMDHERI FTETRQGFDF
     YHRNFGVTYP FGKYDQLFVP EFNAGAMENA GAITFLEDYV FRSRVTRTLY ERRAETILHE
     MAHMWFGDLV TMRWWDDLWL NESFATWASV LCQAEATEYT GAWTTFANLE KSWAYRQDQL
     PSTHPIAADI PDLQAVEVNF DGITYAKGAS VLKQLVAYVG LEPFLAGLRD YFAAHAWGNA
     TFDDLLGSLE KASGRDLSDW GAQWLRTTGL NLLRPSFQVD EAGTFTSFDV VQGGARPGAG
     ELRTHRIAVG VYDDDPETGK LVRTHRVELD ISGERTAVPE LVGLSRGKLV LVNDDDLTYC
     ALRLDPGSLA TLVDRIGDIA ESLPRTLCWS SAWEMTREAE LKARDFVTLV AGGFDTESEI
     GVVQRLLLQA QTATASYCTP EWAQGRGWPL LTDALRFRLD TAPPGSDVQL AVVNALAASV
     LPENTLDRMK GWLLDVDVPK GLTVDADLRW RLLHALVAHG KAGETEIAEE AERDATSTGA
     RQAERARALI PTAEAKERAW QRAVHDDSLP NAINESAISG FSHPALSTVS PGLLDGYVQR
     YFDEIDGVWA RRTSELAQNV VVGLFPSWAV AEPTVAAADA WLADQSKPAS LRRLVSEGRA
     GIVRALAARE FDGQATPDPE RTTAVQQP
//