ID   A0A1D7YFD8_9ACTN        Unreviewed;       859 AA.
AC   A0A1D7YFD8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=BFF78_27685 {ECO:0000313|EMBL:AOR34327.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34327.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017248; AOR34327.1; -; Genomic_DNA.
DR   RefSeq; WP_069780881.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7YFD8; -.
DR   KEGG; spun:BFF78_27685; -.
DR   Proteomes; UP000094960; 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:AOR34327.1};
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          116..191
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          241..451
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          534..844
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   859 AA;  95365 MW;  446E1C4A712E35C6 CRC64;
     MPGENLSREE ARERAALLSV DGYDVSLDLR SAVGDGEGEP RTFRSVTTIR FRCNEPGASS
     FADLIAPSVS AVSLNGRDLD PGEVFDGARI ALEDLAAENE LVVDARCAYS RTGEGLHRFV
     DPEDGEVYLY TQYEPADSRR VFANFEQPDL KAPYRFEVQA PEGWTVWSNG TGERADGVWK
     FAETKPISTY ITCVVAGPYH YVTDSYTRTF EDGTKLEIPL GAMCRKGLAP HFDADDVFLV
     TKQGLDFFHD HFDYPYPFGK YDQAFVPEYN LGAMENPGLV TFREEYIFRG KVTQASYEGR
     ANVILHEMAH MWFGDLVTME WWDDLWLKES FADFMGTFAN VGATRFKDAW ITFANRRKAW
     AYRADQLPST HPITADIRDL EDAKLNFDGI TYAKGASVLK QLVAYVGQDA FLEGARRYFK
     RHAYGNTRLG DLLSVLAETS GRDMSAWARS WLQTAGVNAL TPQVLLDAEG RVAELAVVQE
     APESHPEERP HRIAVGLYRR TPEGALERYA RVETDAHEPR TVVAELAGAE APELVLVNDD
     DLTYCKIRFD ETSLDTLRAH LGLLTDPLAR ALCWSALWNM TRDALLPARE FVDLVLRFGG
     RESDIGVLQM LHAWANSALV HYAAPQWRAT GGELLAEGAL RELRAAEPGS EHQLAWARFF
     ATVAAAEPDL KLLGDLLDGT TSIDGLEVDQ ELRWAFLEPL AAHGAADESV LAAELARDDT
     ASGKRHQVRC LAARPSAAVK AQAWAQVVES DALSNALVEA TISGFGQPSQ RELTAPYAQK
     YFAAIERVWR ERSIQIGMDV VRGLFPALQD RPETLQATDA WLAAHRDAAP ALRRLVLEAR
     DDLARALRAQ ECDATAITG
//