ID   A0A1I0XKS5_9ACTN        Unreviewed;       850 AA.
AC   A0A1I0XKS5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=SAMN05192575_102454 {ECO:0000313|EMBL:SFB00920.1};
OS   Nocardioides alpinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=748909 {ECO:0000313|EMBL:SFB00920.1, ECO:0000313|Proteomes:UP000199113};
RN   [1] {ECO:0000313|EMBL:SFB00920.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFB00920.1};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOKC01000002; SFB00920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0XKS5; -.
DR   STRING; 748909.SAMN05192575_102454; -.
DR   OrthoDB; 3885507at2; -.
DR   Proteomes; UP000199113; 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; 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:SFB00920.1};
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          107..194
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          236..449
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          532..839
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   850 AA;  94031 MW;  7E4BBBA0CAEBCB4D CRC64;
     MPGTNLTRDE AATRAALLDV TAYAVDLDLT GAIRPDQATF TSVTTLEFSC HQPGSSTFAD
     LVAPTVREIT LNGRSLDPAT AYVDSRIALD DLEASNTLVV TADCAYSNTG EGLHRFVDPV
     DDRVYLYSQF EVPDARRVFT TFEQPDLKSV FTFTVTAPSH WVVVSNAATP EPVEKDGGAS
     VWSFPTTKKM STYITAIVAG EYHGEFDTYE GKFGTIPLGH YCRQSIKEHM DTAALVELTK
     QSFAFFEEQF DYPYPFGKYD QLYVPEYNAG AMENAGCVTL RDEYLPRSRQ ARSFFEFRAS
     VITHEMAHMW FGDLVTMKWW DDLWLNESFA EWACYWCEAN ATEFDDAWTG FANARKQTGY
     RADQLPSTHP IAADNVDLHA VEVNFDMITY AKGASVLKQL VAWVGIDPFL EGLRAYFKEW
     EYGNPEFKDL LATLEKASGR ELEGWAQEWL QTAGVNTLAP SFELAEDGTY ASFDVAQSAH
     PAWPTLRRHR LGIGLYDEVD GKLVRRDYLE IDVEGASTAV PELVGVKQPA LLLLNDEDHA
     YAKIRLDERS LATAISALAT FEDSLPRALV WGATWDMTRD GEMRTRDWTD LVLANIGHES
     DAWAVTRIPS STALAVNFYS DPAHRDELRA TWESGLRELL LAAEPGSDHQ LTFVRSYAGA
     AHSAGALDDL IGLLDGSFTV EGLAVDQDMR WTLITALARA GRFGDAEIDA ELEVDKTISG
     KEQAAAARVA QPTAEAKEAG WNAVLDPATP NETSREIAFS IFRFGQEDVL EPYLEKFLDA
     AETLIDTIGF HKASAVLEYG FPKPLGSAAT LARLDEWLAD NDAPKGAQRY VGEARAEVAR
     ALAAQEHDGS
//