ID A0A1I4VJH9_9ACTN Unreviewed; 480 AA.
AC A0A1I4VJH9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN04487980_1009195 {ECO:0000313|EMBL:SFN01341.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN01341.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFN01341.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFN01341.1,
RC ECO:0000313|Proteomes:UP000198530};
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}.
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; FOUV01000009; SFN01341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4VJH9; -.
DR Proteomes; UP000198530; 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; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..480
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011595632"
FT DOMAIN 56..228
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 319..470
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 480 AA; 52292 MW; CC4DFC4FA9CA7B10 CRC64;
MSRSARVVPA ALLTVALALT LTSCTDGGGE AERAKGSAGL RDPYFPRLGN GGYDVTHYAL
TLRYDPDARA RLRATAVVTA RATRDLGSFN LDLKGMDVQS VAVEGAAARW KRAGQELTVT
PEQGLDDGET FRTTVRYSGT PVTITDPDGS REGWLPTADG VLALGEPTGS MAWFPGNHHP
SDKAAYDLTV TVPEGLGAVS NGELRSESTR DGRTTFSWHT AEPMASYLAM LAIGEFEIRR
STVGGRHRLP VYVAVDPSQA EESRAVLGRI PEVVRWAEGN FGPYPFSSTG AIVDRPEDAE
YALETQNRPV FPGAPDLSLL VHELAHQWYG DSVTPKSWRD MWLNEGFATY AEWLWEEDHG
GDSAQETFDA LYEGDYFQDA ADDEAVWDFP PAKPPSAARI SDSPVYERGA MVLHKVRRAV
GDDAFFELIQ GWATAHRHGN ADTADFTDYA EEFAATAAPD ADLTPVWEDW LYGDGKPPKA
//
