ID A0A1H5LY42_9ACTN Unreviewed; 495 AA.
AC A0A1H5LY42;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN05216489_08421 {ECO:0000313|EMBL:SEE81417.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE81417.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SEE81417.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SEE81417.1,
RC ECO:0000313|Proteomes:UP000198754};
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; FNTK01000001; SEE81417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5LY42; -.
DR STRING; 1855348.SAMN05216489_08421; -.
DR Proteomes; UP000198754; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198754};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..495
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011645263"
FT DOMAIN 50..219
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 312..455
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 495 AA; 53609 MW; B60C4AAF8E1A666D CRC64;
MHRRIIAPGA LAAASLLLAI PASAASYSPG APGIGDPYYP AYGNGGYDVS HYDLRLQYQP
ATDELAGTAT ILAKTTQDLS RFNLDFLLDV SEVRVNGVKA TFATSGQHEL EITPKTPLPT
GTPITVVVRY SGVPSTKSAY GFNTWHRTPD GAVAADEPES AWWWFPSNDH PSDKATYDVS
VAVPNGTQVI SNGTLQSTSS QLGWTRYNWR ENKPQATYLA TLAVGRFDIT TSTSEGGVPV
INAYSKDLGD NDGSARASVE RTGEIVDWLS GYFGPYPFSS AGGYVPNTTT GYALETQTRV
YYSQRQFANG INTSVVVHEL AHQWYGDDVS LKGWKDIWIN EGFARYAQWL WSEHEGEGTA
QQLADYVYAS HPADDAFWTI APGDPGPDNQ FELPVYDRGA LAIQALRNEV GDDAFFAILK
GWPKEHAYGN ASVADFRAYA EQVSGKSLGA LFDTWLFQPT KPAAPAARTA SIARAGAAPV
QPKSWKKIGA TNSVH
//