ID A0A2T7SMX7_9ACTN Unreviewed; 511 AA.
AC A0A2T7SMX7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=Y717_12865 {ECO:0000313|EMBL:PVE04250.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE04250.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE04250.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE04250.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVE04250.1}.
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DR EMBL; AZSP01000392; PVE04250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7SMX7; -.
DR STRING; 1440053.GCA_000718095_00937; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000245992; 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 ECO:0000313|EMBL:PVE04250.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:PVE04250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245992};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..511
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039691320"
FT DOMAIN 104..213
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 309..458
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 466..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 56415 MW; 48FCA503E6F6D24E CRC64;
MLLTNRRLRA ALLAAASATL VAATLPAPEP LGIGDPLFPR LGNPGYDVLT YDLDFTYGGD
NRKPLDAITK IDALATQRLQ RINLDFTHGK VRSVEVNGAA ARFATAGEDL VITPAAAVED
GSRMRITVSH TSDPTGNRGG WVRTSDGLAM TNQADAAHRV FPGNDHPADK AYFTIRITAP
QRLTAVANGV QEGKARRGAT TTWTYRTHHP MATELAQVSI GDSAVVRRQG PGGLPVRDVV
PAADRQKLEP WLKKTPGQIG WMERQVGPYP FETYGVLIAG ADTGFELETQ TLSLFERALF
TEPGYPEWYV DSVMVHELAH QWFGDSVSPR RWADLWLNEG HATWYEMRYA QEYAGKSMET
RMREAYQQSD GWRAAGGPPA SPKPPAEGQP ISLFRPVMYD GSALVLYALR HEIGEEAFAR
LERDWVRIHR DGTATTTDFI ELASSVAGRD LSSFFTAWLY RQKTPPMPGH PDWRSEAPAN
NQNAPRNRYA APHRMPHGTG HTAPEQSVKP E
//
