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Database: UniProt
Entry: A0A1Q5N9A1_9ACTN
LinkDB: A0A1Q5N9A1_9ACTN
Original site: A0A1Q5N9A1_9ACTN 
ID   A0A1Q5N9A1_9ACTN        Unreviewed;       511 AA.
AC   A0A1Q5N9A1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-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=AMK16_04730 {ECO:0000313|EMBL:OKK23014.1};
OS   Streptomyces sp. CB00455.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK23014.1, ECO:0000313|Proteomes:UP000185643};
RN   [1] {ECO:0000313|EMBL:OKK23014.1, ECO:0000313|Proteomes:UP000185643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00455 {ECO:0000313|EMBL:OKK23014.1,
RC   ECO:0000313|Proteomes:UP000185643};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKK23014.1}.
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DR   EMBL; LIVQ01000001; OKK23014.1; -; Genomic_DNA.
DR   RefSeq; WP_073910487.1; NZ_LIVQ01000001.1.
DR   AlphaFoldDB; A0A1Q5N9A1; -.
DR   STRING; 1703927.AMK16_04730; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000185643; Unassembled WGS sequence.
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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000185643};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..511
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012592372"
FT   DOMAIN          49..218
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          308..454
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          465..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   511 AA;  55288 MW;  322887B729CB9FEE CRC64;
     MHRKVIAPSV LAASLLLVIP ASAASAGPGA PGIGDPYYPA SGNGGYDVSH YDLRLQYQPK
     TDLLEGTATL LATAKQDLSR FNLDFGLQVS EIRVNGAKAK FAVSGAHELE VTPAKPLARN
     TPLSVVVKYA GKPSEFKVDG WSAWARTPDG AVAAQEPDSA AWWFPSNDHP LDKATFDVSV
     NVPDGLQAIS NGVLQSQSSK LGWTRYNWRS NKPQATYLTT LAVGRFDITT DTTANGLPVL
     NAYSKDLGDN AGAARASVER TTEVAEWLEG VFGPYPFNAL GGYVPNVTSG FALETQTRPF
     YSPRQFQNGT NVSVVVHELA HQWYGDSVSV DGWKDIWINE GFARYSQWLW SEKEGEGTAR
     ELADWTYATR PAEDPFWQVK PGDPGPDNQF HGAVYDRGAL AIQALRNEVG DETFFRILKG
     WPTERALGNA KVGDFVRYAE KASGKPLAQL FETWLYTPGK PDASALNRPA PAAKSPSARS
     GQAAPAAGQA EPKSWKKIAA TNSIHDDDHG H
//
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