ID A0A1T3P1D1_9ACTN Unreviewed; 847 AA.
AC A0A1T3P1D1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B4N89_19975 {ECO:0000313|EMBL:OPC82913.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC82913.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC82913.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC82913.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) 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:OPC82913.1}.
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DR EMBL; MWQN01000001; OPC82913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T3P1D1; -.
DR STRING; 159449.B4N89_19975; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000190037; 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:OPC82913.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000190037};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 114..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 237..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 526..836
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 847 AA; 93800 MW; DF49A3FC0FDDE118 CRC64;
MPGRNLTREE ARERARILSV EDYDVRLDVS TDSTETFHSE TVLRFGCREA GAATFVDLLA
PEVHEVVLNG RVLDPAEVFD GTRVLLTDLV EGANELRVLA SCAYSRTGEG LHRFVDPVDD
RVYLYTQYEP ADSRRVFANF EQPDLKASFR FSITAPADWR VVSNSTTPTP EPVRDGVARW
DFAPTPRIST YLTAIVAGPY HAVFDSYTSE AGLVVPLGGF CRASLAESFD HEEIFAVTKQ
GLDLFHDRFG FPYPFGKYDQ LFVPEYNLGA MENPGAVTFT EEYVFRSKVT DSAYEGRANV
LLHEMAHMWF GDLVTPRWWD DLWLKESFAD FMGSYAQGAA TRWTDAWTSF AARRKDWAYR
QDQLPTTHPI VAVINDLEDA KLNFDGITYA KGASVLKQLV AYVGEDEFFA GARSYFRTHA
WGNTTLADFL TALEETSGRD LKSWSADWLE TSGVNTLRPA IETDADGVIT SFAVLQEAAP
GFPTLRPHRI AIGLYDGAER VARVEVDVVG ARTEVPALVG RVRAPLILLN DDDLTYAKVR
FDPESWRTLL DSLGTIDSSL ARALCWGAAW DMTRDGELSA RDYLDLVLRH AGRESDVGVV
QKLHTQVKTG LDHYTDPALR AEALHRLATG AAEELRAAPA GGDHQLAWAR CLASASATPD
ELAFLRELLS GGQEVPGLAM DTELRWAMLR ALCAGGAADE PEIAAELGRD GTAAGRRHAI
ECRAARPTAE AKAEAWHLAV DSDELPNATL GAVIAGFATA GQEELTDPYV DRYFAALTPV
WRDRSIEIAR RIVVGLYPSG RIDPDTLRRT DEWLAAAEPV PALRRLVLEC RDDVARALRA
RGRDRRN
//
