ID A0A3M0II08_9ACTN Unreviewed; 859 AA.
AC A0A3M0II08;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=pepN {ECO:0000313|EMBL:RMB86513.1};
GN ORFNames=CTZ28_08695 {ECO:0000313|EMBL:RMB86513.1};
OS Streptomyces shenzhenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943815 {ECO:0000313|EMBL:RMB86513.1, ECO:0000313|Proteomes:UP000270471};
RN [1] {ECO:0000313|EMBL:RMB86513.1, ECO:0000313|Proteomes:UP000270471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=193 {ECO:0000313|EMBL:RMB86513.1,
RC ECO:0000313|Proteomes:UP000270471};
RA Siqueira K.A., Liotti R.G., Mendes T.A.O., Soares M.A.;
RT "Draft genome of actinobacteria isolated from guarana (Paullinia cupana
RT (Mart.) Ducke.";
RL Submitted (NOV-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:RMB86513.1}.
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DR EMBL; PENI01000004; RMB86513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0II08; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000270471; 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:RMB86513.1};
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:UP000270471};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 115..191
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 241..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 534..844
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 859 AA; 95434 MW; 7EBF722303D03983 CRC64;
MPGENLSRDE ARERAALLSV DGYEVSLDLR SAVGDGAAEP RTFRSVTTIR FRCNEPGAAS
FADLIAPSVT ALSLNGRDLD PSEVFDGSRI VLEELAAENE LVVDAQCAYS RTGEGLHRFV
DPEDGEVYLY TQYEPADSRR VFANFEQPDL KAPFRFEVRA PEGWTVWSNG AGERADGVWR
FAETKPISTY ITCVVAGPYH YVTDSYERTF EDGTRLEIPL GAMCRKGLAP HFDHDDVFLV
TKQGLDFFHD HFDYPYPFGK YDQAFVPEYN LGAMENPGLV TFREEYIFRG KVTQASYEAR
ANVILHEMAH MWFGDLVTME WWDDLWLKES FADFMGTFAN VGATRFGNAW ITFANRRKAW
AYRADQLPST HPVTADIRDL QDAKLNFDGI TYAKGASVLK QLVAYVGEEP FLEGARRYFK
RNAYGNTRLG DLLSVLEETS GRDMAAWAGA WLQTAGVNAL TPQVLLDAAG RVSELAVLQE
APESHPRLRP HRVAVGLYRR TPAGDLERYA RVETDVDGPR TVVAELAGAA APELVLVNDD
DLTYCKMRLD ATSLATLRDH LGALTDPLAR AQCWSALWNL TRDALLPARD FVELVLRFAG
RESEIGVVQM LHAWTNSALV HYAAPQWRAT GEWLVADGAL DELRRAEPGS EHQLAWARFF
ATVASSEADL GLLRELLDGT AKIDGLEMDQ ELRWAFLEPL AAHGAADEAA LAAELARDDT
ASGKRHQVRC LAARPSAAVK AQAWAQVVES DALSNALVEA TIAGFAQPTQ RELTAPYAER
YFAAIERVWR ERSIQIGMDV VRGLFPAYQD SPRTLAATDA WLESHREAAP ALRRLVLEAR
DDLARALRGQ AHDAGTFGQ
//
