ID A0A2A3I0I8_9ACTN Unreviewed; 839 AA.
AC A0A2A3I0I8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=BX265_2019 {ECO:0000313|EMBL:PBC77277.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC77277.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC77277.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC77277.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-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:PBC77277.1}.
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DR EMBL; NSGV01000001; PBC77277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3I0I8; -.
DR Proteomes; UP000218662; 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:PBC77277.1};
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:UP000218662};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 109..174
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 524..833
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 839 AA; 90487 MW; B8394CD6E49FCE77 CRC64;
MVPARLGKHA GMPALQRSEA AFRAQLLDVR SYSVDLDLTR GDSLFRSTTV IRFGCAEPGA
GSFVDLAPAA LLRAELNGRP LDPAALDGGR LALPGLAAEN ELLVEADMHY SRTCEGLHRF
TDPADGAGYV FASCGPDLAP RMFACFDQPD LKAPFTFTVT APEDWTVIGN GTAVRLPDGR
WQVAPVGPIS TYLVTVVGGP LHAVRTEHDG IPLGLYARRS LAAELEREAE ELFEVTRASF
DRLHGLFDER YPFGKYDQAF VPEFNWGAME NPGCVVFRDE MLFRSAPTEP QREMRAMVVC
HEMAHMWFGD LVTMAWWDDL WLNESFAEML GYRTAADSTR FTGAWTSFAV KRKGWGYDAD
LRGSTHPVAA TAMGSVAEAL VNFDGISYAK GASALRQLVH WLGDEAFFAG LNAYFAKHRR
GNADLADFLA ALGAATDRDV AGWAEAWLRT SGVDTLRLEV EAEGDTLASV VLVNDGTRPH
RIRVGVYDRA GEAVVLRERI DADVAPGGRT VLPELAGAPR PALLLPNDGD LTWALVRLDE
HSAATVGASL SRIEDEQARA VLWEHARDLV RSAELPAAGY LRLVADHLPA ETAVTIVEAV
LRFAADHVVA RYLGPAERPA ALALLGDTAR ALLARPDAGE SLRIAALRAV VATAAGEERL
AELAGWLDGR DLPGGVPFDA DLRWSALLQL AAAGAVDEER IAAELAADPS NTGEQGAARA
RAALPDPAAK ERAWRALFTP DGLSNHLLAA TAEGFWRSGR PDLQQAYVRR YFEQIPAVGE
RGGAVAKALG LSLFPAGLAL PGTVRAAEAC LARTDLTPTL RRVLADELDD LRRALAHRA
//
