ID A0A1I2K8T3_9ACTN Unreviewed; 852 AA.
AC A0A1I2K8T3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05421541_115177 {ECO:0000313|EMBL:SFF62610.1};
OS Actinoplanes philippinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=35752 {ECO:0000313|EMBL:SFF62610.1, ECO:0000313|Proteomes:UP000199645};
RN [1] {ECO:0000313|EMBL:SFF62610.1, ECO:0000313|Proteomes:UP000199645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43019 {ECO:0000313|EMBL:SFF62610.1,
RC ECO:0000313|Proteomes:UP000199645};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FONV01000015; SFF62610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2K8T3; -.
DR STRING; 35752.SAMN05421541_115177; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199645; 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:SFF62610.1};
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:UP000199645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..196
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 531..839
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 852 AA; 93645 MW; C1C111CD6E93B546 CRC64;
MAGVHNLTQV EAAERGRLLE VTGYDITLDL TDGHGNPGSE TFRSTTVINF RCAEPGAATF
IEAAAVRINS ATLNGSPLDI SAWTAEKGLA LPGLAAENTL VVDGDFGYSA SGQGLQRSLD
PVDKEVYLYS QFETADAQRA YACFDQPDLK SVYTWHVTAP GHWKVVSNMP VESEEAAAFG
AKTVHFTTSP RMSTYITAIC AGPYHEVRDS HDGIELGVFC RASMARYLDA DDLFLITKQG
FDFFHEKFGV RYPLPKYDQL WVPDFNAGAM ENFGCVTHAE SHYIFRSQVT DYEYEQRANT
ILHELAHMWF GDLVTMRWWN DLWLNESFAE WASHWCNTEA TRFADAWSTF LSIRKSWGYR
QDQLSSTHPV YCEMPDLEAV EVNFDGITYA KGASVIKQLV AYVGLDPFLT GLRAYFTKHA
WGNATFDDLL TELETASGRE LRKFAAQWLE TAQVNTLRPI VEVGADGTYT SVVVQQEAPA
GFPTLRTHRV GIGLYDLDGD RLVRRELIEA DVAGEQTPIT ALTGVRAPDL LLVNDDDLTY
AKLRLDERSM ATLVRHIGGF DSALPRALSW AAAWDMLRDA ELAARDYVAL VVAGLPAESD
INLTTATLRQ AGMSLTSFAD PAWAPEGWAL LAGLAQRQLA AAEPGSGWQL TWARAFITAA
RTPEQAAVLR GWLSGEAKPE GLVVDTELRW SLLQALAALG AAAETEIDDE LAGDKTASGE
REAAVARALL PTAENKARVW AELTGPQAPP NWLNRSLLQG FQSTRQVALT APYAEKFFAV
VADVWARSDS EPAQEFATMA YPVFQISEET VALTDAWLAQ DGHPASLRRL VAEGRDGVLR
ALKARARDKA AS
//
