ID A0A1E8CRA4_9MICO Unreviewed; 832 AA.
AC A0A1E8CRA4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BA895_07450 {ECO:0000313|EMBL:OFE14973.1};
OS Humibacillus sp. DSM 29435.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Humibacillus.
OX NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE14973.1, ECO:0000313|Proteomes:UP000175826};
RN [1] {ECO:0000313|Proteomes:UP000175826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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}.
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:OFE14973.1}.
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DR EMBL; MAST01000045; OFE14973.1; -; Genomic_DNA.
DR RefSeq; WP_070193349.1; NZ_MAST01000045.1.
DR AlphaFoldDB; A0A1E8CRA4; -.
DR STRING; 1869167.BA895_07450; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000175826; 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; 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 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:OFE14973.1};
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:UP000175826};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 222..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 513..815
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 832 AA; 90765 MW; DAC46B9AE2F2E1FC CRC64;
MRSLTLAESR DRSDLLTVTS YAVDLDLDRG PEVFGSRATV RFASRLENAE TWADLKAVAI
GSITLNGTAL DPASVHDGRL PLPGLALDNE LVVEATMAYS HDGQGLHRAT DPADDLDYVY
GHLFLDAAPS VYVCFDQPDL KAPYDVKVTA PSEWMVIGNG AATQTEPGRW SLATTKPLAT
YFVTVCAGPY VSVLDEHDGI PLGLHARASL REPLERHAAE MIDITRRSFD YFHDLFGIRY
PFGEYHQVFV PEFNAGAMEN PGCVTFRDQY LYRGAATRDE LLSRANTIAH EMSHMWFGDL
VTMQWWDDLW LNESFAEYMS HRCLAGATEY TEAWVDSTIV RKVWGYGAER SPSTHPVAGV
EALDAQSALQ NFDGISYAKG AAALRQLIAY VGDEAFVAGL QAYLTQKSYA NGTLADFLGS
IEQASGQNLA TWSQGWLLTA GRDTLAVELE GATGTVTAAT MRRETPAERP ANRPHAFDVA
GFTDGRETTR IELTVDAAET TIEGLVGQPV PALVVPNASD LTWARVRLSD STLAHLAEQL
PLVDDAQARA VVWSALLDGV HGATVDPRVF LEVFDAAWPH ETNSSILTRV AAYAEHRIIA
WFVPRAEQDA ALRRLTQVAA QMLTTAGDGT TEALAAARLA AAASDDESML TSWAAGHELP
QGLADDGDFR WIVVRNLAGR GLIDAADIDT YLARDDTLQG SLNALMCRAA LPDADAKAWA
WDELTQKRGR SNYEMVHLAR GFWSAPSDSL VADYVPRYFT DVPAMSQWVG EDALARVVLV
AFPKVFTAAT AELSAAALAR DDLSPAVRRQ LIDADAELRE ALESRRVWHG PS
//
