ID A0A1I4QSJ1_9ACTN Unreviewed; 834 AA.
AC A0A1I4QSJ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04487980_1001225 {ECO:0000313|EMBL:SFM42705.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM42705.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFM42705.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFM42705.1,
RC ECO:0000313|Proteomes:UP000198530};
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; FOUV01000001; SFM42705.1; -; Genomic_DNA.
DR RefSeq; WP_045555243.1; NZ_FOUV01000001.1.
DR AlphaFoldDB; A0A1I4QSJ1; -.
DR Proteomes; UP000198530; 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:SFM42705.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 228..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 518..826
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 834 AA; 92541 MW; A49BD34723653990 CRC64;
MSLMSVLTRD EAHARARLLD VHRYEIALDL TRGDETFDSR TVIHFTVRGK KKAADTFVEL
KPAELRSVTL DGEALDPATL DGNRLTLKGL TPGDHELRVD AAMRYSRTGE GMHRFTDPTD
GETYVYTQLF MDDVQRVFAA FDQPDLKAAF DLTVTAPEGW TVLANGVTER RDDGTWRAAT
TPLISTYLVA VAAGPWHSVR TEHRGLPFGI HCRRSLAPHL DTDADEILDV TRALFDRYHE
KFEEPYPFDS YDQAFVPEFN AGAMENPGLV TFRDEFVYRS AVTDTERQTR AMVIAHEMAH
MWFGDLVTLK WWDDIWLNES FAEYMGYQTL TEASRFADTW VDFGVARKAW GYDADQRPST
HPVAPENVDD TAAALLNFDG ISYAKGASAL RQLVAWLGEK DFLAGINAHF TRHRFGNATL
ADFIDNLAGA TERDVHAWAD AWLRTTGVDT LTPKVTRAAD GTYTLTVDHA GGRPHRIAVG
LYDQDHGDDQ GHLTLRDRVE LDLPQTDPQP IGKRPALLLL NDGDLTYAKV RFDPESFTAV
TGHLCGLPDP LTRAVVWNAL RDAVRDAELP PTAYLEAART HLPRESDLAI VQGVLAFAGT
QVADRFLAPE QRAAGLATLG SLCRDLIRRT EDGDNPGLRL TAVRHFIDVA AHPETIAAWL
ADGTVPGGPE LDPELRWRVL GRLAVLGAVD TATIDAELER DPSASGREGA ARCRAALPDP
EAKRAAWEAM FTADDLSNYL FTATAQGFWQ PEQADLLTEY VERYWADAVS LAARRGPAIA
EAAGRWAFPV YAVDAETLGL GERCLQDEDL IPALRRKLVD QLDDLARALR VREV
//
