ID A0A0F0HL46_9PSEU Unreviewed; 835 AA.
AC A0A0F0HL46;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=UK12_30885 {ECO:0000313|EMBL:KJK55082.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK55082.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK55082.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK55082.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK55082.1}.
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DR EMBL; JYJF01000168; KJK55082.1; -; Genomic_DNA.
DR RefSeq; WP_045306512.1; NZ_JYJF01000168.1.
DR AlphaFoldDB; A0A0F0HL46; -.
DR MEROPS; M01.012; -.
DR PATRIC; fig|1427391.3.peg.2348; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000033409; 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 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:UP000033409};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 91..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 521..828
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 835 AA; 91530 MW; 27253135F53D074F CRC64;
MPALQRTEAR IRARLVQVRD YQVDLDLTRG EEVFGSTTVI RFDCTEPGAA TFLDLQPAAL
HRVVLNGREL DPADLDGNRL ALTGLAAGNE LRVEAEMRYS RTGEGLHRFT DPADGAVYLY
AACGPDSAPL VFGCFDQPDL KAPFRLAATA PADWTLVANG PAERTDSGED TAGKRWEFAP
TQPISTYLFT VVAGPLHSRY AEHDGIPFGL HARRSLAADL DREAEEIFEV TRASFDRLHE
LFDERYPFGR YDQAFVPEFN WGAMENPGCV VFNEELLFHS APTEAERELR AVVIAHEMAH
MWFGNLVTMR WWDDLWLNES FAEYLGYRIA AESTRFTGSW TGFGVNRKGW GYDADQRSTT
HPIAATGIES LAEAMVNFDG IAYAKGASAL RQLVAWLGDE AFFAGINEHF ARHRFGNAEL
ADFLDALATA SGRDVQGWAE RWLRTSGVDT LRLDVRYDEA DRVAAAELVP DGTRPHRVGV
GVYDRRSDGA LVLRDRFEAE VEPGCRTALP KSAGTARAAL LLPNHGDLTW AKIRLDEDSW
RTVTTSLSRI EDPLARAVLW ENARDLVRDA ELAPAEYLDL AESQLPAEDA DTVVDAVLTF
ARTKLIADYL APADRPAAAA RLAGLSRRLL ARPDAGDGLR IAALRGAIEN ATGPEQLAEL
EVWLTDGGPA GELSTELRWT ALARLAAEGL ADEARIAAEL AADPSSSAHQ GAACARAARP
APEAKAAAWQ QLFTDGALSN HLMSATAQGF WRSGAEQLQQ DYVRRYFAEL PAAGQRGTTV
ARVLGRVLFP AGRAEPETVR LAEACLAGED LTPSLRRVLA DQVDDLRRAV RVRGR
//
