ID A0A2B8ANA4_9ACTN Unreviewed; 864 AA.
AC A0A2B8ANA4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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 Name=pepN {ECO:0000313|EMBL:PGH50374.1};
GN ORFNames=CRI70_12455 {ECO:0000313|EMBL:PGH50374.1};
OS Streptomyces sp. Ru87.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH50374.1, ECO:0000313|Proteomes:UP000222409};
RN [1] {ECO:0000313|EMBL:PGH50374.1, ECO:0000313|Proteomes:UP000222409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru87 {ECO:0000313|EMBL:PGH50374.1,
RC ECO:0000313|Proteomes:UP000222409};
RA Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA Wellington E.M.H.;
RT "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT soil.";
RL Submitted (OCT-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:PGH50374.1}.
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DR EMBL; PDIX01000186; PGH50374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8ANA4; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000222409; 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:PGH50374.1};
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:UP000222409};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 115..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 247..458
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 540..850
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 864 AA; 95414 MW; E806356686586292 CRC64;
MPGENLTRDE ARERAGLLSV DGYEVALDLR SATEPGGHAS RTFRSVTTVR FRCSRPGAAS
FADLVAPAVA SVTLNGRALD PAAVFDGSRV TLEDLAAENV LTVDARCAYS RTGEGMHRFT
DPEDGATYLY TQYEPADARR VFTNFEQPDL KAPYSFAVTA PGGWTVLGNG EREGEPEPAE
GGGATWRFVT TRPISTYITA IAAGPYHMVH DTYRRTLEDG TELVIPLGAL CRKGLARHFD
ADDIFTVTKQ GLDFFHDHFG FPYPFGKYDQ AFVPEYNIGA MENPGLVTFR EEYVFRGKVT
EASYQGRANV ILHEMAHMWF GDLVTMEWWD DLWLKESFAD FMGALSLVEA TRFEGGWITF
ANRRKAWAYR ADQLPSTHPI TADIRDLQDA KLNFDGITYA KGASVLKQLV AYAGRDAFME
GARRYFRRHA YGNTRLGDLL SVLEETSGRD MTEWSRAWLQ TAGVNSLTPQ AVYDSNGRIT
ELAVLQEAAA SHPRLRPHRV AVGLYRREGT ELVRYARAEA DVDGPRTVVT ALAGAERPEL
ILVNDDDLTY CKTRFDEGSL DTLRKHLGDL TDPLARALCW SALWNLTRDG LMPARDFLAM
VLSFAGRESD IGVLQMLHAW ARSALVHYAA PDWRERGGRA LAEGALSELR MAPPGSGHQL
AWARFFAQCA GSAADLQLLR GLLAGTAKID GLDVDQELRW TFLEPLAAHG VADTAEIAAE
LSRDDTASGK RHQVRCLAAR PSREVKDRAW ADVVDSDRLS NALVEATIAG FDQPDQRELL
APYTGRYFES IERVWQERSI EIGMAVVRGL FPALQGDRAT LDAAQGWLDG HPDAAPALRR
LVLEAHDDLA RALRGQECDA AAAG
//
