ID A0A0W7WTJ4_9ACTN Unreviewed; 834 AA.
AC A0A0W7WTJ4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AT728_01220 {ECO:0000313|EMBL:KUF13903.1};
OS Streptomyces silvensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF13903.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF13903.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF13903.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-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:KUF13903.1}.
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DR EMBL; LOCL01000062; KUF13903.1; -; Genomic_DNA.
DR RefSeq; WP_058851660.1; NZ_LOCL01000062.1.
DR AlphaFoldDB; A0A0W7WTJ4; -.
DR STRING; 1765722.AT728_01220; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000054804; 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:KUF13903.1};
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:UP000054804};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 88..182
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..438
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 513..823
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 834 AA; 91580 MW; C4EF2C3AF14A605D CRC64;
MSVLTRDEAQ TRAQLLDVRR YEVDLDLTTG EDTFDSRTVI TFSAAADGDT FVELKPARLR
SVTLDGTALD PADLDGNRLP LRGLTAGEHE LRVDAVMHYS RTGEGMHRFT DPADGETYLY
TQLFLEDVQR VFAAFDQPDL KAVFALTVTA PEGWTVLANG VVEDLGGGRW QAAPTPLIST
YLVAVAAGPW HSVRTEHRGL PFGLHCRRSL APYLDADADE LLDVTVACFD RYHEKFTEPY
PFDSYDQAFV PEFNAGAMEN PGLVTFRDEF VFRSAVTDTQ RQSRAMVVAH EMAHMWFGDL
VTLAWWDDIW LNESFAEYMG YQTLTEATRF ADTWVDFGVA RKPGGYDADQ RPSTHPVAPD
PDAVPDTASA MLNFDGISYA KGASALRQLV AWLGEKDFLA GINAHFARHR FGNATLADFI
DNLASATDRD VRGWAQAWLR TTGVDTFRPT VTHSGREWTL ALDREGSRPH RVAVGVYDRD
LSDGWSLVLR ERYETDVPSQ EGPVARDGGR PALVVPNDQD LTYAKVRLDG VSQETVLASL
SGVPDALTRA VLWNALRDMV RDGELAPAAY LEAARAHLPA ESDLALVAGV LGFAGFAVAD
RYTPLDGRTA ALATIGALCE DVIRRTEDGS QPGLRLIAVR GVIDSATQPE PLATWLSQGA
VPGGPELDPE LRWRILGRLA ALGAVDESAI AAELRRDPSA TGQEGAALCR AALPDASAKQ
QAWEAMFGSD ELSNYLFTAT AQGFWQPEQE ALVRTYVPRF FEDAVALADR RGPAMAEAAG
RHAFPRSAVD EETLRLGERC LERTDVLPAL RRILADQLDE LRRALRVRDG SGQR
//
