ID A0A2T7SQU0_9ACTN Unreviewed; 841 AA.
AC A0A2T7SQU0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=Y717_01975 {ECO:0000313|EMBL:PVE05349.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE05349.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE05349.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE05349.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) 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:PVE05349.1}.
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DR EMBL; AZSP01000338; PVE05349.1; -; Genomic_DNA.
DR RefSeq; WP_030353604.1; NZ_JOEI01000018.1.
DR AlphaFoldDB; A0A2T7SQU0; -.
DR STRING; 1440053.GCA_000718095_04603; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000245992; 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:PVE05349.1};
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:UP000245992};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 96..182
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 523..833
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 841 AA; 92760 MW; D0730177F7368689 CRC64;
MSVLTRDEAQ TRAQFLDVHR YTIALDLTTG EDTFDSRTVI KFTAQAAGDT FVELKPATLR
SVTLDGRPLD PAALAGNRLP LTGLTAGEHE LRVDAAMRYS RTGEGMHRFT DPADGETYVY
TQLFMDDVQR VFAAFDQPDL KAVFELTVTA PEQWTVLGNG VATRTEGRHW TLAATPLIST
YLVAVAAGPW HSVRTEHAGL PFGIHCRRSL APYLDADADE ILDITRACYD RYHEKFTEPY
PFDSYDQAFV PEFNAGAMEN PGLVTFRDEF VYRSAVTDTE RQTRAMVIAH EMAHMWFGDL
VTLAWWDDIW LNESFAEYMG YQTLTEATLA GSGGNPPRKW GSDTWVDFAI GRKSWGYDAD
QRPSTHPVAP DPDAVPDTAS ALLNFDGISY AKGASALRQL VAWLGEKDFL AGINTHFARH
KFANATLADF IDSLAQATDR DVHAWAGQWL RTTGVDTLTP RISGTDTGWT LDVVRDGSRP
HRVTVGAYDL DRADPARLTR RDLLALDLPL TEPVTAAGHR PDLVVLNDGD LTYAKVRLDA
VSWDTALRAL SGVPDPLTRA VIWNAARDMV RDGELAPTAY LDAARVHLPR ETDLAVVQGV
LDFAALQITD RYLSDTDRPA ALATLTAISR DLIRRTEDGE DPGLRLTAVR HFIDAAGRPG
ALLEWLESGS VPGGPELDPE LRWRVLTRLA VLGAVDPDVI DAELERDPSA TGQEGAARCH
AALPDPEAKA RAWAGLFETD NLSNYLFTAI AKGFWQPEQA ALVREYVPRY YADAVALADR
RGPAIADAAG RHAFPLYAVD EESLRLGRKC LDSAEMIPAL RRKLADQLDD LHRALRVRTA
S
//