ID A0A1C5E1B6_9ACTN Unreviewed; 830 AA.
AC A0A1C5E1B6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-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=GA0115259_1042434 {ECO:0000313|EMBL:SCF89005.1};
OS Streptomyces sp. MnatMP-M17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCF89005.1, ECO:0000313|Proteomes:UP000198886};
RN [1] {ECO:0000313|EMBL:SCF89005.1, ECO:0000313|Proteomes:UP000198886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCF89005.1,
RC ECO:0000313|Proteomes:UP000198886};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMDK01000408; SCF89005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5E1B6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000198886; 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:SCF89005.1};
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:UP000198886};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 98..167
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 511..811
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 830 AA; 91335 MW; 5C9A212594D62C73 CRC64;
MPSLTREEAR ERGSLLLVRA YCVDLDLTSG SDTFRSTTKI RFDAREPGSE TFLDIEPKML
RSITLNGREL DAAEFSDGRF PLTGLDAENE LVVVADMSYS NECEGLHRYV DPADGETYVY
SFVYVDNAPR VFACFDQPDL KAPYEFELTV PETWQVLGNS EAVRTGPGRW RLTESPALAT
YLTALVAGPY ASFRTEHNGI PLGLHCRASL ADSLKTDVDE VFEITAQCLD AYTALFGVGH
PFAKLDQVFV PEFSVLSLDH PGCVLLREQY LFSSAAADSE RETRAVVLAH GISLLWLAGL
VTNAWWNDLW LGQSLADYMA HRVTSEVTRF PGPPTTFAAR RKGQAYLPDQ RPSTHPVSIE
GPDVRTVQLE LDRISYFKGH SALRQLAAHI GDDALTAGLR TYFDRHAYST ATFADFLAAM
GEAAGTDLTD WAEKWLHTPN VNTLTPELTV ADGHITAAAV LQGAPDSHPV LRPHTMDVGL
YYADDSTTVR VRIDGARTEL PELMGRPAPV FLLLNDGDLT YAKIGFDPVS RAALPDTLAR
LSPLNRAMVW CALLLGVQDG TYPAAAHLAL VSGMVRQETE LSILAEVLEQ ARHDVADRFL
APHERPAATA RVAAALRERL ARTDSDDERL ITLFRGLVDF TSDTMELSGW LAGDGLPPGL
ELDTDMSWRI RYRLAVLGGM DTADIAAALD AGPGAVAEQF AAKCRAALPE ASAKEAAWHA
IMRGTDLSNY ELWSLAEGFW QPEQSALTEP YVERFFRDMP AAARGRGDLV LDLLLRFLYP
RYAATPRTLE SAQRMIALDG LPVTLRRRAA DHTHDLRRVI AARAARADEG
//
