ID A0A0M9X7F6_9ACTN Unreviewed; 856 AA.
AC A0A0M9X7F6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ADK41_25040 {ECO:0000313|EMBL:KOT35329.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT35329.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT35329.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT35329.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-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:KOT35329.1}.
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DR EMBL; LGCN01000212; KOT35329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9X7F6; -.
DR PATRIC; fig|36816.3.peg.5405; -.
DR Proteomes; UP000037773; 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:KOT35329.1};
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:UP000037773};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 91..185
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 532..841
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 856 AA; 94860 MW; E4B1842D08DFFC0E CRC64;
MTREEARQRA KLLTVDSYEI DLDLSGAQEG GTYRSVTTVR FDVAEDGDGA ESFIDLVAPA
VHEVTLNGDS LDPAEVFADS RIALPGLLKG RNILRVEADC AYTNTGEGLH RFVDPVDDQA
YLYTQFEVPD ARRVFASFEQ PDLKATFRFT VKAPEGWTVI SNSPTPEPQE NVWRFEPTPR
ISSYITALIV GPYHSVHSVY EKDGRSVPLG IYCRPSLAEY LDSDAIFEVT RQGFDWFQEK
FDYAYPFEKY DQLFVPEFNA GAMENAGAVT IRDQYVFRSK VTDAAYEVRA ETILHELAHM
WFGDLVTMEW WNDLWLNESF ATYTSIACQA AAPGSKWPHS WTTFANSMKT WAYRQDQLPS
THPIMADIRD LDDVLVNFDG ITYAKGASVL KQLVAYVGED AFFRGVQAYF KRHAYGNTRL
SDLLGALEET SGRDLRTWSK QWLETAGINV LRPVIETDAE GVVTSFAVRQ EAPALPAGAK
GEPTLRPHRI AIGAYDLDGD GRLVRGERVE LDVDGELTAV PQLVGKRRPA VVLLNDDDLS
YAKVRLDEES LAVVTEHLGD FAESLPRALC WASAWDMTRD AELAARDYLS LVLSGIGKES
DIGVVQSLHR QVKLAIDLYA DPNARETLLA RWTDATLAHL RSAEPGGDHQ LAWARAFAAT
ARTPEQLDLL EGLLAGTQTV EGLAVDTELR WSFVQRLAAV GRFDEAEIAD EYERDRTAAG
ERHAATARAA RPTEEAKAEA WASVVESDKL PNAVQEAVIA GFVQTDQREL LAPYADRYFE
VLADVWASRS HEIAQQIAVG LYPTVQVSGE TLDKTDAWLT SAEPGAALRR LVSESRAGVE
RALRAQAADA AAGTVR
//
