ID A0A384IXE4_9ACTN Unreviewed; 873 AA.
AC A0A384IXE4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:PZT81932.1};
GN ORFNames=DNK56_07445 {ECO:0000313|EMBL:PZT81932.1};
OS Streptomyces sp. AC1-42W.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT81932.1, ECO:0000313|Proteomes:UP000249154};
RN [1] {ECO:0000313|EMBL:PZT81932.1, ECO:0000313|Proteomes:UP000249154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC1-42W {ECO:0000313|EMBL:PZT81932.1,
RC ECO:0000313|Proteomes:UP000249154};
RA De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
RL Submitted (JUN-2018) 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:PZT81932.1}.
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DR EMBL; QKWY01000001; PZT81932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384IXE4; -.
DR Proteomes; UP000249154; 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:PZT81932.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PZT81932.1};
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:UP000249154};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 125..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 248..458
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 541..861
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 873 AA; 96541 MW; 6C434EAD1FB719A1 CRC64;
MPGENLSRDE ARERAELLTV DGYDVELDVR SAVGDPGRDD RARGPLTFRS VTTIRFRTRR
GGASTFADLI APSVSAVTLD GAELDPAAVF DGARVTLADL SEGEHVLVVD AQCAYSRTGE
GMHRFVDPED GEVYLYTQYE PADARRVFAN FEQPDLKAPY RFRVTAPAEW TVWSNGAEES
REGGVWRFAE TKPISTYITA VVAGPYHYVT DSYSRTFEDG TTLEIPLGAM CRKGLAKHFD
ADDVFLITKQ GLDFFHDNFD YPYPFGKYDQ AFVPEYNLGA MENPGCVTFR EEYIFRGKVT
QAAYEGRANV ILHEMAHMWF GDLVTMGWWD DLWLKESFAD FMGVFAMTGA TRFEDGWITF
ANNRKSWAYR ADQLPSTHPI TADIRDLEDA KLNFDGITYA KGASVLKQLV AYVGREAFLE
GARRYFKKHA YGNTTLGDLL SVLSETSGRD MTAWSRSWLQ TAGVNSMTPV ATYDAAGRIT
ELAVLQEAAE SHPELRPHRV AVGLYRRDAE GALVRYARAE ADVSGPRTVI GELAGAERPE
LILVNDDDLT YCKVRFDEVS LATLRAHLGD ITDPSPSSSS RGYPMARALC WSALWNLTRD
GLMPARDFVS LVLAFAGRET DIGVLQMLHA WTRGALTHYA APAWREEGGR ALAEGALGEL
RLAEPGSEHQ LAWARFFASV AASDTDFQLL SGLLDGSARI DGLDVDQELR WAFLSPLVSH
LVADEAAVDA ELARDDTASG ERHRVRCLAS RPSAEVKARA WADVVESDAL SNALVEATIA
GFEQSSQREL LAPYAERYFE AIERVWADRS IQIGMAVVRG LFPSLQDDPA TLEATDAWLE
SHADAAPALR RLVLESRDDL ARALRAQAVD SVA
//
