ID A0A327WIU4_9ACTN Unreviewed; 492 AA.
AC A0A327WIU4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=K377_01733 {ECO:0000313|EMBL:RAJ89607.1};
OS Streptomyces sp. PsTaAH-137.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ89607.1, ECO:0000313|Proteomes:UP000249376};
RN [1] {ECO:0000313|EMBL:RAJ89607.1, ECO:0000313|Proteomes:UP000249376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ89607.1,
RC ECO:0000313|Proteomes:UP000249376};
RA Currie C.;
RT "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT associated Streptomyces.";
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:RAJ89607.1}.
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DR EMBL; QLLY01000003; RAJ89607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327WIU4; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000249376; 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; cd09603; M1_APN_like; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..492
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016398115"
FT DOMAIN 158..220
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 260..465
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 471..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54317 MW; C7DFE39696A5F7CB CRC64;
MLLSSRTPRT VALLAAGASV ALLAAAAPPR PATPLGVGDR LFPTLGNPGY DVRSYDISFT
YKGDNDKPLD AVTRIDARAT ARLDRVNLDF SHGTVRSVEV NGAPADFATG GEDLVVTPAR
PLVAGQPMHI TVRHTSDPRP GKEEVGWVRT KDGLAMANQA DAAHRVFPCN DHPSDKAMFT
FRVNTPQKYT AVANGLPTSL TPGAGDTTDW TYRTAHPMAT ELAQVSIGRS TVLHQKGPHG
LPVRDVVPTK DVKALRPWVD KTPAQLAWME NKVGRYPFEN YGVLIAEAST GFELETQTLS
LFERDLFVRT EYPAWYVESV MVHELAHQWF GDSVSPRTWS DLWLNEGHAT WYESLYAQEK
ADRPMETRMR NAYRESDGWR ASGGAPAAPK NPTHGEKISI FRPVVYDGSA LVLYALRQEI
GTGKFERLER RWVATHRDGT ATTADFTSLA SRVAGRDLSG FFQQWLYAKK TPPMPGHPDW
KSAPVQKSKA RK
//
