ID A0A327W280_9ACTN Unreviewed; 857 AA.
AC A0A327W280;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=K377_03813 {ECO:0000313|EMBL:RAJ82763.1};
OS Streptomyces sp. PsTaAH-137.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ82763.1, ECO:0000313|Proteomes:UP000249376};
RN [1] {ECO:0000313|EMBL:RAJ82763.1, ECO:0000313|Proteomes:UP000249376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ82763.1,
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:RAJ82763.1}.
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DR EMBL; QLLY01000008; RAJ82763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327W280; -.
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; 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:RAJ82763.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 92..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 539..848
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 857 AA; 94794 MW; D70D1456CC3A4148 CRC64;
MPGTNLTREE AQQRAKLLTV DSYEIDLDLS GAQEGGTFRS VTTVRFDSAE AGAESFIDLI
ADAVHEVVLN GRSLDVAAVF RDSRIALAHL ESGPNELRIV ADCAYTNTGE GLHRFVDPVD
QQAYLYTQFE VPDARRVFAN FEQPDLKGTF QFTVKAPTGW TVISNSATPE PKDDVWHFEP
TPRMSSYITA LIVGPYHSVH SSYDNPETGQ SVPLGIYCRP SLAEYLDSDA IFEVTRQGFA
WFQEKFDYAY PFAKYDQLFV PEFNAGAMEN AGAVTIRDQY VFRSKVTDAA YEVRAETILH
ELAHMWFGDL VTMEWWNDLW LNESFATYTS IACQAYAPDS KWPHSWTTFA NSMKTWAYRQ
DQLPSTHPIM AEINDLDDVL VNFDGITYAK GASVLKQLVA YVGMDEFFQG VQAYFKRHAF
GNTRLSDLLG ALEETSGRDL KSWSKAWLET AGINILRPEI ETDEHGVITS FAIRQEAPAL
PAGAKGEPTL RPHRIAVGFY DLDDASGKLV RGERVELDVT AGESTQVPQL VGKHRPAVVL
LNDDDLSYAK VRLDEESLAF VTQHLGDFEA SLPRALCWAS AWDMTRDAEL SASAYLDLVL
SGVAKESDIG VVQSLQRQVK LALDLYAAPA HRDALLTRWT EATLTHLRTS APGSDHQLAW
ARAFAATART PEQLDVLDAL LEGSQTIEGL AVDTELRWAF VQRLAAVGRF DETEITAEYE
LDRTAAGERH AATARAARPT PEAKAEAWAS VVESDQLPNA VQEAVIGGFV QTDQRELLAP
YTEKYFSALK DVWDSRSHEM AQQIAVGLFP SVQVSEETLA ATNAWLDSAQ PSAALARLVS
ESRAGVERAL KAQGADA
//
