ID   A0A0F4JSH1_9ACTN        Unreviewed;       848 AA.
AC   A0A0F4JSH1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=VR44_05975 {ECO:0000313|EMBL:KJY37317.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY37317.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY37317.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY37317.1};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJY37317.1}.
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DR   EMBL; JZWV01000110; KJY37317.1; -; Genomic_DNA.
DR   RefSeq; WP_045946313.1; NZ_JZWV01000110.1.
DR   AlphaFoldDB; A0A0F4JSH1; -.
DR   STRING; 68223.GCA_002028425_02507; -.
DR   MEROPS; M01.012; -.
DR   PATRIC; fig|68223.7.peg.2409; -.
DR   eggNOG; COG0308; Bacteria.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000033551; 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:KJY37317.1};
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          121..194
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          239..449
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          528..838
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
SQ   SEQUENCE   848 AA;  93704 MW;  6530AA1505C6BC18 CRC64;
     MPGENLSRDE ARVRAELLSV DGYEVVLDLR SAVDEAEPAE GPRTFRSVTT VRFRAAAPGA
     SSFADLIAPS VNSVTLNGRA LDPAVVFDGA RIALDGLAAE NVLVVDANCA YSRTGEGMHR
     FVDPEDGEVY LYTQYEPADA RRVYANFEQP DLKAPYRFEV SAPEGWTVWS NGAEESREGG
     VWRFAETAPI STYITCVVAG PYHYVTDTYT RGDLTIPLGA MCRKGLAKHF DADDVFLVTK
     QGFDLFHEIF DYPYPFGKYD QAFVPEYNLG AMENPGMVTF REEYIFRGKV TQASYERRAN
     VILHEMAHMW FGDLVTMKWW DDLWLKESFA DFMGSFGLVE ATRFDQAWVT FANNRKAWAY
     RADQLPSTHP ITADIRDLED AKLNFDGITY AKGAAVLKQL VAYVGRDAFL DGARRYFKAH
     AYGNTTLDDL LSVLGEVSGR DMAEWSRAWL QTAGVNALTP VVTTDAAGRL TELAVVQEGD
     ELRPHRVAVG LYRLEADGSL VRYARAEADV AGVRTVVGEL AGLERPDLVL VNDEDLTYCK
     IRFDEASLAT LRGHLGDLTD PLARALCWSA LWNLTRDALM PARDFLSLVL AHAGRESDVG
     VLQQLHAQAL SAVTHYAAPD WREQGGRELA AGALHELRLA EPGSEHQLTW ARFFAASAAS
     EGDFQLLLGL LEGSARIDGL EVDQELRWDF LLPLAAHGVV DEAVLAAELV RDDTASGKRH
     QVRCLAARPS AAVKDQAWAV VVESDALSNA LVEATISGMQ QSSQRELLAP YAGRYFEVIE
     RIWAERSIQI GIDVVKGLYP MLQDSQATLD ATDAWLTSRP DAAPALRRLV LESRDDLARA
     LRAQSRDA
//