ID   A0A1G8LQ42_9FLAO        Unreviewed;       836 AA.
AC   A0A1G8LQ42;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=SAMN05421846_1106 {ECO:0000313|EMBL:SDI57755.1};
OS   Chryseobacterium taeanense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=311334 {ECO:0000313|EMBL:SDI57755.1, ECO:0000313|Proteomes:UP000198869};
RN   [1] {ECO:0000313|Proteomes:UP000198869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17071 {ECO:0000313|Proteomes:UP000198869};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNDW01000010; SDI57755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LQ42; -.
DR   STRING; 311334.SAMN05421846_1106; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000198869; 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   Aminopeptidase {ECO:0000313|EMBL:SDI57755.1};
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}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..836
FT                   /note="Aminopeptidase N"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011712859"
FT   DOMAIN          44..233
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          271..477
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   836 AA;  94905 MW;  9D5E73E5A47C909E CRC64;
     MKKAILSIAL LGIFFSTNVA AQTETSGREK VYRATHTKAT ELKHTKLKVN FDYQKEQMNG
     EEWLTASPFF YPTGELTLDA KGMLIHEVAL DTNGKKSPLK YDYKNDVLKI TLDKTYTKNQ
     DYTVYIKYTA RPNEVKQEGS AAINDAKGLY FINPQGKEAD KPTQIWTQGE TESSSAWFPT
     IDKPNQKSTQ EIYMTVPDKY VTLSNGILKD SQKESNGLRT DHWVMDKRHS TYLFFMGVGE
     YAIVKDKWRN IPVDYYIEKK YEPYAKQIYG NTPEMIEFFS KKLGYDYPWA KYAQISGRDY
     VSGAMENTTA TLHGSDILQK PGQLIDENTW EDTIAHELFH HWFGDLVTAE SWSNLTVNES
     FANYSEYLWN EYKYGKDQAD YHQMKDVNMY IHNPGDFKKD LVRFNYDSRE DVFDLVTYQK
     GGGILHMLRN YLGDDAFFAG IQDYLKTNEY QNAEAHQLRL SFEKVSGKDL NWFFNQWYFG
     SGNPKINYSY TFEPVKKQIA VTVEQTQEQP FQFPLAIDVY ENGKPKRYNV WVNAEAKNTF
     NFDVTKNADL VNINADGVLL ADIQDTKTPE QYLMQFTGSK EFKSKYAALN GIKDQLGKNP
     AATKLLAAAI KDPFFRTRIR ALQLMDLSNA EQLKALGSDV EKLATNDPKT LVQAAAISAL
     AKTKDKKYMP VFEKGANAVS NAVKGSSVGA IVAIDPAKAG TYADKIDMEG ASETLAAQML
     PIIVQNKVAS QMANIAQFAA FYPFIKFQNP ELGKSAEEGY NWIMSSDNLK ATESITKMLS
     RAKGQIGNNP QVKMMISQML KDGLNKKMEV LKQNPQNAAS INKQIDLINK AIEDFK
//