ID A0A075JGP7_9MICO Unreviewed; 861 AA.
AC A0A075JGP7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HX89_05330 {ECO:0000313|EMBL:AIF40462.1};
OS Dermacoccus nishinomiyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40462.1, ECO:0000313|Proteomes:UP000027986};
RN [1] {ECO:0000313|EMBL:AIF40462.1, ECO:0000313|Proteomes:UP000027986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M25 {ECO:0000313|EMBL:AIF40462.1,
RC ECO:0000313|Proteomes:UP000027986};
RA Hong K.W., Chan K.G.;
RT "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL Submitted (JUL-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP008889; AIF40462.1; -; Genomic_DNA.
DR RefSeq; WP_038567527.1; NZ_CP008889.1.
DR AlphaFoldDB; A0A075JGP7; -.
DR MEROPS; M01.009; -.
DR GeneID; 41840607; -.
DR KEGG; dni:HX89_05330; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
DR Proteomes; UP000027986; Chromosome.
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:AIF40462.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000027986};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 103..196
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 239..452
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 535..845
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 861 AA; 94620 MW; 68649954EA777C8C CRC64;
MNGANLTRDD AQTRGENITV DSYAVTLDLT TGPTTFATSS VVRFSAQPGS ETWLDFLGES
VSRVVVNGEE RDVDWNGARI SLTGLAAENE VRVDAVGVYM NTGEGLHRFV DPADDEVYLY
SQFEVPDARR MYPVFEQPDL KATFQFTVTA PARWQVLSNE TTPEPKPATQ TYTGPNGVSE
PAATWEFAPT ARISCYITAL VAGPYEAYRD SVETRAGTIP LGVFCRKSLA PHMDADEIFD
ITKRGFAFFE NEFDQPYPFT KYDQIFTPEY NAGAMENVGC VTFSEIYVFR AKVSEAVVER
RALTVLHELA HMWFGDLVTM KWWNDLWLNE SFAEWASTTA QAEATRWESA WTTFGTSEKA
WAYRQDQLSS THPIVAPIRD LADVEVNFDG ITYAKGASVL KQLVAYVGRE PFTAGLRAYF
ARYAWQNTTL PQLLAELETT SGRDLTQWSK LWLETAGVNT LRPIVETDDD GRMTSVVIEQ
SAADDYPTLR PHRLAVGCYT LRDGALTRTA RVELDVDGER TEVSELVGTP QPDLLLVNDD
DLAYAKIRLD ARSLATAIAH PRAFTDSLPR ALVLGAAWDM TRDAEMSARD FIDMALATLP
GESDSTLLRT LLGQLTTAAR TYTASEHRDD VVALVARTLR GLLRSAEPGS DAQLQLAQAF
TSFAASADDL AFVRGLFEGS SVLDGLALDT EMRWTLLTSL VAGGVLGEPE IAAELEQDNT
ATGAERAARA RAAIPTAEAK AAAWASVVDS DALANQTIAE TAAGFGHVHD EALLEPYVER
YFEMAEGYWA SRTHHIAELT IGSFFPFTLA GPQLLAQANT WLDAHRDAPA GLVRTVAENR
DTVARAVEAQ RFDAQAARQH G
//
