ID A0A3N1CNQ0_9ACTN Unreviewed; 495 AA.
AC A0A3N1CNQ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDD29_0278 {ECO:0000313|EMBL:ROO82794.1};
OS Actinocorallia herbida.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinocorallia.
OX NCBI_TaxID=58109 {ECO:0000313|EMBL:ROO82794.1, ECO:0000313|Proteomes:UP000272400};
RN [1] {ECO:0000313|EMBL:ROO82794.1, ECO:0000313|Proteomes:UP000272400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44254 {ECO:0000313|EMBL:ROO82794.1,
RC ECO:0000313|Proteomes:UP000272400};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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:ROO82794.1}.
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DR EMBL; RJKE01000001; ROO82794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1CNQ0; -.
DR Proteomes; UP000272400; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000272400};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..495
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018107495"
FT DOMAIN 84..256
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 344..486
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 25..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 53065 MW; 9ECB979FAA4F70F8 CRC64;
MPFPRASRRA AAVVTLTALT AASACQLPGG DPPPPAPPTG ASTAPAAGPI AGNGPNQEPL
QATRDGAGDP YVPTDGNGGY DVQNYALDLT VDPGKPAKTL DAVATIRARA TQDMVEFNLD
LTGLDVSSVK VDGKDSKFVR AGSELTVSPA ATIAGGRDFT VRVAYSGTPQ AVNDPILGQY
GWIKTPDGVS AACQPSGAHT WFPGNDHPGD KATFAITLTV PKGLTAISNG ERGKVTDKGG
FSTVTWKADQ PMATYLAMIS VGKFKVKEGL TKGGIPILVA VDDTVRSPSV DEFYRMKADI
TDAWAKIFGP YPFGSTGGVI DNAAVGFALE SQTRSIYGDF APGESIIAHE LAHQWFGDSV
GVTRWQDIWL NEGFASYAEW IWSEQQGGMT AEEFFTTRYN EPENSQSWLV PTGDPGRERM
FDGFGVYERG AMTLHALRKR IGDDRFFTLL RTWAADHQYG NATTEEFVEL AERISQTELT
EFFNAWLYGT VRPAL
//
