ID A0A366DU67_9NOCA Unreviewed; 829 AA.
AC A0A366DU67;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=DFR74_10249 {ECO:0000313|EMBL:RBO93633.1};
OS Nocardia puris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO93633.1, ECO:0000313|Proteomes:UP000252586};
RN [1] {ECO:0000313|EMBL:RBO93633.1, ECO:0000313|Proteomes:UP000252586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO93633.1,
RC ECO:0000313|Proteomes:UP000252586};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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:RBO93633.1}.
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DR EMBL; QNRE01000002; RBO93633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366DU67; -.
DR STRING; 1210090.GCA_001613185_06999; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000252586; 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:RBO93633.1};
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:UP000252586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 101..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 507..815
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 829 AA; 91477 MW; 8627AAA2F5261516 CRC64;
MSTENLTRAE AAARSAAVTV RGYRVELDVS DAPDPDRPGF ATTTTVEFDA TTDRTWLDFL
GPAVEAVTVN GREVPVEYDG ARIALGSLAA SNVVTVRATG AYSRSGEGLH RFLDPADGQT
YLYTQYEPAD ARRVFACFEQ PDLKAPFTFV VTAPRGWEVL SNRPAEAVAA EGERQTVTFS
PTLPLSTYIT AVAAGPYHRV ESSWRRDDLV VPLGVLCRAS LAKYLDADTI LEVTTQGLDF
FAEHFDYPYP WGKYDQVFVP EYNLGAMENP GLVTFTEEYV FRGAATAAQY EGRANTILHE
MAHMWFGDLV TMTWWDDLWL KESFADYMGA LANAEATRWR DAWVAFANRR KAWAYSQDQL
PTTHPIVADI PDLEAAKLNF DGITYAKGAS VLKQLVAWVG RDEFFAGSRR YFRKHAFGNT
TLADLLTELS AESGRDLEQW ARAWLQMSGM STISLEDGAI MQTDPRPHRL AVGLYDFDTA
GDLVRRDRVE LDLVGERTPV ALAPAPLILL NDGDLTYAKI RLDANSLATV EGSLDRVTDP
LARGLLWSAL WNAVRDGVLD PSRYLAMARR FAPAESNMAL LTAVLANASF TIAHYLPGAA
RDRWRGDWLE SCWAALHSAA PGSGAQLAWA RATATAATVD GRHATEIRDI LLERAPAPDG
LALDPDLRWS LWRALAATGA ADAADLDAEL ARDDTSSGRT ARLEALAARP DARVKAEAWS
SALEDTALSN DHLDAVIDGF RAGARRDLLA PYDGEYFANL RTVWARRSIE IARRIVLGLF
PTTESLAPVD DWLAANEDAP GALRRLVIEQ RDHLARDLRV RRIEWPETE
//
