ID V6KVZ6_9ACTN Unreviewed; 867 AA.
AC V6KVZ6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=N566_17560 {ECO:0000313|EMBL:EST35616.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST35616.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST35616.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST35616.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST35616.1}.
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DR EMBL; AWQV01000580; EST35616.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KVZ6; -.
DR STRING; 1380770.N566_17560; -.
DR MEROPS; M01.012; -.
DR PATRIC; fig|1380770.3.peg.3049; -.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000017915; 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:EST35616.1};
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:UP000017915};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 119..200
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 249..460
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 543..853
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 867 AA; 96089 MW; ECE58DC5088C7E0D CRC64;
MPGENLTRDE ARRRAELLAV DGYEVALDVR SALGTPPADG VRTFRSTTTI RFRCTEPGAS
TFVDLVAPEL HSATLNGRAL NPDTAFDGAR LTVDGLAAEN ELVVDARCAY SRTGEGLHHF
VDPEDGEVYL YTQYEPADAR RVFANFEQPD LKAPYDFVVT APATWRVLSN GAQEGDPELL
DDGASSVRRF ARTQPISTYI TAVVAGPYHH VSDVYRRRLD DGTELEIPLG ALCRKGLARH
FDADDIFTIT KQGLDFFHDH FDFPYPFGKY DQAFVPEYNL GAMENPGCVT FREEFVFRGR
VTDASYEARA NVILHEMAHM WFGDLVTMEW WDDLWLKESF ADFMGSLSMV ESTRFSDGWI
TFANRRKSWA YRADQLPSTH PVTADIRDLE DAKLNFDGIT YAKGASVLKQ LVAYAGRDAF
LEGARRYFKR HAWGNTRLHD LLSVLEETSG RDMGEWAKAW LQTAGVNSLT PEASYGPDGR
LTELAVLQDA PDEHPVLRPH RVAVGLYRLD EGGALTRYAR AETDVSGVRT TIAELAGAER
PDLILLNDED LTYCKVRFDD ASLATLHDRL GSLSDPLARA LCWSALWNMT RDALMPGRDF
LGLVLRFAAD ETDIGVLQML HAWSRSALTH YLAPGRRAEG GRALAEGALR MLRGSEAGSG
HQLAWARFFA AVAESDDDLR LLEGLLAGTE HVDGLAVDQE LRWTLLEPLA VHGRADAAVL
GAELDRDDTA SGKRHQVRLL AARPSAEVKE QAWDAVVATD RLSNALVEAT IAGFHQPEQR
RLTAPYASRY FAALEEVWES RSIETGLSLV RGLYPALQAE QSTLDATDAW LSSHEDAAPA
LRRLVLEARD DLARALRGRA CDEAAAV
//
