ID A0A401Y334_9ACTN Unreviewed; 825 AA.
AC A0A401Y334;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=NLS1_09940 {ECO:0000313|EMBL:GCD88988.1};
OS Nocardioides sp. LS1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1027620 {ECO:0000313|EMBL:GCD88988.1, ECO:0000313|Proteomes:UP000288271};
RN [1] {ECO:0000313|EMBL:GCD88988.1, ECO:0000313|Proteomes:UP000288271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS1 {ECO:0000313|EMBL:GCD88988.1,
RC ECO:0000313|Proteomes:UP000288271};
RA Morimura H., Sato I., Uesaka K.;
RT "Draft Genome sequence of the deoxynivalenol-degrading actinomycete
RT Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
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:GCD88988.1}.
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DR EMBL; BIFF01000002; GCD88988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Y334; -.
DR Proteomes; UP000288271; 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:GCD88988.1};
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:UP000288271};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 100..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 519..814
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 825 AA; 90175 MW; 6A93BC6A931B007C CRC64;
MTAVTNPTST PTQSLQHAEA LARFDLLTVD GYDVRLDLAS SDETFRSVTT VRFQSQGGPT
FIDLKPVSVR EIRLNGAPVD VDTLVRGRLP LDTVAGANEL VVDAVMRFRN DGEGLHRSVD
PADGKHYVYG MCFMDAAPSI FPCFDQPDLK APYTFLVTAP TDWVVVGNAP GTQVEPGTWE
FETTQPLSTY FVTLVAGPYH LVTDDHDGIA LGLSARASIA RDLDADADEL FTMTKQCFDE
FHRLFGIRYP FGNYHQAFVP EFNAGAMENP GCVTFRDPLI FSSRVTRGVR IQRATTVAHE
MAHQWFGNIV TPKWWDDLWL NESFAEYMGN RVTADVTEYD DAWTHNAYAR RQWGLVADQR
PSTHPVAGNG AEDALSALQN FDGISYAKGS SILKQLNATL GDDVFFAGAI DHFTQHRFGN
ATMHDLFASW EQAGAGDLSS FTSHWLRTAG PDQIVLDRAA GVVRRTPPAD HPADRPHTLR
VARAVDGKWE TSTLSITGPE TPVEAGDSAF LLDPYEDTWA LVQPDDVTVA ALKGLLPSTD
DTLLRAGVWN NVRSAFHNAA IAPADVIDLL EAGLPVEDSD DAVFYTMPWA VAKVAPLAPE
PASALRRIHD AAMGKVTSAA AGSTLQLSAF QAAVSTSTDP GQLRSWLEGR VLPDGIGLDL
DLRWRILVQL AVLGETDREE LQAALDAEPT ARSRVEHTKA VASLPDAEAK AWAWARFTGE
VDVPNYELEA AGVGMWRSGQ EHLTEPYVER YFADLPGTVE KRSGWVLADT AAVFFPSTSL
TEETVAAAKA FIDSDGLDLS VRRRVVDATD ELQRRLAIRQ AFPAS
//
