ID A0A1L7D1V5_9CORY Unreviewed; 833 AA.
AC A0A1L7D1V5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CPHO_03145 {ECO:0000313|EMBL:APT92053.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT92053.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT92053.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT92053.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-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}.
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DR EMBL; CP009249; APT92053.1; -; Genomic_DNA.
DR RefSeq; WP_075733139.1; NZ_VXKJ01000030.1.
DR AlphaFoldDB; A0A1L7D1V5; -.
DR STRING; 161895.CPHO_03145; -.
DR KEGG; cpho:CPHO_03145; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000185491; 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:APT92053.1};
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:UP000185491};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..169
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 238..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 525..822
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 833 AA; 92925 MW; 9834F063BB59EB00 CRC64;
MSSINLTRTE AQQRSEMLQV NHYTIDLDLT GEEKFNSRTV VEFEVKKKGS TFIDLRADEL
RSARLDGEAL PVSYYSAKAG IPLHSLSEGS HTLEVEAAIS YSRTGEGLHR FTDPADGETY
LYTQFQTADA KRVFACFDQP DLKATYSLRF TTPENWTVIT NSPVTRSGNT WTAEIDYQLS
TYLVALCAGP YVGVEDTWTG ELTAHPEGKP AQKLEVPLGI YCRASLADAL DSERLFTETK
QGFDWYHRNF GFAYPFGKYD QIFVPEFNAG AMENAGCVTI RDEYVFTSKA THYQYELRAD
TVLHELAHMW FGDLVTMQWW DDLWLNESFA TWAAAISQAE ETEYDTAWVT FANTEKAGAY
RQDQLPTTHP ISTDASDIET VEQNFDGITY AKGASALKQL QAYVGREEFL AGVRRHFTEH
AWGNATFADL LRHLEEASGR DLSFWANQWL KTTGVNTLRP DFVRDEGKIQ DFSVVQSGDT
LRTHRIAIGA YSLVDGKVVR THRVEVDISG ELTEVDEMNG IEADLVIVND DDLTYALLEF
DAESLDFVKK HIADFSDPMA RTLCWSAAWE MTRGASMRAR DFVGLVARGA QAETELAVLE
RLISQAVTAQ TRFADPEWAQ EDTQLADCLL SGAKSADPER AIIYQRAMTE IKLTPATYEF
LNEKLAETSD ANLRWRMLTA LIADASVTDP QAAVAAELER DNTATGYQAS LKALAAINEP
GAKRAVWEEI VAGGLGNRDL TSKLAGLTFT GAEKLLPSAE FFDVAEKLWD TGSNEVALTT
VGGLFPTWDV TQENLDRAEA FLARDIPSGL RRAVTEERDH TARALRNRTF DAA
//
