ID A0A1I2J6U3_9ACTN Unreviewed; 864 AA.
AC A0A1I2J6U3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=SAMN05216251_11683 {ECO:0000313|EMBL:SFF49573.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF49573.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF49573.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF49573.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONG01000016; SFF49573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2J6U3; -.
DR STRING; 380248.SAMN05216251_11683; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199323; 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:SFF49573.1};
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:UP000199323};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 105..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 543..852
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 864 AA; 94784 MW; 64B9BC977A2A00F5 CRC64;
MPGTNLTREE AQERARLLTV DAYEIELDLR GAQEGGTFRS VTVVRFAAAQ AAGTFIDLVA
PAVHEVVLNG EVLEPADVFA DSRIALPSVR AGENELRVVA DCAYTNTGEG LHRFVDPVDK
QAYLYTQFEV PDARRVFASF EQPDLKASFA FTVKAPEGWT VISNSPTPEP PADGVWVFAP
TPRISSYITA LIVGPYASVH SSWEGNGRSV PLGIYCRPSL AEYLDAEAIF AVTRQGFDWF
EEKFDYAYPF AKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE TRAETILHEL
AHMWFGDLVT MEWWNDLWLN ESFATFTSIA CQAYAPGSKW PHSWTSFANS MKTWAYRQDQ
LPSTHPIMAE INDLDDVLVN FDGITYAKGA SVLKQLVAYV GEDEFFAGVQ AYFKRHAWGN
TRLTDLLGAL EETSGRDLKT WSKAWLETAG INVLRPEITL ADDGTIASLA VRQEAPALPA
GAKGAVSDDA APPRGVLRPH RIAVGAYDLK DGKLVRTRRV ELDVDGELTQ VEWPAGTPRP
AVLLLNDDDL SYAKVRLDEQ SLAAVRDHVG DFTESLPRAL VWASAWDMTR DGELATRDYL
ELVLHGVGKE TDIGVVQSLH RQVKLALDLY SDPAWRESGL ARWTEAAREH LAAAAPGSDH
QLAWARAFTQ AARTDEQLDI LAGLLDGTVS YEGLAVDTEL RWALLNRLAA TGRADEKAID
AELALDPTSA GEQHAAAARA ARPSAEVKAA AWASVVEDDK LPNAVQESVI DGFVQSDQRE
LLSAYTERYF AAVKGVWDSR SHEMAQQIVI GLYPTYQVSQ ATLDATDAWL ASAEPVPALR
RLVVESRSGV ERALRAQAAD AAAG
//