ID A0A2I2KSZ9_9ACTN Unreviewed; 844 AA.
AC A0A2I2KSZ9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=pepN {ECO:0000313|EMBL:SNQ48782.1};
GN ORFNames=FRACA_280004 {ECO:0000313|EMBL:SNQ48782.1};
OS Frankia canadensis.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ48782.1, ECO:0000313|Proteomes:UP000234331};
RN [1] {ECO:0000313|EMBL:SNQ48782.1, ECO:0000313|Proteomes:UP000234331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ48782.1};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZMO01000201; SNQ48782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2KSZ9; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000234331; 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:SNQ48782.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SNQ48782.1};
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:UP000234331};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 105..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 529..838
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 844 AA; 91737 MW; D18281F09F38D25B CRC64;
MHTLTRDEAV TRASLLRVDG YDIELDLTAA RTSTEFTSTT RVRFSLREPA APGASTFAEL
KPAAVSDLRL NGRPLDPASL DGNRLPLTDL EASNELVATT TMRYSNTGEG LHRFTDPEDG
EVYLYAQTFL DDAQRIFACF DQPDLKAPVR LTVQAPAGWV VRANGAGRRT APGRFAFAET
PPLATYFVTV VAGPYHVIED SHDGIPLGLL CRRSLAPHLT ADAAEIFEVT KACLDRYHEL
FADRYPFGTY DQAFVPEFNA GAMENPGCVT FRDEFVYRSA VTDTERELRA VVIAHEMAHM
WFGDLVTMRW WDDLWLNESF AEYMGYRITA EATRFTSAWT SFAVGRKSWG YAADQRPSTH
PVAPAEVADT ALALLNFDGI SYAKGASVLR QLVAWVGEDA FRTGLRAYFA AHAYANASLA
DLLAALSEAS GRDLAGWAEL WLRREQVNTL RPHVTLGADG RFAQVTLEQT APADHPTLRP
HRVAVGVYGP DGAGPIVQLR RVEVDVDPAA PDGRTDLPAL VGTPAGRLLL VNDGDLTYAK
VRFTPNDLAA LPDVLPRIAD PLARAVIWAA AADATRDADW PAADYLTLAT TALPHESQLA
ILEDALRFAR TTALTRYLAP EGRRGAAARL HAMCRAVLTQ ADPGSGRQLS AARGAIGCAG
PAEAPILAAW LAGDDVPAGL VVDPELRWTL LHRLVVLGRA GEAEITAEGQ RDRSARAAEH
AARARAALAD PAAKARAWEM IVADDVASAR LVAASAEGFW QPEQDELTAD YVDRYFEQMP
AMTSRRSPHA ARQIATAAYP QYAVSSATLA AARALLDRDD VDPLLRRVIV DATDELRRAV
RARG
//
