ID I0R0W9_9MICO Unreviewed; 856 AA.
AC I0R0W9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=IMCC13023_10580 {ECO:0000313|EMBL:EIC91505.1};
OS Candidatus Aquiluna sp. IMCC13023.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Aquiluna.
OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91505.1, ECO:0000313|Proteomes:UP000054510};
RN [1] {ECO:0000313|Proteomes:UP000054510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX PubMed=22689238; DOI=10.1128/JB.00586-12;
RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT member of the Actinobacteria isolated from an arctic fjord.";
RL J. Bacteriol. 194:3550-3551(2012).
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:EIC91505.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJKR01000003; EIC91505.1; -; Genomic_DNA.
DR AlphaFoldDB; I0R0W9; -.
DR STRING; 1081644.IMCC13023_10580; -.
DR MEROPS; M01.009; -.
DR PATRIC; fig|1081644.3.peg.1068; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000054510; 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:EIC91505.1};
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:UP000054510};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 27..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 532..844
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 856 AA; 95955 MW; DA940184C890FE41 CRC64;
MEKKMPGENL TRQEAQARSA IIDVDSYIVE VNLTQDPKVF SYVSTVRFAC SEEGQETFID
AITTSVESIE LNGLDLDPSE YSDGTRITLP NLKSENVLTV KANGVFSNSG EGLHRFVDPV
DNEVYFYTQF EVPDSRRMFA VFEQPDLKAS FEFKVIGNQD WQMISNSTTP KPVLIGDGLA
RWDFAPTPRI SSYITALVAG PYTVWRDELT SSNGQIVPLG VFCRSSLATF MDPEYIFDKT
KAGFTYFENL FDYPYPFEKY DQLWVPDFNA GAMENAGAVT FTESYIFRSA VTDAVKERRV
VTILHELAHM WFGDLVTMVW WNDLWLNESF AEYVSTLATA EATEWTEAWT TFASLEKSWA
YRQDQLPSTH PIVAEIADLE DVQVNFDGIT YAKGASVLKQ LVAWVGQDSF MRGVGNYFKK
HQWKNTELRD LLVELEAESG RDLKEWSSLW LETAGVNTLR PEIEVDEDGR FTKFDIIQTA
IADYPYLRPH RLGVGMFQLV GGRLERNGEI EIDVAGPITS VSQLLGEVKP DLILINDKDL
AYAKIRLDDG SWAVALENLS GISDSLARTM IWSAAWDTTR DAEAKPRDFI QLVLDHIASE
TESTTVTTLL RQLVTTATLY VAEDRRTETI EHIAQSLIEL AETAEAGSDN QLQFAKFVAQ
FATTDKQLDW LDALVSGQKA LTGLTVNGDL RWEILLGLAV GNRADQDRIA TELAHDNTAN
GKKFAAAALA AISTPVAKLE AWVELTERTE YSNTLISSAS ASFGRVSDIT LLEIYADKYM
SIAQKIWEER SYQIASYLLT NLYPIALANK SLAEKTQKLI DSSFAQSKPA FRRTLVENLA
GLERGIKAQA KDQEEN
//
