ID A0A166SQ61_9ACTN Unreviewed; 889 AA.
AC A0A166SQ61;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=UG55_100588 {ECO:0000313|EMBL:OAA28576.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA28576.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA28576.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA28576.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA28576.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA28576.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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:OAA28576.1}.
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; LRTK01000005; OAA28576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166SQ61; -.
DR STRING; 683316.UG55_100588; -.
DR PATRIC; fig|683316.3.peg.478; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000077018; 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; 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 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:OAA28576.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAA28576.1};
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:UP000077018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 226..438
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 539..857
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 870..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 95372 MW; E52D5E16BA5B55FF CRC64;
MQPLSQAEAV ARAMLVRVRS YQVDLDLTGT PEGPRFTSTS TVSFTCGEPG ASTFVDLRAI
SVESAQLNGR ELDPGWWQGD RGVLTGLEAV NTLVVRATMA CTNTGEGLHR FTDTEDGEVY
LYAQSFLDDA PRIFACFDQP DLKAPLSLAV AAPESWEVRA NGAGTRVAPG RWEFARTAPL
ATYVVSLVAG PYQVWSRTHD GVPLGLLCRR SLAPHLDDQT AEIFRITTAC LDHYHALFGV
RYPFGKYDQA FVPEFNMGAM ENPGLVVFRD ELVFRSAVTE AERERRAVVI AHEMAHMWFG
DLVTMRWWDD LWLNESFAEY MGTRVTAAVT EHSEAWTSFA VGRKSWGYAA DQRPSTHPVA
PAAVEDTAAA LLNFDGISYA KGASALRQLV EWMGDEAFLA GLRAYFDAHA FGNATLADLL
AALARASGKD LAAWAEAWLR RAGTDTLRPR VRLDGRGAYA AVEVVRTDPA EPPAELPAGL
SEEPPAARPH RIGVGVYDAD PRGGPLRLLR RVQVDLDQVA PGGGAAVPEL VGTRPGRLLL
VNDGDLTFAR VRFAAVDLAR LDVVLADLAD PLARALVWSA AADMTRDAEW PAGDYLRLAA
RALRTERSVA VLEDALGFAA GAVVDRFLPG SDRPVARGAL VSACQVVIDG AAPGREPAAG
ADGSGLLLAA ARGLIACAAP PEVGRLRGWL QGRGVPPGLV VDPDLRWRLL DRLVVLGAAG
EREIAAELGR DRSTRGAELA ARIRAAAGDP AAKSRAWKVI TADLETSARL VAATAQGFWQ
PEQQDLTDPY VDRYFAEMPR LARTRSPHAL RQIAAAAFPR YAVRAETLAA ARHLLGAAAT
GPVLARVVVD AADDLRRAVA ARELHRHAYP AGWPGPEAAG GPAGQPVSG
//
