ID A0A0T2IF01_9MICO Unreviewed; 824 AA.
AC A0A0T2IF01;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASD62_08140 {ECO:0000313|EMBL:KQZ89279.1};
OS Phycicoccus sp. Root563.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736562 {ECO:0000313|EMBL:KQZ89279.1, ECO:0000313|Proteomes:UP000051641};
RN [1] {ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|Proteomes:UP000051641};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ89279.1, ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|EMBL:KQZ89279.1,
RC ECO:0000313|Proteomes:UP000051641};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ89279.1}.
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DR EMBL; LMGM01000001; KQZ89279.1; -; Genomic_DNA.
DR RefSeq; WP_056915525.1; NZ_LMGM01000001.1.
DR AlphaFoldDB; A0A0T2IF01; -.
DR STRING; 1736562.ASD62_08140; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000051641; 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:KQZ89279.1};
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:UP000051641};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 222..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 507..810
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 824 AA; 88821 MW; 3034867A2AA68C82 CRC64;
MPSLTRSEAR ERSALLQVTR MEVDLDLDQG EERFGSSTRI TFSCNDPGAS TFVDVKPAEL
RSMVLNGEPV DVTTLTDGRV TLSGLAADNV LEVEAQMSYS RDGQGLHRAV DPADGEHYVY
GHLFLDAGPR VFACFDQPDL KAPYAVTVAA PEAWTVLGNG AATKVAPGRW ELAETKPLAT
YFVTVCAGPY ASVLDEHDGI PLGIHARASL REALERGAPQ MLEVTRASFD YYHQLFGIRY
PFGEYHQVFV PEFNAGAMEN PGCVTFRDVY VFRGAAARDE ILTRSNTIAH EMAHMWFGDL
VTMQWWDDLW LNESFAEYMS HRTLDAATEF GTEAWVDSTM ARKAWGYAAE RTPSTHPVAG
SAALDAQSAL QDFDGISYAK GAATLRQLIA HIGDDAFIAG VSAYLREHSF GNGTLADFMG
FMERASGKDL GAWTQAWLLT AGVDVISLDR AAGAVDRTVP EAFPADRPHT FDVAGFSAGA
ETFRVPVTTS GDRTVVPELA AAPAGDLVVP NAGDLTWATV TLDPDSIAAV PEQLALVPDP
QARAVVWVSL IDGVCLGTVD PRVMVRTVGA AWPHEDNASI LNRSAGSLLG RIIPTFLPHE
EQGDAEQVVA AAAASVLAAA EPGSTRALVA ARAVARTSAD EELLRAWAAG ERRPVGLEGD
SDFGWIVVRN LASHGLAGRE LIETTRERDD TLQGRLSALM AGASMPDAEA KAWAWGQITT
NRERSNYELN ALAQGFWSSG ELDVLRPYAA RYFSDVPAMS AWVGDDALAR VAQLGFPSRV
VEEATDDMAR AALQRTDLTP AVRRGIVDAR SELGEALRSR ATFG
//
