ID A0A2N3XVW5_SACSN Unreviewed; 857 AA.
AC A0A2N3XVW5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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=A8926_2467 {ECO:0000313|EMBL:PKW14817.1};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW14817.1, ECO:0000313|Proteomes:UP000233786};
RN [1] {ECO:0000313|EMBL:PKW14817.1, ECO:0000313|Proteomes:UP000233786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW14817.1,
RC ECO:0000313|Proteomes:UP000233786};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-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}.
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:PKW14817.1}.
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DR EMBL; PJNB01000001; PKW14817.1; -; Genomic_DNA.
DR RefSeq; WP_010695881.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; A0A2N3XVW5; -.
DR STRING; 994479.GCA_000194155_02976; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000233786; 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:PKW14817.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 107..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 239..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 533..846
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 857 AA; 95281 MW; 6B272966B80E03BC CRC64;
MAPPNLTRDQ AEQRAALLEV QSYVIELDLS AGAGGPDVET FGSTTTVRFR SNEASADSWI
DLVADRVHSA VLNGVELDVS DYDESTGIRL PNLAADNELV VRADCAYTNT GEGLHRFIDP
VDGGVYLYSQ FETADAKRMF TCFDQPDLKA TYQITVDAPE SWKVISNATA EVTDSANGKR
HEFATTKPMS TYLVALVAGP YAEWRDVFPG EDGQDEIPLG IYCRASLAEH LDAERLFTET
KQGFGFYHKA FGVPYPFGKY DQCFVPEFNA GAMENAGCVT FLEDYVFRSK VTGYLYERRC
ETVLHEMAHM WFGDLVTMRW WDDLWLNESF ATWASVLAQV GATQYGHAWT TFASVEKSWA
YRQDQLPSTH PVAADIQDLQ AVEVNFDGIT YAKGASVLKQ LVAYVGLDNF LAGLRIYFNR
HAWGNATLND LLRALEEASG RDLSWWSAQW LETTGLNMLR PRFATDDEGR FTSFEVVQNG
ARPGAGELRT HRLAIGIYDD EGGKLVRKHR VELDVTGERT EVPDLVGVHR GKLVLVNDDD
LTYCSLRFDP ESLAALIDRI GDIDESLPRA LCWSTAWEMT REAELKARDF VTLVLGASAE
GGIGAESEIG VVQRVLLQTQ TALASYVDPS WQPEGWRRFT GRLFELARAA EPGSDHQLAF
VNSLAGSVFS ADQVAELRGW LDGSAPLAGL TVDTDLRWQL LQALVAHGAA GESEIDAELE
KDQTATGRRR AERARALIPT PESKEKAWQR AVHDDQLPNA VSDSIIAGFQ HPAQRELLAP
YVRRYFEEID EVWQRRSSER AQPTVIGLFP SWAVTDDTVA ESDAWLANEH PSALRRLVSE
GRAGIVRALA AREFDRS
//
