ID A0A2P4URT4_9ACTN Unreviewed; 844 AA.
AC A0A2P4URT4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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_4 {ECO:0000313|EMBL:POM27746.1};
GN ORFNames=BTM25_21650 {ECO:0000313|EMBL:POM27746.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM27746.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM27746.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM27746.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM27746.1}.
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DR EMBL; MTBP01000001; POM27746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4URT4; -.
DR Proteomes; UP000242367; 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:POM27746.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:POM27746.1};
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:UP000242367};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 93..185
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 229..441
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 523..832
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 844 AA; 93017 MW; B6C734D983324292 CRC64;
MAGNLTRDEA RERARSLTVE SYAVELDLTT GEERFGSTTV IRFACADEGA DSFVDLHDAV
VREATLNGRP IDPARYDAAK GRLPLDGLAA SNELRVAADV LYSRSGEGLH RFVDPVDGSV
YLYTQFETAD AHRMYTCFDQ PDLKATFELT VRAPQDWQVV TNEAADSASG GVWHFPPTPK
VSTYITALVA GPYHVVTDEY RRPDGTAIPL GVFCRASLAE HLDADAIIDV TKQGFAFFEK
VFDRPYPFAK YDQLFVPEFN AGAMENAGCV TFLEDYVFRS RVTDAAYERR AETILHEMAH
MWFGDLVTMR WWDDLWLNES FATYMSVLCQ AEATKWTGSW TTFANVEKAW AYRQDQLPST
HPISADIPDI RAVEVNFDGI TYAKGASVLK QLVAYVGRDN FLEGVRRYFQ RHAWGNTVLA
DLLDALEETS GRDLASWSKE WLETAGANTL RPSYEVDGDG NFTSFAVLQE AKADYPTLRS
HRVAIGLYDR TADGLVRRDR VELDVVGART DVPELIGTAR PDLVLVNDDD LTYAKIRLDD
HSLRTLVAGI GDIRDGLPRA LCWSAAWDMT RDAEMATRDY IKLVISGIRG VTDMTVLQTL
LRQARTAVQQ YAAPEWRPEG LRLLADALYD LSREAAPGSD FQLAYLQAFA GVATSDEHLA
WIAALLDGSS VLDGLTVDTD LRWTLLRRLV ATGRAGAAAI DAEAARDATA AGERQAAGAR
AQIPTAEAKA AAWAAITGGE LPNAVFRATI GGFVDAEGAA LLEPYVERYF AEVGRVWTSW
TSDMSQTFAE VAYPFLVIDQ ATLDRTDAYI AAENPPSALR RLLSEGRDGV ARALRARARD
AAAS
//
