ID A0A1Q4UZN7_9ACTN Unreviewed; 855 AA.
AC A0A1Q4UZN7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=AB852_31805 {ECO:0000313|EMBL:OKH91067.1};
OS Streptomyces uncialis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH91067.1, ECO:0000313|Proteomes:UP000186455};
RN [1] {ECO:0000313|EMBL:OKH91067.1, ECO:0000313|Proteomes:UP000186455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCA2648 {ECO:0000313|EMBL:OKH91067.1,
RC ECO:0000313|Proteomes:UP000186455};
RA Yan X., Huang T., Ge H., Shen B.;
RT "Cloning and characterization of the uncialamcin biosynthetic gene
RT cluster.";
RL Submitted (JUN-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:OKH91067.1}.
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; LFBV01000010; OKH91067.1; -; Genomic_DNA.
DR RefSeq; WP_073793743.1; NZ_LFBV01000010.1.
DR AlphaFoldDB; A0A1Q4UZN7; -.
DR STRING; 1048205.AB852_31805; -.
DR Proteomes; UP000186455; 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:OKH91067.1};
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:UP000186455};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 535..844
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 855 AA; 93925 MW; E0E79AAF8ADACD5A CRC64;
MPGTNLTREE AQRRAALLTV DSYGIDLDLG GAQEGGTYRS VTTVRFDSAE ADAETFIDLV
APEVHEVVLN GTALDPAAVF ADSRITLPGL LAGRNELRVV ADCAYTNTGE GLHRFVDPVD
QQAYLYTQFE VPDARRVFAS FEQPDLKAAF QFTVKAPAGW TVISNSPTPE PKDDVWVFEP
TPRISTYITA LIVGPYHAVH SVYEKDGQSV PLGIYCRPSL AEFLDADAIF DVTRQGFEWF
QEKFDYAYPF AKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAETILHEL
AHMWFGDLVT MEWWNDLWLN ESFATYTSIA CQAYAPGSRW PHSWTTFANS MKTWAYRQDQ
LPSTHPIMAE ISDLDDVIVN FDGITYAKGA SVLKQLVAYV GMDEFFKGVQ KYFKAHAYGN
TRLSDLLGAL EETSGRDLKN WSKLWLETAG INILRPEIET GADGVITSFA VRQEAPALPA
GAKGEPTLRP HRIAVGFYDL DGAGKLVRGE RVELDVDGEL TDVPQLVGKA RPAVVLLNDD
DLSYAKVRLD EASLAFVTEH LGDFAESLPR ALSWASAWDM TRDAELPARE YLELVLSGIA
KESDIGVVQS LQRQVKLALD LYAAPSWREA GLTRWTDATL AHLRAAEAGG DHQLAWARAF
AATARTPEQL DLLEALLDGT RTIEGLAVDT ELRWALVQRL AAVGRFDEAE ISAEYERDRT
AAGERHAAAA RAARPTAEAK AEAWASVVES DQLPNAVQEA VIAGFVQTDQ RELLAPYTEK
YFAAVKGVWE SRSHEMAQQV VVGLYPVLQV SSGTVEATDA WVAAAGPGAS LLRLVSEAKS
GVERALRAQS ADASA
//
