ID S2Y8N4_9ACTN Unreviewed; 856 AA.
AC S2Y8N4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF1211_05216 {ECO:0000313|EMBL:EPD60466.1};
OS Streptomyces sp. HGB0020.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD60466.1, ECO:0000313|Proteomes:UP000014410};
RN [1] {ECO:0000313|EMBL:EPD60466.1, ECO:0000313|Proteomes:UP000014410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD60466.1,
RC ECO:0000313|Proteomes:UP000014410};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptomyces sp. HGB0020.";
RL Submitted (APR-2013) 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:EPD60466.1}.
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DR EMBL; AGER01000019; EPD60466.1; -; Genomic_DNA.
DR RefSeq; WP_016435129.1; NZ_KE150428.1.
DR AlphaFoldDB; S2Y8N4; -.
DR STRING; 1078086.HMPREF1211_05216; -.
DR MEROPS; M01.009; -.
DR PATRIC; fig|1078086.3.peg.5268; -.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000014410; 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:EPD60466.1};
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:UP000014410};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 107..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 536..845
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 856 AA; 94971 MW; 5C7C667C025A483F CRC64;
MPGTNLTREE AQQRAKLLTV DSYEIDLDLS GAQEGGTYRS VTTVRFDVAE NGAESFIDLV
APTVHEVTLN GDALDAAELF KDSRIALPGL LRGRNVLRVV ADCAYTNTGE GLHRFVDPVD
QQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPPGW TVVSNSPTPE PRDDTWVFEP
TPRISSYITA LIVGPYHSVH SVYEKNGQSV PLGIYCRPSL AEYLDSDAIF EVTRQGFEWF
QEKFDHAYPF AKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDASYE LRAETILHEL
AHMWFGDLVT MEWWNDLWLN ESFATYTSIA CQAHHPDSRW PHSWTTFANS MKTWAYRQDQ
LPSTHPIMAE INDLDDVLVN FDGITYAKGA SVLKQLVAYV GMDAFFSGVQ AYFKRHAFGN
TRLSDLLGAL EETSGRDLKT WSKKWLETAG INVLRPEIET DAEGVITSFA IRQEAPALPA
GAKGEPTLRP HRIAVGLYDL DPDSGKLVRG DRVELDVDGE LTAVPQLTGR SRPAVILLND
DDLSYAKVRL DEASLAVVTE HLGDFEASLP RALCWASAWD MTRDAELATR DYLSLVLSGI
GKESDIGVVQ SLHRQVKLAI DLYADPAARE ALLTRWTDAT LAHLRTAAPG SDHQLAWARA
FTATARTPEQ LDLLESLLDG SQTIEGLAVD TELRWAFVHR LAAVGRWDEA EIAGEYELDR
TAAGERHAAA ARAARPTAEA KAEVWASVVE SDKLPNAVQE AVIGGFVQTD QRELLAPYTE
KYFEVVKDIW ESRSHEIAQQ IAVGLYPAIQ VSQETLERTD AWLASAEPGA ALRRLVSEAR
SGIERALKAQ AADARA
//
