ID A0A367B137_9ACTN Unreviewed; 853 AA.
AC A0A367B137;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 {ECO:0000313|EMBL:RBY93536.1};
GN ORFNames=DQ237_17215 {ECO:0000313|EMBL:RBY93536.1};
OS Blastococcus sp. TF02-8.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY93536.1, ECO:0000313|Proteomes:UP000252403};
RN [1] {ECO:0000313|EMBL:RBY93536.1, ECO:0000313|Proteomes:UP000252403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-8 {ECO:0000313|EMBL:RBY93536.1,
RC ECO:0000313|Proteomes:UP000252403};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-8.";
RL Submitted (JUL-2018) 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:RBY93536.1}.
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DR EMBL; QOHK01000011; RBY93536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367B137; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000252403; 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:RBY93536.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RBY93536.1};
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:UP000252403};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 528..837
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 853 AA; 94065 MW; 2013B17E1AB2DBF5 CRC64;
MAVPNLTRTD AAARAELLAV QSYDISLDVT DGAGRPGEHT FRSTTTVEFT SRTAGADTFI
DLVAENVLSA TLNGTELDVS TYTEDGGLPL PGLAEKNTLV VTADCRYSNS GEGLHRFLDP
VDGQVYLYTQ FEPADAKRMF TCFDQPDLKA TFTLHVTAPF DWQVISNSGD RTIEAGDGGS
QLAHFAPTKR ISTYLVALIA GPYARVTDLH EGIPLGIYCR ASLAEFLDPE EIFRVTKQGF
DFYHRVFDYP YPFDKYDQLF VPEFNAGAME NAGAVTFLED YVFRSKVSRA RYERRAETIL
HELGHMWFGD LVTMRWWDDL WLNESFATYI STLCQAEATE YTTAWTTFAN TEKAWAQAQD
QLPSTHPIAA DIPDVAAVEV NFDGITYAKG ASVLKQLVAY VGRDEFLAGV RRYFRKHEYG
NTTLADLLGP LSESSGRDLS EWADQWLRTS QVNTLRPVSE LTDDGRYASF AIEQTAVAEH
PVLRNHRLAV GLYSEGPDGL TRTHRVELDV AGARTEVAEL VGHPAADLVL VNDDDLTYAK
LRLDERSLAT LRTRIGAIPD PLARALCWSA AWDMTRDAEL PAREWVQLVL AGIGAETESS
VIQSLLARVQ TALSSFADPT WAPTGWAQLA DHALAALEAA PAGSDQQLLW SRTLATAARS
DEHAAALRGL LDGSRSYEGL TVDADARWAF LHGLVAIGAA GDAEIDAEAE RDATATGIRR
AATARALRPP AESKEETWQR AFTDETIPNA VHEAMLQGFW HHAQRELTAG YVDRYFADIR
PLWDRRPGEI AKNAVQYLFP PVVEPRTIVA ADAWLSDAEQ PPALRRLVFE GRDGIARALR
ARERDADAGH ATA
//
