ID A0A2S3ZXD5_ARTGL Unreviewed; 849 AA.
AC A0A2S3ZXD5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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 {ECO:0000313|EMBL:POH73602.1};
GN ORFNames=CVS27_09515 {ECO:0000313|EMBL:POH73602.1};
OS Arthrobacter glacialis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1664 {ECO:0000313|EMBL:POH73602.1, ECO:0000313|Proteomes:UP000237061};
RN [1] {ECO:0000313|EMBL:POH73602.1, ECO:0000313|Proteomes:UP000237061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLT2-12-2 {ECO:0000313|EMBL:POH73602.1,
RC ECO:0000313|Proteomes:UP000237061};
RA Liu Q., Xin Y.-H.;
RT "Arthrobacter sp. nov., from glaciers in China.";
RL Submitted (JAN-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:POH73602.1}.
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DR EMBL; PPXC01000006; POH73602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S3ZXD5; -.
DR Proteomes; UP000237061; 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:POH73602.1};
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:UP000237061};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 18..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 229..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 529..839
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 849 AA; 92493 MW; 3A1188486FB3FC0E CRC64;
MNLTRAEAIE RSATLTVKSY DVTLDLTTSD TIFASTTTVE FSAKEGSASF IDAVTAAVHQ
VTLNGVELDP AQVSDGVRIQ LPNLAAENVL TVKADALYMN TGEGLHRFVD PVDGEVYLYS
QFEVPDSRRM FAVFEQPDQK AAFTFHVTTP AHWDVISNSP TPAPESAGEG KSSWHFEPTL
TMSSYITALI AGPYASVRSE LTSSDGRIIP LGVFARKSLM EFMDAENVFE LTRQGFEFFE
KQFGTPYPFP KYDQLFVPEF NAGAMENAGA VTFLESYVFR SKVTDAMVER RAITILHELA
HMWFGDLVTM RWWNDLWLNE SFAEFMSTLA AAENTKYVDA WTTFSSLEKS WAYRQDQLPS
THPIKAEIND LEDVLVNFDG ITYAKGASVL RQLVAWVGQE EFMAGVRAYF GKHAWSNTEL
PDLMVELEAA SGRDLSAWTE KWLETAGVNT FKPALEVTDD GVITSFAILQ SAIAEHPTLR
PHRTAVGFYN LATDGEDTGK LVRTHRVELD VDGAVTSVPE LVGMKRPALI LLNDDDLAYA
KIRLDAASLT TAKTHLQDFK ESLPRTLVSA SVWDATRDGE TPAREYVEFV LATIGLESDS
TVIMVLLRQL ATALSLYVAP GHQKATAVAA ADSLWALAQS AGAGSDAQLQ FVKAFAAHAQ
SGEQLDLVQS LLDGDQELDS LTLDTDMRWE FLTSLAAGGR APGAVIDAAL ALDNTQTGQL
AAATAHAAIP TAEAKAATWE SVVVQGDAAN SIQRAAIGGF TKVWDTALLE PYVAAYFASI
ERVWAEKSYE ISSTIITGLY PSQLVQESTV AATDAFLAAL GDSTPALRRL LVESRDGVVR
ALKAQAADH
//
