ID A0A286EPI8_9ACTN Unreviewed; 859 AA.
AC A0A286EPI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05892883_2174 {ECO:0000313|EMBL:SOD72847.1};
OS Jatrophihabitans sp. GAS493.
OC Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC Jatrophihabitantaceae; Jatrophihabitans.
OX NCBI_TaxID=1907575 {ECO:0000313|EMBL:SOD72847.1, ECO:0000313|Proteomes:UP000218903};
RN [1] {ECO:0000313|EMBL:SOD72847.1, ECO:0000313|Proteomes:UP000218903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS493 {ECO:0000313|EMBL:SOD72847.1,
RC ECO:0000313|Proteomes:UP000218903};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; LT907982; SOD72847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286EPI8; -.
DR InParanoid; A0A286EPI8; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000218903; Chromosome i.
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:SOD72847.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 533..844
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 859 AA; 94129 MW; B91DBA3BC9F8EE9F CRC64;
MAVPNLTRDD ARVRAALLEV ESYDIDLDLT DGQGNPSEIT FRARTTLRFS AQTSGRSTFL
DVVAQSIESA TLNGEPVDVS GYDPENGIVL ENLALENTVV IESTMLYTNT GEGMHRFVDP
VDSEVYLYTQ FEASDAKRVY ACFDQPDLKA TFTFHVTAPQ SWEVISNSPV TATTDDGSQK
TVHFGTTVRI SPYITAIVAG PYYHVHDTHD GIELGLYCRK GFAEYLEPEE NFATTKQGFD
WYHANFGVRY PFGKYDQLFV PEFNAGAMEN AGCVTFNEIY LFRGKVTEAR RERRGSTILH
EMAHMWFGDL VTMRWFDDLW LNESFATYAS ALSQANGTRW TDAWTTFANV EKTWAYRQDQ
LPSTHPIAAD APDVQTAETN FDGITYAKGA SVLKQLAAYV GVEDFLAALR EYFTEHAYAN
TTLADLLRAL EKTSGRDLGT WSTSWLETTG INTIRPEFTL DSAGHYASFE LVQQAPTEVA
TTNVVRPHRL AIGLYNHDPA TSTLVRTGRV ELDLDAARTT VEELVGVSQP DLLMVNDDDL
TYCKARLDER SVKTLRTGGI AELAESLPRA LAWSSVWDMT RDAEVPARDY IALVVAGAAA
ETNIGLLQSI TRQALRALEI YADPSWAPAG YQALAEESLR ALNASEPGSD HQLAWVHAFL
GSARSAEHAE IIKQLSTGAY VVEGLAIDNE LRWSIVQALA SRGLIDADGI SAELERDPSD
AGHRHADTAR ALIPTAEAKA AAWKIAVEDA GISNFVQKAA VAGFGTSIHS ELLTGYVEKY
FDVIADVWSS RSGELAQTAV VGLFPLWSST ATEATLATAD AFLARTDLPA ALRRLVSEGQ
ADIVRALAAR KTDTEAGTA
//
