ID A0A1I1FVB4_9ACTN Unreviewed; 805 AA.
AC A0A1I1FVB4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN04487968_10366 {ECO:0000313|EMBL:SFC00930.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFC00930.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFC00930.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFC00930.1,
RC ECO:0000313|Proteomes:UP000198832};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLB01000003; SFC00930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1FVB4; -.
DR STRING; 574651.SAMN04487968_10366; -.
DR OrthoDB; 3885507at2; -.
DR Proteomes; UP000198832; 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; 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 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:SFC00930.1};
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:UP000198832};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 228..442
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 506..799
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 805 AA; 87080 MW; F7AC26E5C8D30392 CRC64;
MPSLTLIEAR ARAQQISEVS YEVELDLTDA DGPTFGSRTV TRFRSTTEST FLELTSAREL
TVHVDGSLVE PAYDGHRIQL RLDPSEALHE VVVDARLPYT TDGEGMHRAV DAADGETYLG
AYLGLDIAQR VYACFDQNDL KAPITTSVAA DPRWTVLANG RAVADGAANG DGRWTFEATP
PIPPALFTVA AGPWRSVRWQ HAGLPFGWHA RASLGVELDR DAAELRSVTE RCFDHYAGLF
DEPYPFDSYD QVLVPGLNWG AQEMPGCVLF RDELLPRGRV PAETRVLRAS IIAHEMAHMW
FGDSMTMTWW EDTWLQESFA DYMGYRVAAG AAGFPGAQVT HEIMQKPAAY LADERRSTHP
VAPATEDVPD VDSAATIFDA ISYAKGNSVL RQLATWLGDE AFLRGVNDHL TRHRFANASL
ADLVDALADA TDRDVRAWVD LWLRRSGFDT LRVERVDGVP VLHRDGSRPH RVTVTAYDDD
LTEVARLLVD VADEPIPLPQ LAGRVIVPNA AGETFARIVL DGRSRAAVAA GLSGIGDVVA
RAVLWTMVLD EVGTRALPVD GLVDLVERHL PVEPDPTVVT AIVEHSLRLV LLRAGAGDVA
GLVERVAEAC AAGLAAAPAP DVAAAFARGV VVGSMDADLL LGWLDADEVA GQPMTPALRW
RAVQRLAELG AVDADGIEAE RRLSPGLEAD IGVAAALAAR PTAEAKSAAW RVAAVADVGN
RIFDATFRGL WAAGPGDLLA PYVERYLREA PGWAARGQGF AQVVGRARPP FALTPAQLAM
LDEACAGELP TVLRRQWEDW RDDLG
//
